|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5239 |
| Enzyme 1 Name |
ATP-citrate synthase |
| Enzyme 1 Synonyms |
- ATP-citrate
- pro-S--lyase
- Citrate cleavage enzyme
|
| Enzyme 1 Gene Name |
ACLY |
| Enzyme 1 Protein Sequence |
>ATP-citrate synthase
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
|
| Enzyme 1 Number of Residues |
1101 |
| Enzyme 1 Molecular Weight |
120841 |
| Enzyme 1 Theoretical pI |
7.34 |
| Enzyme 1 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Energy production and conversion |
| Enzyme 1 Specific Function |
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
28935  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P53396  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ACLY_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>3318 bp
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA
|
| Enzyme 1 GenBank Gene ID |
X64330  |
| Enzyme 1 GeneCard ID |
ACLY  |
| Enzyme 1 GenAtlas ID |
ACLY  |
| Enzyme 1 HGNC ID |
HGNC:115  |
| Enzyme 1 Chromosome Location |
17 |
| Enzyme 1 Locus |
17q12-q21 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5242 |
| Enzyme 2 Name |
Acetyl-CoA acetyltransferase, cytosolic |
| Enzyme 2 Synonyms |
- Cytosolic acetoacetyl-CoA thiolase
- Acetyl CoA transferase-like protein
|
| Enzyme 2 Gene Name |
ACAT2 |
| Enzyme 2 Protein Sequence |
>Acetyl-CoA acetyltransferase, cytosolic
MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHV
LAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGME
NMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDK
VAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT
DGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPA
IKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGC
RILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE
|
| Enzyme 2 Number of Residues |
397 |
| Enzyme 2 Molecular Weight |
41351 |
| Enzyme 2 Theoretical pI |
6.92 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
2 acetyl-CoA = CoA + acetoacetyl-CoA |
| Enzyme 2 Pathways |
- Benzoate Degradation via CoA Ligation (map00632
)
- Butyrate Metabolism (map00650
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Lysine Degradation (map00310
)
- Propanoate Metabolism (map00640
)
- Pyruvate Metabolism (map00620
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Tryptophan Metabolism (map00380
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 2 Reactions |
- 2 acetyl-CoA = CoA + acetoacetyl-CoA
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
546901  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BWD1  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
THIC_HUMAN  |
| Enzyme 2 PDB ID |
1WL5  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1194 bp
ATGAATGCAGGCTCAGATCCTGTGGTCATCGTCTCGGCGGCGCGGACCATCATAGGTTCC
TTCAATGGTGCCTTAGCTGCTGTTCCTGTCCAGGACCTGGGCTCCACTGTCATCAAAGAA
GTCTTGAAGAGGGCCACTGTGGCTCCGGAAGATGTGTCTGAGGTCATCTTTGGACATGTC
TTGGCAGCAGGCTGTGGGCAGAATCCTGTTAGACAAGCCAGTGTGGGTGCAGGAATTCCC
TACTCTGTTCCAGCATGGAGCTGCCAGATGATCTGTGGGTCAGGCCTAAAAGCTGTGTGC
CTTGCAGTCCAGTCAATAGGGATAGGAGACTCCAGCATTGTGGTTGCAGGAGGCATGGAA
AATATGAGCAAGGCTCCTCACTTGGCTTACTTGAGAACAGGAGTAAAGATAGGTGAGATG
CCACTGACTGACAGTATACTCTGTGATGGTCTTACAGATGCATTTCACAACTGTCATATG
GGTATTACAGCTGAAAATGTAGCCACAAAATGGCAAGTGAGTAGAGAAGATCAGGACAAG
GTTGCAGTTCTGTCCCAGAACAGGACAGAGAATGCACAGAAAGCTGGCCATTTTGACAAA
GAGATTGTACCAGTTTTGGTGTCAACTAGAAAAGGTCTTATTGAAGTTAAAACAGATGAG
TTTCCTCGCCATGGGAGCAACATAGAAGCCATGTCCAAGCTAAAGCCTTACTTTCTTACT
GATGGAACGGGAACAGTCACCCCAGCCAATGCTTCAGGAATAAATGATGGTGCTGCAGCT
GTTGCTCTTATGAAGAAGTCAGAAGCTGATAAACGTGGGCTTACACCTTTAGCACGGATA
GTTTCCTGGTCCCAAGTGGGTGTGGAGCCTTCCATTATGGGAATAGGACCAATTCCAGCC
ATAAAGCAAGCTGTTACAAAAGCAGGTTGGTCACTGGAAGATGTTGACATATTTGAAATC
AATGAAGCCTTTGCAGCTGTCTCTGCTGCAATAGTTAAAGAACTTGGATTAAACCCAGAG
AAGGTCAATATTGAAGGAGGGGCTATAGCCTTGGGCCACCCTCTTGGAGCATCTGGCTGT
CGAATTCTTGTGACCCTGTTACACACACTGGAGAGAATGGGCAGAAGTCGTGGTGTTGCA
GCCCTGTGCATTGGGGGTGGGATGGGAATAGCAATGTGTGTTCAGAGAGAATGA
|
| Enzyme 2 GenBank Gene ID |
S70154  |
| Enzyme 2 GeneCard ID |
ACAT2  |
| Enzyme 2 GenAtlas ID |
ACAT2  |
| Enzyme 2 HGNC ID |
HGNC:94  |
| Enzyme 2 Chromosome Location |
6 |
| Enzyme 2 Locus |
6q25.3-q26 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Song XQ, Fukao T, Yamaguchi S, Miyazawa S, Hashimoto T, Orii T: Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem Biophys Res Commun. 1994 May 30;201(1):478-85. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5244 |
| Enzyme 3 Name |
Diamine acetyltransferase 2 |
| Enzyme 3 Synonyms |
- Spermidine/spermine N(1- acetyltransferase 2
- Polyamine N-acetyltransferase 2
|
| Enzyme 3 Gene Name |
SAT2 |
| Enzyme 3 Protein Sequence |
>Diamine acetyltransferase 2
MASVRIREAKEGDCGDILRLIRELAEFEKLSDQVKISEEALRADGFGDNPFYHCLVAEIL
PAPGKLLGPCVVGYGIYYFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDK
GCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQGEATRKLAGK
|
| Enzyme 3 Number of Residues |
170 |
| Enzyme 3 Molecular Weight |
19155 |
| Enzyme 3 Theoretical pI |
5.84 |
| Enzyme 3 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Transcription |
| Enzyme 3 Specific Function |
Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine |
| Enzyme 3 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 3 Reactions |
- acetyl-CoA + an alkane-alpha,omega -diamine = CoA + an N-acetyldiamine
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
19070527  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q96F10  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SAT2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>513 bp
ATGGCTTCCGTGCGGATCCGAGAGGCCAAGGAGGGAGACTGTGGAGATATCCTGAGGCTG
ATTCGGGAGCTAGCCGAATTCGAAAAACTCTCGGATCAGGTGAAGATCAGTGAAGAAGCC
CTGAGAGCAGATGGCTTTGGAGACAATCCTTTCTATCACTGTTTGGTAGCAGAGATTCTT
CCAGCGCCCGGGAAGCTACTGGGGCCCTGCGTGGTGGGCTATGGGATATACTATTTCATC
TACAGTACATGGAAGGGACGCACCATTTATCTGGAGGATATCTATGTGATGCCAGAATAT
CGGGGTCAAGGGATTGGTTCCAAAATAATCAAAAAGGTGGCTGAGGTGGCCTTGGATAAG
GGCTGCTCCCAATTCCGCCTGGCCGTCCTGGACTGGAACCAGAGGGCCATGGACTTGTAC
AAGGCCCTAGGAGCCCAAGATCTGACGGAAGCTGAGGGCTGGCACTTCTTCTGCTTTCAA
GGAGAGGCAACGAGAAAGTTGGCAGGAAAGTGA
|
| Enzyme 3 GenBank Gene ID |
AF348524  |
| Enzyme 3 GeneCard ID |
SAT2  |
| Enzyme 3 GenAtlas ID |
SAT2  |
| Enzyme 3 HGNC ID |
HGNC:23160  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17p13.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Chen Y, Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase. Biochem J. 2003 Aug 1;373(Pt 3):661-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5249 |
| Enzyme 4 Name |
Arylamine N-acetyltransferase 1 |
| Enzyme 4 Synonyms |
- Arylamide acetylase 1
- Monomorphic arylamine N-acetyltransferase
- MNAT
- N- acetyltransferase type 1
- NAT-1
|
| Enzyme 4 Gene Name |
NAT1 |
| Enzyme 4 Protein Sequence |
>Arylamine N-acetyltransferase 1
MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVV
RRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYI
VDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDL
LEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLT
HRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI
|
| Enzyme 4 Number of Residues |
290 |
| Enzyme 4 Molecular Weight |
33899 |
| Enzyme 4 Theoretical pI |
6.51 |
| Enzyme 4 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- arylamine N-acetyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 4 Specific Function |
Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
34994  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P18440  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ARY1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>873 bp
ATGGACATTGAAGCATATCTTGAAAGAATTGGCTATAAGAAGTCTAGGAACAAATTGGAC
TTGGAAACATTAACTGACATTCTTCAACACCAGATCCGAGCTGTTCCCTTTGAGAACCTT
AACATCCATTGTGGGGATGCCATGGACTTAGGCTTAGAGGCCATTTTTGATCAAGTTGTG
AGAAGAAATCGGGGTGGATGGTGTCTCCAGGTCAATCATCTTCTGTACTGGGCTCTGACC
ACTATTGGTTTTGAGACCACGATGTTGGGAGGGTATGTTTACAGCACTCCAGCCAAAAAA
TACAGCACTGGCATGATTCACCTTCTCCTGCAGGTGACCATTGATGGCAGGAACTACATT
GTCGATGCTGGGTTTGGACGCTCATACCAGATGTGGCAGCCTCTGGAGTTAATTTCTGGG
AAGGATCAGCCTCAGGTGCCTTGTGTCTTCCGTTTGACGGAAGAGAATGGATTCTGGTAT
CTAGACCAAATCAGAAGGGAACAGTACATTCCAAATGAAGAATTTCTTCATTCTGATCTC
CTAGAAGACAGCAAATACCGAAAAATCTACTCCTTTACTCTTAAGCCTCGAACAATTGAA
GATTTTGAGTCTATGAATACATACCTGCAGACATCTCCATCATCTGTGTTTACTAGTAAA
TCATTTTGTTCCTTGCAGACCCCAGATGGGGTTCACTGTTTGGTGGGCTTCACCCTCACC
CATAGGAGATTCAATTATAAGGACAATACAGATCTAATAGAGTTCAAGACTCTGAGTGAG
GAAGAAATAGAAAAAGTGCTGAAAAATATATTTAATATTTCCTTGCAGAGAAAGCTTGTG
CCCAAACATGGTGATAGATTTTTTACTATTTAG
|
| Enzyme 4 GenBank Gene ID |
X17059  |
| Enzyme 4 GeneCard ID |
NAT1  |
| Enzyme 4 GenAtlas ID |
NAT1  |
| Enzyme 4 HGNC ID |
HGNC:7645  |
| Enzyme 4 Chromosome Location |
8 |
| Enzyme 4 Locus |
8p23.1-p21.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Blum M, Grant DM, McBride W, Heim M, Meyer UA: Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression. DNA Cell Biol. 1990 Apr;9(3):193-203. [PubMed
]
- Ohsako S, Deguchi T: Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver. J Biol Chem. 1990 Mar 15;265(8):4630-4. [PubMed
]
- Vatsis KP, Weber WW: Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus. Arch Biochem Biophys. 1993 Feb 15;301(1):71-6. [PubMed
]
- Doll MA, Jiang W, Deitz AC, Rustan TD, Hein DW: Identification of a novel allele at the human NAT1 acetyltransferase locus. Biochem Biophys Res Commun. 1997 Apr 28;233(3):584-91. [PubMed
]
- Butcher NJ, Ilett KF, Minchin RF: Functional polymorphism of the human arylamine N-acetyltransferase type 1 gene caused by C190T and G560A mutations. Pharmacogenetics. 1998 Feb;8(1):67-72. [PubMed
]
- Lo-Guidice JM, Allorge D, Chevalier D, Debuysere H, Fazio F, Lafitte LJ, Broly F: Molecular analysis of the N-acetyltransferase 1 gene (NAT1*) using polymerase chain reaction-restriction fragment-single strand conformation polymorphism assay. Pharmacogenetics. 2000 Jun;10(4):293-300. [PubMed
]
- Ebisawa T, Deguchi T: Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1252-7. [PubMed
]
- Delomenie C, Goodfellow GH, Krishnamoorthy R, Grant DM, Dupret JM: Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis. Biochem J. 1997 Apr 1;323 ( Pt 1):207-15. [PubMed
]
- Hughes NC, Janezic SA, McQueen KL, Jewett MA, Castranio T, Bell DA, Grant DM: Identification and characterization of variant alleles of human acetyltransferase NAT1 with defective function using p-aminosalicylate as an in-vivo and in-vitro probe. Pharmacogenetics. 1998 Feb;8(1):55-66. [PubMed
]
- Lin HJ, Probst-Hensch NM, Hughes NC, Sakamoto GT, Louie AD, Kau IH, Lin BK, Lee DB, Lin J, Frankl HD, Lee ER, Hardy S, Grant DM, Haile RW: Variants of N-acetyltransferase NAT1 and a case-control study of colorectal adenomas. Pharmacogenetics. 1998 Jun;8(3):269-81. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5251 |
| Enzyme 5 Name |
5-aminolevulinate synthase, nonspecific, mitochondrial precursor |
| Enzyme 5 Synonyms |
- 5-aminolevulinic acid synthase
- Delta-aminolevulinate synthase
- Delta-ALA synthetase
- ALAS-H
|
| Enzyme 5 Gene Name |
ALAS1 |
| Enzyme 5 Protein Sequence |
>5-aminolevulinate synthase, nonspecific, mitochondrial precursor
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
|
| Enzyme 5 Number of Residues |
640 |
| Enzyme 5 Molecular Weight |
70582 |
| Enzyme 5 Theoretical pI |
8.57 |
| Enzyme 5 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthesis
- cellular metabolism
- heme biosynthesis
- heterocycle metabolism
- metabolism
- physiological process
- porphyrin biosynthesis
- porphyrin metabolism
|
| Component |
| — |
|
| Enzyme 5 General Function |
Coenzyme transport and metabolism |
| Enzyme 5 Specific Function |
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2) |
| Enzyme 5 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 5 Reactions |
- succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
28583  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P13196  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
HEM1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1923 bp
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
|
| Enzyme 5 GenBank Gene ID |
X56351  |
| Enzyme 5 GeneCard ID |
ALAS1  |
| Enzyme 5 GenAtlas ID |
ALAS1  |
| Enzyme 5 HGNC ID |
HGNC:396  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed
]
- Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5252 |
| Enzyme 6 Name |
General transcription factor 3C polypeptide 4 |
| Enzyme 6 Synonyms |
- Transcription factor IIIC subunit delta
- TF3C-delta
- TFIIIC 90 kDa subunit
- TFIIIC 90
|
| Enzyme 6 Gene Name |
GTF3C4 |
| Enzyme 6 Protein Sequence |
>General transcription factor 3C polypeptide 4
MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKL
QYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKV
GSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRC
LLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQ
RRHSMQTPVRMEWSGICTTQQVKHNNESRDVGSVLLAVLFENGNIAVWQFQLPFVGKESI
SSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPV
ILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWRLLLISKAGLNLHNSHVTG
LHSLPIVSMTADKQNGTVYTCSSDGKVRQVIPIFTDVALKFEHQLIKLSDVFGSVRTHGI
AVKPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLI
DLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPT
HEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAG
GREPMEEKLLEIQGKIEAVEMHLTREHMKPVLGEVYLHTWITENTSIPTRGLCNFLMSDE
EYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSC
QSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF
|
| Enzyme 6 Number of Residues |
822 |
| Enzyme 6 Molecular Weight |
92002 |
| Enzyme 6 Theoretical pI |
6.71 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 6 Pfam Domain Function |
Not Available |
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
6175593  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9UKN8  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
TF3C4_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2469 bp
ATGAACACGGCCGACCAGGCCAGGGTGGGGCCCGCGGACGACGGGCCTGCGCCGTCTGGG
GAGGAGGAGGGAGAGGGGGGCGGCGAGGCGGGCGGGAAGGAGCCAGCAGCGGACGCGGCC
CCGGGGCCCAGCGCTGCATTCCGCCTCATGGTGACTCGGCGGGAGCCGGCCGTGAAGCTG
CAGTATGCGGTGAGCGGCCTGGAACCGCTGGCTTGGTCCGAGGACCACCGCGTGTCTGTG
TCCACGGCCCGCAGCATCGCTGTGCTGGAGCTCATCTGCGACGTGCACAACCCGGGCCAG
GACCTGGTTATCCACCGCACCTCGGTGCCCGCACCGCTCAACAGCTGTCTCCTCAAAGTT
GGCTCAAAAACAGAAGTTGCTGAGTGCAAGGAGAAATTCGCCGCCTCCAAGGACCCCACG
GTCAGTCAGACTTTCATGTTGGATAGGGTGTTCAACCCTGAGGGGAAGGCTTTACCACCA
ATGAGAGGATTCAAGTACACCAGCTGGTCTCCCATGGGTTGCGATGCTAATGGCAGGTGC
CTCTTGGCAGCACTGACCATGGACAATCGCCTGACCATCCAGGCAAATCTCAACAGACTG
CAGTGGGTCCAGCTGGTTGACCTGACTGAGATCTATGGAGAACGTCTTTATGAGACCAGT
TACAGGCTCTCTAAAAATGAGGCCCCGGAAGGAAATCTCGGGGATTTTGCTGAGTTTCAG
AGGAGACACAGCATGCAGACCCCAGTCAGAATGGAGTGGTCGGGCATCTGTACCACCCAG
CAGGTCAAGCATAACAACGAAAGCCGGGACGTTGGCAGTGTGCTCCTGGCTGTCCTCTTT
GAAAACGGTAATATCGCCGTGTGGCAGTTTCAGCTGCCGTTTGTAGGAAAAGAATCCATC
TCTTCATGCAACACAATTGAGTCAGGAATCACCTCTCCCAGTGTATTGTTTTGGTGGGAA
TATGAGCACAATAATCGAAAAATGAGTGGCCTTATTGTGGGGAGTGCTTTTGGACCCATA
AAAATTCTTCCTGTCAATCTCAAAGCAGTCAAAGGCTATTTCACTTTAAGGCAGCCTGTT
ATCTTGTGGAAAGAAATGGACCAGTTACCTGTGCACAGTATCAAATGTGTGCCACTTTAT
CATCCTTACCAGAAGTGTAGTTGCAGCTTAGTAGTGGCTGCAAGAGGCTCTTATGTATTT
TGGCGTCTTCTTCTGATCTCCAAAGCAGGGCTGAATCTTCACAATTCCCATGTCACAGGC
CTTCACTCACTGCCAATTGTCTCCATGACTGCAGACAAACAGAATGGAACAGTCTATACT
TGCTCCAGTGACGGAAAGGTGAGGCAGGTGATTCCGATTTTCACAGATGTTGCATTGAAG
TTTGAACACCAGTTGATTAAACTCTCAGATGTGTTTGGCTCAGTGAGGACTCACGGGATA
GCAGTGAAGCCCTGCGGTGCATACCTGGCCATCATCACCACTGAGGGCATGATCAACGGC
CTCCACCCTGTTAACAAAAACTACCAGGTCCAATTTGTTACTCTCAAAACCTTTGAAGAA
GCAGCTGCTCAGCTCCTGGAATCTTCAGTTCAAAACCTTTTTAAGCAGGTAGATTTAATA
GACCTAGTACGCTGGAAGATTTTAAAAGATAAACATATCCCTCAATTTTTACAAGAAGCT
TTGGAAAAAAAGATTGAAAGCAGTGGAGTCACCTATTTTTGGCGTTTTAAGCTTTTCCTC
CTGAGGATTTTATATCAGTCAATGCAGAAAACCCCTTCAGAAGCCTTGTGGAAACCCACC
CATGAGGACTCAAAAATCTTACTAGTGGATTCGCCTGGGATGGGCAATGCTGACGATGAA
CAGCAGGAAGAAGGCACTTCTTCCAAACAGGTGGTGAAGCAAGGCCTGCAGGAGAGGAGC
AAGGAAGGAGATGTAGAGGAGCCCACTGATGACTCGCTCCCCACGACTGGAGATGCTGGA
GGCCGTGAGCCAATGGAAGAGAAACTCCTGGAAATCCAAGGGAAAATCGAAGCTGTGGAG
ATGCACTTGACCAGGGAACACATGAAGCCAGTCTTAGGAGAAGTGTATCTGCACACCTGG
ATCACAGAAAACACTAGCATCCCCACCCGCGGACTCTGTAACTTTTTAATGTCTGATGAA
GAGTATGATGACAGAACTGCACGGGTGCTGATTGGACATATCTCAAAGAAGATGAACAAA
CAGACTTTCCCTGAGCACTGTAGTTTGTGTAAAGAGATCTTGCCATTCACAGATCGCAAA
CAGGCAGTCTGTTCCAATGGCCACATTTGGCTCCGGTGCTTCTTAACCTACCAGTCCTGC
CAGAGTTTGATATATAGAAGGTGTTTGCTCCATGACAGCATTGCCCGGCATCCAGCTCCA
GAAGATCCCGACTGGATTAAGAGGTTACTGCAAAGCCCCTGCCCTTTCTGTGATTCTCCT
GTCTTCTAA
|
| Enzyme 6 GenBank Gene ID |
AF142328  |
| Enzyme 6 GeneCard ID |
GTF3C4  |
| Enzyme 6 GenAtlas ID |
GTF3C4  |
| Enzyme 6 HGNC ID |
HGNC:4667  |
| Enzyme 6 Chromosome Location |
9 |
| Enzyme 6 Locus |
9q34.13 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG: The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity. Mol Cell Biol. 1999 Nov;19(11):7697-704. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5254 |
| Enzyme 7 Name |
Choline O-acetyltransferase |
| Enzyme 7 Synonyms |
- CHOACTase
- Choline acetylase
- ChAT
|
| Enzyme 7 Gene Name |
CHAT |
| Enzyme 7 Protein Sequence |
>Choline O-acetyltransferase
MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPH
PRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMA
AKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQ
QKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLIS
GVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPE
PEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSE
WAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANR
WYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQSSRKLIRADSVSELPAP
RRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQ
LAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLL
KDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQV
PTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRD
LCSLLPPTESKPLATKEKATRPSQGHQP
|
| Enzyme 7 Number of Residues |
748 |
| Enzyme 7 Molecular Weight |
82569 |
| Enzyme 7 Theoretical pI |
8.69 |
| Enzyme 7 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- acetyl-CoA + choline = CoA + O-acetylcholine
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
301096  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P28329  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
CLAT_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2247 bp
ATGGGGCTGAGGACAGCGAAGAAGAGGGGGCTTGGGGGAGGGGGGAAATGGAAGAGAGAG
GAGGGAGGAGGTACAAGAGGAAGGAGAGAAGTGCGGCCAGCTTGCTTTCTCCAGTCGGGT
GGCCGCGGGGACCCGGGCGACGTCGGAGGCCCTGCCGGGAACCCAGGCTGCAGCCCCCAC
CCCCGCGCTGCGACACGCCCCCCACCCCTTCCGGCTCACACCCCCGCCCACACTCCTGAG
TGGTGCGGTGCAGCGTCGGCCGAGGCAGCAGAGCCGAGGAGAGCAGGTCCACACCTCTGC
ATCCCTGCACCAGGACTCACCAAGACGCCCATCCTGGAAAAGGTCCCCCGTAAGATGGCA
GCAAAAACTCCCAGCAGTGAGGAGTCTGGGCTGCCCAAACTGCCCGTGCCCCCGCTGCAG
CAGACCCTGGCCACGTACCTGCAGTGCATGCGACACTTGGTGTCTGAGGAGCAGTTCAGG
AAGAGCCAGGCCATTGTGCAGCAGTTTGGGGCCCCTGGTGGCCTCGGCGAGACCCTGCAG
CAGAAACTCCTGGAGCGGCAGGAGAAGACAGCCAACTGGGTGTCTGAGTACTGGCTGAAT
GACATGTATCTCAACAACCGCCTGGCCCTGCCTGTCAACTCCAGCCCTGCCGTGATCTTT
GCTCGGCAGCACTTCCCTGGCACCGATGACCAGCTGAGGTTTGCAGCCAGCCTCATCTCT
GGTGTACTCAGCTACAAGGCCCTGCTGGACAGCCACTCCATTCCCACTGACTGTGCCAAA
CCGGAGCTGTCAGGGCAGCCCCTTTGCATGAAGCAATACTATGGGCTCTTCTCCTCCTAC
CGGCTCCCCGGCCATACCCAGGACACGCTGGTGGCTCAGAACAGCAGCATCATGCCGGAG
CCTGAGCACGTCATCGTAGCCTGCTGCAATCAGTTCTTTGTCTTGGATGTTGTCATTAAT
TTCCGCCGTCTCAGTGAGGGGGATCTGTTCACTCAGTTGAGAAAGATAGTCAAAATGGCT
TCCAACGAGGACGAGCGTTTGCCTCCAATTGGCCTGCTGACGTCTGACGGGAGGAGCGAG
TGGGCCGAGGCCAGGACGGTCCTCGTGAAAGACTCCACCAACCGGGACTCGCTGGACATG
ATTGAGCGCTGCATCTGCCTTGTATGCCTGGACGGCCCAGGAGGCGTGGAGCTCAGCGAC
ACCCACAGGGCACTCCAGCTCCTTCACGGCGGAGGCTACAGCAAGAACGGGGCCAATCGC
TGGTACGACAAGTCCCTGCAGTTTGTGGTGGGCCGAGACGCGACCTGCGGTGTGGTGTGC
GAACACTCCCCATTCGATGGCATCGTCCTGGTGCAGTGCACTGAGCATCTGCTCAAGCAC
ATGACGCAGAGCAGCAGGAAGCTGATCCGAGCAGACTCCGTCAGCGAGCTCCCCGCCCCC
CGGAGGCTGCGGTGGAAATGCTCCCCGGAAATTCAAGGCCACTTAGCCTCCTCGGCAGAA
AAACTTCAACGAATAGTAAAGAACCTTGACTTCATTGTCTATAAGTTTGACAACTATGGG
AAAACATTCATTAAGAAGCAGAAATGCAGCCCTGATGCCTTCATCCAGGTGGCCCTCCAG
CTGGCCTTCTACAGGCTCCACCGAAGACTGGTGCCCACCTACGAGAGCGCGTCCATCCGC
CGATTCCAGGAGGGACGCGTGGACAACATCAGATCGGCCACTCCAGAGGCACTGGCTTTT
GTGAGAGCCGTGACTGACCACAAGGCTGCTGTGCCAGCTTCTGAGAAGCTTCTGCTCCTG
AAGGATGCCATCCGTGCCCAGACTGCATACACAGTCATGGCCATAACAGGGATGGCCATT
GACAACCACCTGCTGGCACTGCGGGAGCTGGCCCGGGCCATGTGCAAGGAGCTGCCCGAG
ATGTTCATGGATGAAACCTACCTGATGAGCAACCGGTTTGTCCTCTCCACTAGCCAGGTG
CCCACAACCACGGAGATGTTCTGCTGCTATGGTCCTGTGGTCCCAAATGGGTATGGTGCC
TGCTACAACCCCCAGCCAGAGACCATCCTTTTCTGCATCTCTAGCTTTCACAGCTGCAAA
GAGACTTCTTCTAGCAAGTTTGCAAAAGCTGTGGAAGAAAGCCTCATTGACATGAGAGAC
CTCTGCAGTCTGCTGCCGCCTACTGAGAGCAAGCCATTGGCAACAAAGGAAAAAGCCACG
AGGCCCAGCCAGGGACACCAACCTTGA
|
| Enzyme 7 GenBank Gene ID |
S56138  |
| Enzyme 7 GeneCard ID |
CHAT  |
| Enzyme 7 GenAtlas ID |
CHAT  |
| Enzyme 7 HGNC ID |
HGNC:1912  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Oda Y, Nakanishi I, Deguchi T: A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. Brain Res Mol Brain Res. 1992 Dec;16(3-4):287-94. [PubMed
]
- Ohno K, Tsujino A, Brengman JM, Harper CM, Bajzer Z, Udd B, Beyring R, Robb S, Kirkham FJ, Engel AG: Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):2017-22. [PubMed
]
- Lorenzi MV, Trinidad AC, Zhang R, Strauss WL: Two mRNAs are transcribed from the human gene for choline acetyltransferase. DNA Cell Biol. 1992 Oct;11(8):593-603. [PubMed
]
- Toussaint JL, Geoffroy V, Schmitt M, Werner A, Garnier JM, Simoni P, Kempf J: Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. Genomics. 1992 Feb;12(2):412-6. [PubMed
]
- Cervini R, Rocchi M, DiDonato S, Finocchiaro G: Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. Neurosci Lett. 1991 Nov 11;132(2):191-4. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5256 |
| Enzyme 8 Name |
Histone acetyltransferase PCAF |
| Enzyme 8 Synonyms |
- P300/CBP-associated factor
- P/CAF
- Histone acetylase PCAF
|
| Enzyme 8 Gene Name |
PCAF |
| Enzyme 8 Protein Sequence |
>Histone acetyltransferase PCAF
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAA
AGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTP
PRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEED
ADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKE
RQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPR
YETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQ
NSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSG
LEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSA
RDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFD
PKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKH
DILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFS
VIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSK
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNR
YYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
|
| Enzyme 8 Number of Residues |
832 |
| Enzyme 8 Molecular Weight |
93014 |
| Enzyme 8 Theoretical pI |
9.37 |
| Enzyme 8 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
5468533  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q92831  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PCAF_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2499 bp
ATGTCCGAGGCTGGCGGGGCCGGGCCGGGCGGCTGCGGGGCAGGAGCCGGGGCAGGGGCC
GGGCCCGGGGCGCTGCCCCCGCAGCCTGCGGCGCTTCCGCCCGCGCCCCCGCAGGGCTCC
CCCTGCGCCGCTGCCGCCGGGGGCTCGGGCGCCTGCGGTCCGGCGACGGCAGTGGCTGCA
GCGGGCACGGCCGAAGGACCGGGAGGCGGTGGCTCGGCCCGAATCGCCGTGAAGAAAGCG
CAACTACGCTCCGCTCCGCGGGCCAAGAAACTGGAGAAACTCGGAGTGTACTCCGCCTGC
AAGGCCGAGGAGTCTTGTAAATGTAATGGCTGGAAAAACCCTAACCCCTCACCCACTCCC
CCCAGAGCCGACCTGCAGCAAATAATTGTCAGTCTAACAGAATCCTGTCGGAGTTGTAGC
CATGCCCTAGCTGCTCATGTTTCCCACCTGGAGAATGTGTCAGAGGAAGAAATGAACAGA
CTCCTGGGAATAGTATTGGATGTGGAATATCTCTTTACCTGTGTCCACAAGGAAGAAGAT
GCAGATACCAAACAAGTTTATTTCTATCTATTTAAGCTCTTGAGAAAGTCTATTTTACAA
AGAGGAAAACCTGTGGTTGAAGGCTCTTTGGAAAAGAAACCCCCATTTGAAAAACCTAGC
ATTGAACAGGGTGTGAATAACTTTGTGCAGTACAAATTTAGTCACCTGCCAGCAAAAGAA
AGGCAAACAATAGTTGAGTTGGCAAAAATGTTCCTAAACCGCATCAACTATTGGCATCTG
GAGGCACCATCTCAACGAAGACTGCGATCTCCCAATGATGATATTTCTGGATACAAAGAG
AACTACACAAGGTGGCTGTGTTACTGCAACGTGCCACAGTTCTGCGACAGTCTACCTCGG
TACGAAACCACACAGGTGTTTGGGAGAACATTGCTTCGCTCGGTCTTCACTGTTATGAGG
CGACAACTCCTGGAACAAGCAAGACAGGAAAAAGATAAACTGCCTCTTGAAAAACGAACT
CTAATCCTCACTCATTTCCCAAAATTTCTGTCCATGCTAGAAGAAGAAGTATATAGTCAA
AACTCTCCCATCTGGGATCAGGATTTTCTCTCAGCCTCTTCCAGAACCAGCCAGCTAGGC
ATCCAAACAGTTATCAATCCACCTCCTGTGGCTGGGACAATTTCATACAATTCAACCTCA
TCTTCCCTTGAGCAGCCAAACGCAGGGAGCAGCAGTCCTGCCTGCAAAGCCTCTTCTGGA
CTTGAGGCAAACCCAGGAGAAAAGAGGAAAATGACTGATTCTCATGTTCTGGAGGAGGCC
AAGAAACCCCGAGTTATGGGGGATATTCCGATGGAATTAATCAACGAGGTTATGTCTACC
ATCACGGACCCTGCAGCAATGCTTGGACCAGAGACCAATTTTCTGTCAGCACACTCGGCC
AGGGATGAGGCGGCAAGGTTGGAAGAGCGCAGGGGTGTAATTGAATTTCACGTGGTTGGC
AATTCCCTCAACCAGAAACCAAACAAGAAGATCCTGATGTGGCTGGTTGGCCTACAGAAC
GTTTTCTCCCACCAGCTGCCCCGAATGCCAAAAGAATACATCACACGGCTCGTCTTTGAC
CCGAAACACAAAACCCTTGCTTTAATTAAAGATGGCCGTGTTATTGGTGGTATCTGTTTC
CGTATGTTCCCATCTCAAGGATTCACAGAGATTGTCTTCTGTGCTGTAACCTCAAATGAG
CAAGTCAAGGGCTATGGAACACACCTGATGAATCATTTGAAAGAATATCACATAAAGCAT
GACATCCTGAACTTCCTCACATATGCAGATGAATATGCAATTGGATACTTTAAGAAACAG
GGTTTCTCCAAAGAAATTAAAATACCTAAAACCAAATATGTTGGCTATATCAAGGATTAT
GAAGGAGCCACTTTAATGGGATGTGAGCTAAATCCACGGATCCCGTACACAGAATTTTCT
GTCATCATTAAAAAGCAGAAGGAGATAATTAAAAAACTGATTGAAAGAAAACAGGCACAA
ATTCGAAAAGTTTACCCTGGACTTTCATGTTTTAAAGATGGAGTTCGACAGATTCCTATA
GAAAGCATTCCTGGAATTAGAGAGACAGGCTGGAAACCGAGTGGAAAAGAGAAAAGTAAA
GAGCCCAGAGACCCTGACCAGCTTTACAGCACGCTCAAGAGCATCCTCCAGCAGGTGAAG
AGCCATCAAAGCGCTTGGCCCTTCATGGAACCTGTGAAGAGAACAGAAGCTCCAGGATAT
TATGAAGTTATAAGGTTCCCCATGGATCTGAAAACCATGAGTGAACGCCTCAAGAATAGG
TACTACGTGTCTAAGAAATTATTCATGGCAGACTTACAGCGAGTCTTTACCAATTGCAAA
GAGTACAACGCCGCTGAGAGTGAATACTACAAATGTGCCAATATCCTGGAGAAATTCTTC
TTCAGTAAAATTAAGGAAGCTGGATTAATTGACAAGTGA
|
| Enzyme 8 GenBank Gene ID |
U57317  |
| Enzyme 8 GeneCard ID |
PCAF  |
| Enzyme 8 GenAtlas ID |
PCAF  |
| Enzyme 8 HGNC ID |
HGNC:8638  |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed
]
- Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [PubMed
]
- Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM: Structure and ligand of a histone acetyltransferase bromodomain. Nature. 1999 Jun 3;399(6735):491-6. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5257 |
| Enzyme 9 Name |
Carnitine O-acetyltransferase |
| Enzyme 9 Synonyms |
- Carnitine acetylase
- CAT
- Carnitine acetyltransferase
- CrAT
|
| Enzyme 9 Gene Name |
CRAT |
| Enzyme 9 Protein Sequence |
>Carnitine O-acetyltransferase
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSE
EEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSP
GVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSC
RVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSS
LQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVY
RSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGFPIVTLLDYVIE
YTKKPELVRSPMVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKD
FPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVK
AMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMD
TSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNA
ARLAHYLEKALLDMRALLQSHPRAKL
|
| Enzyme 9 Number of Residues |
626 |
| Enzyme 9 Molecular Weight |
70927 |
| Enzyme 9 Theoretical pI |
8.63 |
| Enzyme 9 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
- acetyl-CoA + carnitine = CoA + O-acetylcarnitine
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
927415  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P43155  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
CACP_HUMAN  |
| Enzyme 9 PDB ID |
1S5O  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1876 bp
AGCCTTCGCTGCCAGGACCGTGGTGAAGCCTCTGGGCTTCCTGAAGCCCTTCTCCTTGAT
GAAGGCTTCCAGCCGCTTCAAGGCACACCAGGATGCCCTGCCACGGCTGCCCGTGCCCCC
TCTCCAGCAGTCCCTGGACCACTACCTGAAGGCGCTGCAGCCCATCGTGAGTGAGGAGGA
GTGGGCCCACACCAAGCAGCTGGTGGATGAGTTTCAGGCCTCAGGAGGTGTAGGGGAGCG
CCTGCAGAAGGGGCTGGGGCGTCGGGCCAGGAAGACGGAGAACTGGCTGTCTGAGTGGTG
GCTCAAGACCGCCTACCTCCAGTACCGCCAGCCTGTGGTCATCTACTCGAGCCCAGGCGT
GATGCTACCCAAGCAGGACTTCGTGGACCTGCAGGGTCAGCTCCGATTTGCTGCCAAACT
CATTGAGGGTGTGTTGGATTTCAAGGTCATGATTGACAACGAGACCCTGCCCGTGGAGTA
CCTGGNGGGGAAGCCACTGTGCATGAACCAGTACTATCAGATCTTGTCCTCCTGCCGAGT
GCCGGGCCCCAAGCAGGACACAGTCAGCAACTTCAGCAAGACCAAGAAGCCTCCCACGCA
CATCACCGTGGTACACAACTACCAGTTTTTTGAGCTGGATGTGTACCACAGTGACGGGAC
ACCCCTCACTGCGGATCAGATCTTTGTGCAGCTGGAGAAGATCTGGAACTCATCCCTACA
GACCAACAAGGAGCCTGTGGGCATCCTCACCTCCAACCACCGCAACTCCTGGGCCAAGGC
ATACAACACCCTCATCAAAGACAAGGTGAACCGGGATTCCGTGCGCTCCATCCAGAAGAG
CATCTTCACCGTGTGCCTAGATGCAACCATGCCCAGGGTCTCAGAAGACGTGTACCGCAG
CCACGTGGCAGGCCAGATGCTGCATGGGGGCGGCAGCAGGCTCAACAGCGGCAACCGCTG
GTTTGACAAGACGCTGCAGTTCATCGTGGCAGAAGATGGCTCCTGTGGGCTTGTGTACGA
GCATGCTGCAGCNGAGGGTTTCCCTATTGTCACCCTTCTGGACTATGTCATCGAGTACAC
GAAGAAACCCGAGCTTGTGCNGTCTCCCATGGTGCCCCTGCCCATGCCCAAGAAGCTGCG
GTTCAACATCACCCCCGAGATCAAGAGCGACATCGAGAAGGCCAAGCAGAACCTCAGCAT
CATGATCCANNACCTGGATATCACCGTGATGGTGTTCCACCATTTTGGAAAAGACTTCCC
CAAGTCGGAGAAGCTAAGCCCAGATGCCTTCATCCAGATGGCTTTGCAGCTGGCCTACTA
CAGGATCTACGGACAGGCATGTGCCACCTATGAAAGTNCNTCCCTGCGCATGTTTCACCT
GGGCCGCACCGACACCATCCGCTCGGCTTCCATGGACTCACTCACCTTTGTCAAGGCCAT
GGATGACTCCAGCGTCACGGAGCACCAGAAGGTGGAGCTGCTGCGGAAGGCCGTGCAGGC
CCACCGGGGCTACACCGACCGGGCCATCCGCGGGGAGGCCTTTGGTCGACACCTGCTGGG
CCTGAAGCTGCAGGCCATCGAGGACCTGGTGAGCACGCCCGACATCTTCATGGACACCTC
CTACGCCATCGCCATGCACTTCCACCTCTCCACCAGCCAGGTCCCTGCCAAGACAGACTG
TGTCATGTTCTTCGGGCCCGTGGTCCCCGACGGCTACGGTGTCTGCTATAACCCCATGGA
GGCCCACATCAACTTCTCCCTGTCGGCCTACAACAGCTGCGCGGAGACCAACGCCGCCCG
CCTGGCGCATTACCTGGAGAAGGCGCTCCTGGACATGCGTGCCCTGCTGCAGAGCCACCC
CCGGGCCAAGCTCTGA
|
| Enzyme 9 GenBank Gene ID |
X78706  |
| Enzyme 9 GeneCard ID |
CRAT  |
| Enzyme 9 GenAtlas ID |
CRAT  |
| Enzyme 9 HGNC ID |
HGNC:2342  |
| Enzyme 9 Chromosome Location |
9 |
| Enzyme 9 Locus |
9q34.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Corti O, Finocchiaro G, Rossi E, Zuffardi O, DiDonato S: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. Genomics. 1994 Sep 1;23(1):94-9. [PubMed
]
- Corti O, DiDonato S, Finocchiaro G: Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. Biochem J. 1994 Oct 1;303 ( Pt 1):37-41. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5258 |
| Enzyme 10 Name |
Diamine acetyltransferase 1 |
| Enzyme 10 Synonyms |
- Spermidine/spermine N(1- acetyltransferase 1
- SSAT
- SSAT-1
- Putrescine acetyltransferase
- Polyamine N-acetyltransferase 1
|
| Enzyme 10 Gene Name |
SAT1 |
| Enzyme 10 Protein Sequence |
>Diamine acetyltransferase 1
MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVP
KEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRC
RCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE
|
| Enzyme 10 Number of Residues |
171 |
| Enzyme 10 Molecular Weight |
20024 |
| Enzyme 10 Theoretical pI |
4.82 |
| Enzyme 10 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Transcription |
| Enzyme 10 Specific Function |
Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine = spermidine >> spermine > 1- N-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells |
| Enzyme 10 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 10 Reactions |
- acetyl-CoA + an alkane-alpha,omega -diamine = CoA + an N-acetyldiamine
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
338392  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P21673  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SAT1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>516 bp
ATGGCTAAATTCGTGATCCGCCCAGCCACTGCCGCCGACTGCAGTGACATACTGCGGCTG
ATCAAGGAGCTGGCTAAATATGAATACATGGAAGAACAAGTAATCTTAACTGAAAAAGAT
CTGCTAGAAGATGGTTTTGGAGAGCACCCCTTTTACCACTGCCTGGTTGCAGAAGTGCCG
AAAGAGCACTGGACTCCGGAAGGACACAGCATTGTTGGTTTTGCCATGTACTATTTTACC
TATGACCCGTGGATTGGCAAGTTATTGTATCTTGAGGACTTCTTCGTGATGAGTGATTAT
AGAGGCTTTGGCATAGGATCAGAAATTCTGAAGAATCTAAGCCAGGTTGCAATGAGGTGT
CGCTGCAGCAGCATGCACTTCTTGGTAGCAGAATGGAATGAACCATCCATCAACTTCTAT
AAAAGAAGAGGTGCTTCTGATCTGTCCAGTGAAGAGGGTTGGAGACTGTTCAAGATCGAC
AAGGAGTACTTGCTAAAAATGGCAACAGAGGAGTGA
|
| Enzyme 10 GenBank Gene ID |
M77693  |
| Enzyme 10 GeneCard ID |
SAT1  |
| Enzyme 10 GenAtlas ID |
SAT1  |
| Enzyme 10 HGNC ID |
HGNC:10540  |
| Enzyme 10 Chromosome Location |
X |
| Enzyme 10 Locus |
Xp22.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Casero RA Jr, Celano P, Ervin SJ, Applegren NB, Wiest L, Pegg AE: Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. J Biol Chem. 1991 Jan 15;266(2):810-4. [PubMed
]
- Xiao L, Celano P, Mank AR, Pegg AE, Casero RA Jr: Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase. Biochem Biophys Res Commun. 1991 Aug 30;179(1):407-15. [PubMed
]
- Xiao L, Celano P, Mank AR, Griffin C, Jabs EW, Hawkins AL, Casero RA Jr: Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1). Biochem Biophys Res Commun. 1992 Sep 30;187(3):1493-502. [PubMed
]
- Casero RA Jr, Celano P, Ervin SJ, Wiest L, Pegg AE: High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma. Biochem J. 1990 Sep 15;270(3):615-20. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5259 |
| Enzyme 11 Name |
Serotonin N-acetyltransferase |
| Enzyme 11 Synonyms |
- Aralkylamine N- acetyltransferase
- AA-NAT
- Serotonin acetylase
|
| Enzyme 11 Gene Name |
AANAT |
| Enzyme 11 Protein Sequence |
>Serotonin N-acetyltransferase
MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVL
GVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAH
LHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCA
ITVGSLTFMELHCSLRGHPFLRRNSGC
|
| Enzyme 11 Number of Residues |
207 |
| Enzyme 11 Molecular Weight |
23344 |
| Enzyme 11 Theoretical pI |
7.57 |
| Enzyme 11 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Catalyzes the N-acetylation of serotonin into N- acetylserotonin |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- acetyl-CoA + an aralkylamine = CoA + an N-acetylaralkylamine
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
1389594  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q16613  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
SNAT_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>624 bp
ATGTCCACGCAGAGCACCCACCCCCTGAAACCTGAGGCCCCACGTCTGCCACCTGGGATC
CCCGAGTCCCCGAGCTGTCAGCGGCGCCACACACTCCCTGCCAGTGAGTTTCGCTGCCTC
ACCCCGGAGGACGCTGTCAGCGCCTTTGAGATCGAGCGTGAAGCCTTCATCTCCGTCTTG
GGCGTCTGCCCCCTGTACCTGGATGAGATCCGGCACTTCCTGACCCTATGTCCAGAGCTG
TCCCTGGGCTGGTTCGAGGAGGGCTGCCTTGTGGCCTTCATCATCGGCTCGCTCTGGGAC
AAGGAGAGACTCATGCAGGAGTCACTGACGCTGCACAGGTCTGGGGGCCACATAGCCCAC
CTGCATGTGCTGGCCGTGCACCGCGCCTTCCGGCAGCAGGGCAGGGGCCCCATCCTGCTG
TGGCGCTACCTGCACCACCTGGGCAGCCAGCCGGCCGTGCGCCGGGCCGCGCTCATGTGC
GAGGACGCGCTGGTACCCTTCTATGAGAGGTTCAGCTTCCACGCCGTGGGCCCCTGCGCC
ATCACCGTGGGCTCCCTCACCTTCATGGAGCTCCACTGCTCCCTGCGGGGCCACCCCTTC
CTGCGCAGGAACAGCGGCTGCTGA
|
| Enzyme 11 GenBank Gene ID |
U40391  |
| Enzyme 11 GeneCard ID |
AANAT  |
| Enzyme 11 GenAtlas ID |
AANAT  |
| Enzyme 11 HGNC ID |
HGNC:19  |
| Enzyme 11 Chromosome Location |
17 |
| Enzyme 11 Locus |
17q25 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR: The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. Genomics. 1996 May 15;34(1):76-84. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5260 |
| Enzyme 12 Name |
3-ketoacyl-CoA thiolase, mitochondrial |
| Enzyme 12 Synonyms |
- Beta- ketothiolase
- Acetyl-CoA acyltransferase
- Mitochondrial 3-oxoacyl- CoA thiolase
- T1
|
| Enzyme 12 Gene Name |
ACAA2 |
| Enzyme 12 Protein Sequence |
>3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
|
| Enzyme 12 Number of Residues |
397 |
| Enzyme 12 Molecular Weight |
41925 |
| Enzyme 12 Theoretical pI |
8.21 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Lipid transport and metabolism |
| Enzyme 12 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 12 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 12 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
509676  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P42765  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
THIM_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1194 bp
ATGCGTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTACTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
|
| Enzyme 12 GenBank Gene ID |
D16294  |
| Enzyme 12 GeneCard ID |
ACAA2  |
| Enzyme 12 GenAtlas ID |
ACAA2  |
| Enzyme 12 HGNC ID |
HGNC:83  |
| Enzyme 12 Chromosome Location |
18 |
| Enzyme 12 Locus |
18q21.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5262 |
| Enzyme 13 Name |
Testis-specific chromodomain protein Y 1 |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
CDY1 |
| Enzyme 13 Protein Sequence |
>Testis-specific chromodomain protein Y 1
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNRKLFAASKNVRR
KAASILSDTKNMEIINSTIETLAPDSPFDHKTVSGFQKLEKLDPIAADQQDTVVFKVTEG
KLLRDPLSRPGAEQTGIQNKTQIHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANGT
TDMHTSVPRVKGGQRNITDDSRDQPFIKKMHFTIRLTESASTYRDIVVKKEDGFTQIVLS
TRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVKHLRNNRNT
ASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTF
GQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIK
ELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDEF
|
| Enzyme 13 Number of Residues |
540 |
| Enzyme 13 Molecular Weight |
60474 |
| Enzyme 13 Theoretical pI |
9.61 |
| Enzyme 13 GO Classification |
| Function |
- binding
- chromatin binding
|
| Process |
- DNA metabolism
- DNA packaging
- cellular metabolism
- chromatin assembly or disassembly
- establishment and/or maintenance of chromatin architecture
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- chromatin
- chromosome
- intracellular membrane-bound organelle
- intracellular non-membrane-bound organelle
- membrane-bound organelle
- non-membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 13 General Function |
Lipid transport and metabolism |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
3342716  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9Y6F8  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CDY1_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1665 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACGCCAGTGACT
GATAAACACCACAGGTCCAAAAACCGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAATTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAAACTGTGAGTGGCTTTCAGAAACTTGAG
AAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAAGGG
AAACTCCTCCGGGACCCTTTGTCACGTCCTGGTGCAGAACAGACTGGAATACAGAACAAG
ACTCAGATACACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCCACA
GGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGGACA
ACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGATGAC
AGCAGAGACCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGTGCC
AGCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTATCA
ACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATAGTTAATGCT
CTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGTGTC
TTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAAGCACTTAAGGAATAACAGAAACACA
GCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTTAAA
AAGCCTATTGTTGTATCAGTCAATGGCCCTGCGATTGGACTAGGTGCATCCATCCTGCCT
CTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACCTTT
GGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCATCT
GCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCAAGGGAGGCATGCGCCAAAGGC
CTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATTAAG
GAGCTTGCCTCATACAATCCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGTAAT
ATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATCTGG
AGCTCAGCCCAAGGGATAGAATCCATGTTAAAAATACCTCTGTTGGGATATAAAGCAGCC
TTCCCTCCCAGAAAGACACAGAATGATCAGAGATGGTGCCCTTGA
|
| Enzyme 13 GenBank Gene ID |
AF000981  |
| Enzyme 13 GeneCard ID |
CDY1  |
| Enzyme 13 GenAtlas ID |
CDY1  |
| Enzyme 13 HGNC ID |
HGNC:1809  |
| Enzyme 13 Chromosome Location |
Y |
| Enzyme 13 Locus |
Yq11.23 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Lahn BT, Page DC: Functional coherence of the human Y chromosome. Science. 1997 Oct 24;278(5338):675-80. [PubMed
]
- Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5264 |
| Enzyme 14 Name |
Fatty acid synthase |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
FASN |
| Enzyme 14 Protein Sequence |
>Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
|
| Enzyme 14 Number of Residues |
2511 |
| Enzyme 14 Molecular Weight |
273403 |
| Enzyme 14 Theoretical pI |
6.39 |
| Enzyme 14 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- oxidoreductase activity
- phosphopantetheine binding
- transferase activity
- vitamin binding
|
| Process |
- biosynthesis
- carboxylic acid metabolism
- cellular metabolism
- fatty acid biosynthesis
- fatty acid metabolism
- metabolism
- organic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 14 Specific Function |
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
1049053  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P49327  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
FAS_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>7515 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
|
| Enzyme 14 GenBank Gene ID |
U26644  |
| Enzyme 14 GeneCard ID |
FASN  |
| Enzyme 14 GenAtlas ID |
FASN  |
| Enzyme 14 HGNC ID |
HGNC:3594  |
| Enzyme 14 Chromosome Location |
17 |
| Enzyme 14 Locus |
17q25 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed
]
- Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed
]
- Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5265 |
| Enzyme 15 Name |
Histone acetyltransferase HTATIP |
| Enzyme 15 Synonyms |
- 60 kDa Tat interactive protein
- Tip60
- HIV-1 Tat interactive protein
- cPLA(2-interacting protein
|
| Enzyme 15 Gene Name |
HTATIP |
| Enzyme 15 Protein Sequence |
>Histone acetyltransferase HTATIP
MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTH
ERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPK
EREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAV
AAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTIS
FFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKE
STEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQ
TILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
|
| Enzyme 15 Number of Residues |
513 |
| Enzyme 15 Molecular Weight |
58583 |
| Enzyme 15 Theoretical pI |
8.64 |
| Enzyme 15 GO Classification |
| Function |
- binding
- chromatin binding
|
| Process |
- DNA metabolism
- DNA packaging
- cellular metabolism
- chromatin assembly or disassembly
- establishment and/or maintenance of chromatin architecture
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- chromatin
- chromosome
- intracellular membrane-bound organelle
- intracellular non-membrane-bound organelle
- membrane-bound organelle
- non-membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. In case of HIV-1 infection, interaction with the viral Tat protein leads to HTATIP polyubiquitination and targets it to degradation |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
1657982  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q92993  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
TIP60_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1542 bp
ATGGCGGAGGTGGGGGAGATAATCGAGGGCTGCCGCCTACCCGTGCTGCGGCGGAACCAG
GACAACGAAGATGAGTGGCCCCTGGCCGAGATCCTGAGCGTGAAGGACATCAGTGGCCGG
AAGCTTTTCTACGTCCATTACATTGACTTCAACAAACGTCTGGATGAATGGGTGACGCAT
GAGCGGCTGGACCTAAAGAAGATCCAGTTCCCCAAGAAAGAGGCCAAGACCCCCACTAAG
AACGGACTTCCTGGGTCCCGTCCTGGCTCTCCAGAGAGAGAGGTGCCGGCCTCGGCGCAG
GCCAGCGGGAAGACCTTGCCAATCCCGGTCCAGATCACACTCCGCTTCAACCTGCCCAAG
GAGCGGGAGGCCATTCCCGGTGGCGAGCCTGACCAGCCGCTCTCCTCCAGCTCCTGCCTG
CAGCCCAACCACCGCTCAACGAAACGGAAGGTGGAGGTGGTTTCACCAGCAACTCCAGTG
CCCAGCGAGACAGCCCCGGCCTCGGTTTTTCCCCAGAATGGAGCCGCCCGTAGGGCAGTG
GCAGCCCAGCCAGGACGGAAGCGAAAATCGAATTGTTTGGGCACTGATGAGGACTCCCAG
GACAGCTCTGATGGAATACCGTCAGCACCACGCATGACTGGCAGCCTGGTGTCTGATCGA
AGCCACGACGACATCGTCACCCGGATGAAGAACATTGAGTGCATTGAGCTGGGCCGGCAC
CGCCTCAAGCCGTGGTACTTCTCCCCGTACCCACAGGAACTCACCACATTGCCTGTCCTC
TACCTGTGCGAGTTCTGCCTCAAGTACGGCCGTAGTCTCAAGTGTCTTCAGCGTCATTTG
ACCAAGTGTGACCTACGACATCCTCCAGGCAATGAGATTTACCGCAAGGGCACCATCTCC
TTCTTTGAGATTGATGGACGTAAGAACAAGAGTTATTCCCAGAACCTGTGTCTTTTGGCC
AAGTGTTTCCTTGACCATAAGACACTGTACTATGACACAGACCCTTTCCTCTTCTACGTC
ATGACAGAGTATGACTGTAAGGGCTTCCACATCGTGGGCTACTTCTCCAAGGAGAAAGAA
TCAACGGAAGACTACAATGTGGCCTGCATCCTAACCCTGCCTCCCTACCAGCGCCGGGGC
TACCGGAAGCTGCTGATCGAGTTCAGCTATGAACTCTCCAAAGTGGAAGGGAAAACAGGG
ACCCCTGAGAAGCCCCTCTCAGACCTTGGCCTCCTATCCTATCGAAGCTACTGGTCCCAG
ACCATCCTGGAGATCCTGATGGGGCTGAAGTCGGAGAGCGGGGAGAGGCCACAGATCACC
ATCAATGAGATTAGTGAAATCACCAGCATCAAGAAGGAGGATGTCATCTCCACTCTGCAG
TACCTCAATCTCATCAACTACTACAAGGGCCAGTACATCCTCACACTGTCAGAGGACATC
GTGGATGGCCATGAGCGGGCCATGCTCAAGCGGCTCCTGCGGATCGACTCCAAGTGTCTG
CACTTCACTCCCAAGGACTGGAGCAAGAGGGGGAAGTGGTGA
|
| Enzyme 15 GenBank Gene ID |
U74667  |
| Enzyme 15 GeneCard ID |
HTATIP  |
| Enzyme 15 GenAtlas ID |
HTATIP  |
| Enzyme 15 HGNC ID |
HGNC:5275  |
| Enzyme 15 Chromosome Location |
11 |
| Enzyme 15 Locus |
11q13 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G: Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology. 1996 Feb 15;216(2):357-66. [PubMed
]
- Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed
]
- Kimura A, Horikoshi M: Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells. 1998 Dec;3(12):789-800. [PubMed
]
- Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell. 2000 Aug 18;102(4):463-73. [PubMed
]
- Lee HJ, Chun M, Kandror KV: Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. J Biol Chem. 2001 May 18;276(20):16597-600. Epub 2001 Mar 21. [PubMed
]
- Xiao H, Chung J, Kao HY, Yang YC: Tip60 is a co-repressor for STAT3. J Biol Chem. 2003 Mar 28;278(13):11197-204. Epub 2003 Jan 27. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5268 |
| Enzyme 16 Name |
Nuclear receptor coactivator 1 |
| Enzyme 16 Synonyms |
- NCoA-1
- Steroid receptor coactivator 1
- SRC-1
- RIP160
- Protein Hin-2
- Renal carcinoma antigen NY-REN-52
|
| Enzyme 16 Gene Name |
NCOA1 |
| Enzyme 16 Protein Sequence |
>Nuclear receptor coactivator 1
MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSL
SVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEAL
DGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNG
VPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQ
SCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFF
QPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMG
IHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINR
QQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNKGQASSQSSKPSLNLNNPPMEGTG
ISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTS
LQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASTLNEMIQSDN
SSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSC
TGTSNSASANSSGGSCPSSHSSLTARHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVS
VTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQ
MDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAV
TSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAIN
QSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKL
VQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPFPTANLPSPFQGMVRQKPSLGT
MPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQF
AATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSF
GNNLPPSSGLPVQTGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLAN
RNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPI
PPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVS
MAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTE
ADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLT
E
|
| Enzyme 16 Number of Residues |
1441 |
| Enzyme 16 Molecular Weight |
156742 |
| Enzyme 16 Theoretical pI |
6.33 |
| Enzyme 16 GO Classification |
| Function |
- binding
- protein binding
- signal transducer activity
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transcription regulator activity
|
| Process |
- cell communication
- cellular process
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- signal transduction
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3 |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
1480646  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q15788  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
NCOA1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>4323 bp
ATGAGTGGCCTCGGGGACAGTTCATCCGACCCTGCTAACCCAGACTCACATAAGAGGAAA
GGATCGCCATGTGACACACTGGCATCAAGCACGGAAAAGAGGCGCAGGGAGCAAGAAAAT
AAATATTTAGAAGAACTAGCTGAGTTACTGTCTGCCAACATTAGTGACATTGACAGCTTG
AGTGTAAAACCAGACAAATGCAAGATTTTGAAGAAAACAGTCGATCAGATACAGCTAATG
AAGAGAATGGAACAAGAGAAATCAACAACTGATGACGATGTACAGAAATCAGACATCTCA
TCAAGTAGTCAAGGAGTGATAGAAAAGGAATCCTTGGGACCCCTTCTTTTGGAGGCTTTG
GATGGATTTTTCTTTGTTGTGAACTGTGAAGGGAGAATTGTATTTGTGTCAGAGAATGTA
ACCAGCTACTTAGGTTACAATCAGGAGGAATTAATGAATACCAGCGTCTACAGCATACTG
CACGTGGGGGATCATGCAGAATTTGTGAAGAATCTGCTACCAAAATCACTAGTAAATGGA
GTTCCTTGGCCTCAAGAGGCAACACGACGAAATAGCCATACCTTTAACTGCAGGATGCTA
ATTCACCCTCCAGATGAGCCAGGGACCGAGAACCAAGAAGCTTGCCAGCGTTATGAAGTA
ATGCAGTGTTTCACTGTGTCACAGCCAAAATCAATTCAAGAGGATGGAGAAGATTTCCAG
TCATGTCTGATTTGTATTGCACGGCGATTACCTCGGCCTCCAGCTATTACGGGTGTAGAA
TCCTTTATGACCAAGCAAGATACTACAGGTAAAATCATCTCTATTGATACTAGTTCCCTG
AGAGCTGCTGGCAGAACTGGTTGGGAAGATTTAGTGAGGAAGTGCATTTATGCTTTTTTC
CAACCTCAGGGCAGAGAACCATCTTATGCCAGACAGCTGTTCCAAGAAGTGATGACTCGT
GGCACTGCCTCCAGCCCCTCCTATAGATTCATATTGAATGATGGGACAATGCTTAGCGCC
CACACCAAGTGTAAACTTTGCTACCCTCAAAGTCCAGACATGCAACCTTTCATCATGGGA
ATTCATATCATCGACAGGGAGCACAGTGGGCTTTCTCCTCAAGATGACACTAATTCTGGA
ATGTCAATTCCCCGAGTAAATCCCTCGGTCAATCCTAGTATCTCTCCAGCTCATGGTGTG
GCTCGTTCATCCACATTGCCACCATCCAACAGCAACATGGTATCCACCAGAATAAACCGC
CAGCAGAGCTCAGACCTTCATAGCAGCAGTCATAGTAATTCTAGCAACAGCCAAGGAAGT
TTCGGATGCTCACCCGGAAGTCAGATTGTAGCCAATGTTGCCTTAAACCAAGGACAGGCC
AGTTCACAGAGCAGTAATCCCTCTTTAAACCTCAATAATTCTCCTATGGAAGGTACAGGA
ATATCCCTAGCACAGTTCATGTCTCCAAGGAGACAGGTTACTTCTGGATTGGCAACAAGG
CCCAGGATGCCAAACAATTCCTTTCCTCCTAATATTTCGACATTAAGCTCTCCCGTTGGC
ATGACAAGTAGTGCCTGTAATAATAATAACCGATCTTATTCAAACATCCCAGTAACATCT
TTACAGGGTATGAATGAAGGACCCAATAACTCCGTTGGCTTCTCTGCCAGTTCTCCAGTC
CTCAGGCAGATGAGCTCACAGAATTCACCTAGCAGATTAAATATACAACCAGCAAAAGCT
GAGTCCAAAGATAACAAAGAGATTGCCTCAATTTTAAATGAAATGATTCAATCTGACAAC
AGCTCTAGTGATGGCAAACCTCTGGATTCAGGGCTTCTGCATAACAATGACAGACTTTCA
GATGGAGACAGTAAATACTCTCAAACCAGTCACAAACTAGTGCAGCTTTTGACAACAACT
GCCGAACAGCAGTTACGGCATGCTGATATAGACACAAGCTGCAAAGATGTCCTGTCTTGC
ACAGGCACTTCCAACTCTGCCTCTGCTAACTCTTCAGGAGGTTCTTGTCCCTCTTCTCAT
AGCTCATTGACAGAACGGCATAAAATTCTACACCGGCTCTTACAGGAGGGTAGCCCCTCA
GATATCACCACTTTGTCTGTCGAGCCTGATAAAAAGGACAGTGCATCTACTTCTGTGTCA
GTGACTGGACAGGTACAAGGAAACTCCAGTATAAAACTAGAACTGGATGCTTCAAAGAAA
AAAGAATCAAAAGACCATCAGCTCCTACGCTATCTTTTAGATAAAGATGAGAAAGATTTA
AGATCAACTCCAAACCTGAGCCTGGATGATGTAAAGGTGAAAGTGGAAAAGAAAGAACAG
ATGGATCCATGTAATACAAACCCAACCCCAATGACCAAACCCACTCCTGAGGAAATAAAA
CTGGAGGCCCAGAGCCAGTTTACAGCTGACCTTGACCAGTTTGATCAGTTACTGCCCACG
CTGGAGAAGGCAGCACAGTTGCCAGGCTTATGTGAGACAGACAGGATGGATGGTGCGGTC
ACCAGTGTAACCATCAAATCGGAGATCCTGCCAGCTTCACTTCAGTCCGCCACTGCCAGA
CCCACTTCCAGGCTAAATAGATTACCTGAGCTGGAATTGGAAGCAATTGATAACCAATTT
GGACAACCAGGAACAGGCGATCAGATTCCATGGACAAATAATACAGTGACAGCTATAAAT
CAGAGTAAATCAGAAGACCAGTGTATTAGCTCACAATTAGATGAGCTTCTCTGTCCACCC
ACAACAGTAGAAGGGAGAAATGATGAGAAGGCTCTTCTTGAACAGCTGGTATCCTTCCTT
AGTGGCAAAGATGAAACTGAGCTAGCTGAACTAGACAGAGCTCTGGGAATTGACAAACTT
GTTCAGGGGGGTGGATTAGATGTATTATCAGAGAGATTTCCACCACAACAAGCAACGCCA
CCTTTGATCATGGAAGAAAGACCCAACCTTTATTCCCAGCCTTACTCTTCTCCTTCTCCT
ACTGCCAATCTCCCTAGCCCTTTCCAAGGCATGGTCAGGCAAAAACCTTCACTGGGGACG
ATGCCTGTTCAAGTAACACCTCCCCGAGGTGCTTTTTCACCTGGCATGGGCATGCAGCCC
AGGCAAACTCTAAACAGACCTCCGGCTGCACCTAACCAGCTTCGACTTCAACTACAGCAG
CGATTACAGGGACAACAGCAGTTGATACACCAAAATCGGCAAGCTATCTTAAACCAGTTT
GCAGCAACTGCTCCTGTTGGCATCAATATGAGATCAGGCATGCAACAGCAAATTACACCT
CAGCCACCCCTGAATGCTCAAATGTTGGCACAACGTCAGCGGGAACTGTACAGTCAACAG
CACCGACAGAGGCAGCTAATACAGCAGCAAAGAGCCATGCTTATGAGGCAGCAAAGCTTT
GGGAACAACCTCCCTCCCTCATCTGGACTACCAGTTCAAATGGGGAACCCCCGTCTTCCT
CAGGGTGCTCCACAGCAATTCCCCTATCCACCAAACTATGGTACAAATCCAGGAACCCCA
CCTGCTTCTACCAGCCCGTTTTCACAACTAGCAGCAAATCCTGAAGCATCCTTGGCCAAC
CGCAACAGCATGGTGAGCAGAGGCATGACAGGAAACATAGGAGGACAGTTTGGCACTGGA
ATCAATCCTCAGATGCAGCAGAATGTCTTCCAGTATCCAGGAGCAGGAATGGTTCCCCAA
GGTGAGGCCAACTTTGCTCCATCTCTAAGCCCTGGGAGCTCCATGGTGCCGATGCCAATC
CCTCCTCCTCAGAGTTCTCTGCTCCAGCAAACTCCACCTGCCTCCGGGTATCAGTCACCA
GACATGAAGGCCTGGCAGCAAGGAGCGATAGGAAACAACAATGTGTTCAGTCAAGCTGTC
CAGAACCAGCCCACGCCTGCACAGCCAGGAGTATACAACAACATGAGCATCACCGTTTCC
ATGGCAGGTGGAAATACGAATGTTCAGAACATGAACCCAATGATGGCCCAGATGCAGATG
AGCTCTTTGCAGATGCCAGGAATGAACACTGTGTGCCCTGAGCAGATAAATGATCCCGCA
CTGAGACACACAGGCCTCTACTGCAACCAGCTCTCATCCACTGACCTTCTCAAAACAGAA
GCAGATGGAACCCAGGTGCAACAGGTTCAGGTGTTTGCTGACGTCCAGTGTACAGTGAAT
CTGGTAGGCGGGGACCCTTACCTGAACCAGCCTGGTCCACTGGGAACTCAAAAGCCCACG
TCAGGACCACAGACCCCCCAGGCCCAGCAGAAGAGCCTCCTTCAGCAGCTACTGACTGAA
TAA
|
| Enzyme 16 GenBank Gene ID |
U59302  |
| Enzyme 16 GeneCard ID |
NCOA1  |
| Enzyme 16 GenAtlas ID |
NCOA1  |
| Enzyme 16 HGNC ID |
HGNC:7668  |
| Enzyme 16 Chromosome Location |
2 |
| Enzyme 16 Locus |
2p23 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Takeshita A, Yen PM, Misiti S, Cardona GR, Liu Y, Chin WW: Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator. Endocrinology. 1996 Aug;137(8):3594-7. [PubMed
]
- Kalkhoven E, Valentine JE, Heery DM, Parker MG: Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 1998 Jan 2;17(1):232-43. [PubMed
]
- Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 1995 Nov 24;270(5240):1354-7. [PubMed
]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed
]
- Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed
]
- Carrero P, Okamoto K, Coumailleau P, O'Brien S, Tanaka H, Poellinger L: Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol Cell Biol. 2000 Jan;20(1):402-15. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5269 |
| Enzyme 17 Name |
Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor |
| Enzyme 17 Synonyms |
- HMG-CoA synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
|
| Enzyme 17 Gene Name |
HMGCS2 |
| Enzyme 17 Protein Sequence |
>Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
|
| Enzyme 17 Number of Residues |
508 |
| Enzyme 17 Molecular Weight |
56636 |
| Enzyme 17 Theoretical pI |
8.28 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- acetyl-CoA metabolism
- cellular metabolism
- coenzyme metabolism
- cofactor metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Lipid transport and metabolism |
| Enzyme 17 Specific Function |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Enzyme 17 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 17 Reactions |
- acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
Not Available |
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
619877  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P54868  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
HMCS2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1527 bp
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGCCCA
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTATATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
|
| Enzyme 17 GenBank Gene ID |
X83618  |
| Enzyme 17 GeneCard ID |
HMGCS2  |
| Enzyme 17 GenAtlas ID |
HMGCS2  |
| Enzyme 17 HGNC ID |
HGNC:5008  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1p13-p12 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed
]
- Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed
]
- Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5271 |
| Enzyme 18 Name |
Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor |
| Enzyme 18 Synonyms |
- Acetate--CoA ligase 2
- Acetyl-CoA synthetase 2
- Acyl- CoA synthetase short-chain family member 1
|
| Enzyme 18 Gene Name |
ACSS1 |
| Enzyme 18 Protein Sequence |
>Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
|
| Enzyme 18 Number of Residues |
689 |
| Enzyme 18 Molecular Weight |
74857 |
| Enzyme 18 Theoretical pI |
7.11 |
| Enzyme 18 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Lipid transport and metabolism |
| Enzyme 18 Specific Function |
Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2) |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
56203089  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9NUB1  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
ACS2L_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1439 bp
CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA
|
| Enzyme 18 GenBank Gene ID |
AL035661  |
| Enzyme 18 GeneCard ID |
ACSS1  |
| Enzyme 18 GenAtlas ID |
ACSS1  |
| Enzyme 18 HGNC ID |
HGNC:16091  |
| Enzyme 18 Chromosome Location |
20 |
| Enzyme 18 Locus |
20p11.23-p11.21 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5272 |
| Enzyme 19 Name |
Citrate synthase, mitochondrial precursor |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
CS |
| Enzyme 19 Protein Sequence |
>Citrate synthase, mitochondrial precursor
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
|
| Enzyme 19 Number of Residues |
466 |
| Enzyme 19 Molecular Weight |
51713 |
| Enzyme 19 Theoretical pI |
8.53 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- citrate (Si)-synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- cellular metabolism
- energy derivation by oxidation of organic compounds
- generation of precursor metabolites and energy
- main pathways of carbohydrate metabolism
- metabolism
- physiological process
- tricarboxylic acid cycle
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 19 General Function |
Energy production and conversion |
| Enzyme 19 Specific Function |
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- acetyl-CoA + H2O + oxaloacetate = citrate + CoA
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
Not Available |
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
3288815  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
O75390  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
CISY_HUMAN  |
| Enzyme 19 PDB ID |
4CTS  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1401 bp
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
|
| Enzyme 19 GenBank Gene ID |
AF047042  |
| Enzyme 19 GeneCard ID |
CS  |
| Enzyme 19 GenAtlas ID |
CS  |
| Enzyme 19 HGNC ID |
HGNC:2422  |
| Enzyme 19 Chromosome Location |
12 |
| Enzyme 19 Locus |
12q13.2-q13.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed
]
- Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5273 |
| Enzyme 20 Name |
Testis-specific chromodomain protein Y 2 |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
CDY2A |
| Enzyme 20 Protein Sequence |
>Testis-specific chromodomain protein Y 2
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNCKLFAASKNVRR
KAASTLSDTKNMEIINSTIETLAPDSPFDHKKTVSGFQKLEKLDPIAADQQDTVVFKVTE
GKLLRDPLSHPGAEQTGIQNKTQMHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANG
TTDMHTSVPRVKGGQRNITDDSRGQPFIKKMHFTIRLTESAITYRDIVVKKEDGFTQIVL
STRSTEKNALNTEVIKEMVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVRHLRNDRN
TASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTT
FGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQI
KELASYNAIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDE
F
|
| Enzyme 20 Number of Residues |
541 |
| Enzyme 20 Molecular Weight |
60525 |
| Enzyme 20 Theoretical pI |
9.42 |
| Enzyme 20 GO Classification |
| Function |
- binding
- chromatin binding
|
| Process |
- DNA metabolism
- DNA packaging
- cellular metabolism
- chromatin assembly or disassembly
- establishment and/or maintenance of chromatin architecture
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- chromatin
- chromosome
- intracellular membrane-bound organelle
- intracellular non-membrane-bound organelle
- membrane-bound organelle
- non-membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 20 General Function |
Lipid transport and metabolism |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
4558754  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9Y6F7  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
CDY2_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1626 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACTCCAGTGACT
GATAAACACCACAGGTCCAAAAACTGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAACTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAGAAAACTGTGAGTGGCTTTCAGAAACTT
GAGAAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAA
GGGAAACTCCTCCGGGACCCTTTGTCACATCCTGGTGCAGAACAGACTGGAATACAGAAC
AAGACTCAGATGCACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCC
ACAGGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGG
ACAACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGAT
GACAGCAGAGGCCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGT
GCCATCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTA
TCAACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATGGTTAAT
GCTCTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGT
GTCTTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAGGCACTTAAGGAATGACAGAAAC
ACAGCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTT
AAAAAGCCTATTGTTGTATCAGTCAATGGCCCTGCCATTGGACTAGGTGCATCCATCCTG
CCTCTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACC
TTTGGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCA
TCTGCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCACGGGAGGCATGCGCCAAA
GGCCTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATT
AAGGAGCTTGCCTCATACAATGCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGT
AATATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATC
TGGAGCTCAGCCCAAGGGATAGAATCCATGTTAAAGTATGTTGAAAATAAAATTGATGAG
TTTTAA
|
| Enzyme 20 GenBank Gene ID |
AF080598  |
| Enzyme 20 GeneCard ID |
CDY2A  |
| Enzyme 20 GenAtlas ID |
CDY2A  |
| Enzyme 20 HGNC ID |
HGNC:1810  |
| Enzyme 20 Chromosome Location |
Y |
| Enzyme 20 Locus |
Yq11.221 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5275 |
| Enzyme 21 Name |
Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor |
| Enzyme 21 Synonyms |
- PDHE1-A type I
|
| Enzyme 21 Gene Name |
PDHA1 |
| Enzyme 21 Protein Sequence |
>Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS
|
| Enzyme 21 Number of Residues |
390 |
| Enzyme 21 Molecular Weight |
43296 |
| Enzyme 21 Theoretical pI |
8.14 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Energy production and conversion |
| Enzyme 21 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
Not Available |
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
387009  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P08559  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
ODPA_HUMAN  |
| Enzyme 21 PDB ID |
1NI4  |
| Enzyme 21 PDB File |
Show |
| Enzyme 21 3D Structure |
|
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1173 bp
ATGAGGAAGATGCTCGCCGCCGTCTCCCGCGTGCTGTCTGGCGCTTCTCAGAAGCCGGCA
AGCAGAGTGCTGGTAGCATCCCGTAATTTTGCAAATGATGCTACATTTGAAATTAAGAAA
TGTGACCTTCACCGGCTGGAAGAAGGCCCTCCTGTCACAACAGTGCTCACCAGGGAGGAT
GGGCTCAAATACTACAGGATGATGCAGACTGTACGCCGAATGGAGTTGAAAGCAGATCAG
CTGTATAAACAGAAAATTATTCGTGGTTTCTGTCACTTGTGTGATGGTCAGGAAGCTTGC
TGTGTGGGCCTGGAGGCCGGCATCAACCCCACAGACCATCTCATCACAGCCTACCGGGCT
CACGGCTTTACTTTCACCCGGGGCCTTTCCGTCCGAGAAATTCTCGCAGAGCTTACAGGA
CGAAAAGGAGGTTGTGCTAAAGGGAAAGGAGGATCGATGCACATGTATGCCAAGAACTTC
TACGGGGGCAATGGCATCGTGGGAGCGCAGGTGCCCCTGGGCGCTGGGATTGCTCTAGCC
TGTAAGTATAATGGAAAAGATGAGGTCTGCCTGACTTTATATGGCGATGGTGCTGCTAAC
CAGGGCCAGATATTCGAAGCTTACAACATGGCAGCTTTGTGGAAATTACCTTGTATTTTC
ATCTGTGAGAATAATCGCTATGGAATGGGAACGTCTGTTGAGAGAGCGGCAGCCAGCACT
GATTACTACAAGAGAGGCGATTTCATTCCTGGGCTGAGAGTGGATGGAATGGATATCCTG
TGCGTCCGAGAGGCAACAAGGTTTGCTGCTGCCTATTGTAGATCTGGGAAGGGGCCCATC
CTGATGGAGCTGCAGACTTACCGTTACCACGGACACAGTATGAGTGACCCTGGAGTCAGT
TACCGTACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGTGACCCTATTATGCTTCTC
AAGGACAGGATGGTGAACAGCAATCTTGCCAGTGTGGAAGAACTAAAGGAAATTGATGTG
GAAGTGAGGAAGGAGATTGAGGATGCTGCCCAGTTTGCCACGGCCGATCCTGAGCCACCT
TTGGAAGAGCTGGGCTACCACATCTACTCCAGCGACCCACCTTTTGAAGTTCGTGGTGCC
AATCAGTGGATCAAGTTTAAGTCAGTCAGTTAA
|
| Enzyme 21 GenBank Gene ID |
M27257  |
| Enzyme 21 GeneCard ID |
PDHA1  |
| Enzyme 21 GenAtlas ID |
PDHA1  |
| Enzyme 21 HGNC ID |
HGNC:8806  |
| Enzyme 21 Chromosome Location |
X |
| Enzyme 21 Locus |
Xp22.2-p22.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Koike K, Urata Y, Matsuo S, Koike M: Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit. Gene. 1990 Sep 14;93(2):307-11. [PubMed
]
- Ho L, Wexler ID, Liu TC, Thekkumkara TJ, Patel MS: Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5330-4. [PubMed
]
- Dahl HH, Hunt SM, Hutchison WM, Brown GK: The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. 1987 May 25;262(15):7398-403. [PubMed
]
- Maragos C, Hutchison WM, Hayasaka K, Brown GK, Dahl HH: Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex. J Biol Chem. 1989 Jul 25;264(21):12294-8. [PubMed
]
- De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH: Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. 1988 Feb 5;263(4):1991-5. [PubMed
]
- Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed
]
- Harris EE, Hey J: X chromosome evidence for ancient human histories. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3320-4. [PubMed
]
- Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed
]
- Dahl HH, Brown GK, Brown RM, Hansen LL, Kerr DS, Wexler ID, Patel MS, De Meirleir L, Lissens W, Chun K, et al.: Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene. Hum Mutat. 1992;1(2):97-102. [PubMed
]
- Hansen LL, Brown GK, Kirby DM, Dahl HH: Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis. 1991;14(2):140-51. [PubMed
]
- De Meirleir L, Lissens W, Vamos E, Liebaers I: Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit. Hum Genet. 1992 Mar;88(6):649-52. [PubMed
]
- Dahl HH, Hansen LL, Brown RM, Danks DM, Rogers JG, Brown GK: X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation. J Inherit Metab Dis. 1992;15(6):835-47. [PubMed
]
- Matthews PM, Marchington DR, Squier M, Land J, Brown RM, Brown GK: Molecular genetic characterization of an X-linked form of Leigh's syndrome. Ann Neurol. 1993 Jun;33(6):652-5. [PubMed
]
- Chun K, MacKay N, Petrova-Benedict R, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex. Hum Mol Genet. 1993 Apr;2(4):449-54. [PubMed
]
- Matthews PM, Brown RM, Otero LJ, Marchington DR, LeGris M, Howes R, Meadows LS, Shevell M, Scriver CR, Brown GK: Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients. Brain. 1994 Jun;117 ( Pt 3):435-43. [PubMed
]
- Hansen LL, Horn N, Dahl HH, Kruse TA: Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit. Hum Mol Genet. 1994 Jun;3(6):1021-2. [PubMed
]
- Dahl HH, Brown GK: Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit. Hum Mutat. 1994;3(2):152-5. [PubMed
]
- Awata H, Endo F, Tanoue A, Kitano A, Matsuda I: Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia. J Inherit Metab Dis. 1994;17(2):189-95. [PubMed
]
- Chun K, MacKay N, Petrova-Benedict R, Federico A, Fois A, Cole DE, Robertson E, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex. Am J Hum Genet. 1995 Mar;56(3):558-69. [PubMed
]
- Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, Lithgow T, Dahl HH: An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am J Hum Genet. 1995 Oct;57(4):772-80. [PubMed
]
- Hemalatha SG, Kerr DS, Wexler ID, Lusk MM, Kaung M, Du Y, Kolli M, Schelper RL, Patel MS: Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit. Hum Mol Genet. 1995 Feb;4(2):315-8. [PubMed
]
- Lissens W, De Meirleir L, Seneca S, Benelli C, Marsac C, Poll-The BT, Briones P, Ruitenbeek W, van Diggelen O, Chaigne D, Ramaekers V, Liebaers I: Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency. Hum Mutat. 1996;7(1):46-51. [PubMed
]
- Tripatara A, Kerr DS, Lusk MM, Kolli M, Tan J, Patel MS: Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS). Hum Mutat. 1996;8(2):180-2. [PubMed
]
- Otero LJ, Brown RM, Brown GK: Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity. Hum Mutat. 1998;12(2):114-21. [PubMed
]
- Ito M, Huq AH, Naito E, Saijo T, Takeda E, Kuroda Y: Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein. J Inherit Metab Dis. 1992;15(6):848-56. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5277 |
| Enzyme 22 Name |
Trifunctional enzyme subunit beta, mitochondrial precursor |
| Enzyme 22 Synonyms |
- TP-beta[Includes: 3-ketoacyl-CoA thiolase
- Acetyl-CoA acyltransferase
- Beta-ketothiolase]
|
| Enzyme 22 Gene Name |
HADHB |
| Enzyme 22 Protein Sequence |
>Trifunctional enzyme subunit beta, mitochondrial precursor
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
|
| Enzyme 22 Number of Residues |
474 |
| Enzyme 22 Molecular Weight |
51295 |
| Enzyme 22 Theoretical pI |
9.94 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Lipid transport and metabolism |
| Enzyme 22 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 22 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 22 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
862458  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P55084  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
ECHB_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
|
| Enzyme 22 GenBank Gene ID |
D16481  |
| Enzyme 22 GeneCard ID |
HADHB  |
| Enzyme 22 GenAtlas ID |
HADHB  |
| Enzyme 22 HGNC ID |
HGNC:4803  |
| Enzyme 22 Chromosome Location |
2 |
| Enzyme 22 Locus |
2p23 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed
]
- Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5278 |
| Enzyme 23 Name |
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial precursor |
| Enzyme 23 Synonyms |
- AKB ligase
- Glycine acetyltransferase
- Aminoacetone synthetase
|
| Enzyme 23 Gene Name |
GCAT |
| Enzyme 23 Protein Sequence |
>2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial precursor
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
|
| Enzyme 23 Number of Residues |
419 |
| Enzyme 23 Molecular Weight |
45286 |
| Enzyme 23 Theoretical pI |
8.11 |
| Enzyme 23 GO Classification |
| Function |
- C-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- glycine C-acetyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Coenzyme transport and metabolism |
| Enzyme 23 Specific Function |
Acetyl-CoA + glycine = CoA + 2-amino-3- oxobutanoate |
| Enzyme 23 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 23 Reactions |
- acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
Not Available |
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
3342906  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
O75600  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
KBL_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1260 bp
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCCGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTCAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATTCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTTAGC
TCGGTCCGCTTCATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACCGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGTTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCACTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCAGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGATCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
|
| Enzyme 23 GenBank Gene ID |
AF077740  |
| Enzyme 23 GeneCard ID |
GCAT  |
| Enzyme 23 GenAtlas ID |
GCAT  |
| Enzyme 23 HGNC ID |
HGNC:4188  |
| Enzyme 23 Chromosome Location |
22 |
| Enzyme 23 Locus |
22q13.1 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem. 2000 Mar;267(6):1805-12. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5279 |
| Enzyme 24 Name |
Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor |
| Enzyme 24 Synonyms |
- PDHE1-A type II
|
| Enzyme 24 Gene Name |
PDHA2 |
| Enzyme 24 Protein Sequence |
>Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS
|
| Enzyme 24 Number of Residues |
388 |
| Enzyme 24 Molecular Weight |
42934 |
| Enzyme 24 Theoretical pI |
8.56 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Energy production and conversion |
| Enzyme 24 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
Not Available |
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
190790  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P29803  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
ODPAT_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1167 bp
ATGCTGGCCGCCTTCATCTCCCGCGTGTTGAGGCGAGTTGCCCAGAAATCAGCTCGCAGA
GTGCTGGTGGCATCCCGTAACTCCTCAAATGACGCTACATTTGAAATTAAGAAATGTGAT
CTTTATCTGTTGGAAGAGGGTCCCCCTGTCACTACAGTGCTCACTAGGGCGGAGGGGCTT
AAATACTACAGGATGATGCTGACTGTTCGCCGCATGGAATTGAAGGCAGATCAGCTGTAC
AAACAGAAATTCATTCGCGGTTTCTGTCACCTGTGCGATGGTCAGGAAGCTTGTTGCGTG
GGCCTTGAGGCCGGCATAAACCCCTCGGATCACGTCATTACATCCTATAGGGCTCATGGT
GTGTGCTATACTCGGGGACTTTCTGTCCGATCCATTCTCGCAGAGCTGACGGGAAGAAGA
GGAGGTTGTGCTAAAGGAAAAGGAGGATCGATGCATATGTATACCAAGAACTTCTATGGG
GGCAATGGCATCGTCGGTGCACAGGGCCCCCTGGGCGCTGGCATTGCTCTGGCCTGTAAA
TATAAAGGAAACGATGAGATCTGTTTGACTTTATATGGGGATGGCGCTGCGAATCAGGGG
CAGATAGCCGAAGCTTTCAATATGGCAGCTTTATGGAAATTACCTTGTGTTTTCATCTGT
GAGAATAACCTATATGGAATGGGAACATCTACTGAGAGAGCAGCAGCCAGCCCTGATTAC
TACAAGAGGGGCAATTTTATCCCTGGGCTAAAGGTCGATGGAATGGATGTTCTGTGTGTT
CGTGAGGCAACAAAATTTGCAGCTAACTACTGTAGATCTGGAAAGGGGCCCATACTGATG
GAGCTGCAAACCTACCGTTATCATGGACACAGTATGAGTGATCCTGGAGTCAGTTATCGT
ACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGGGATCCTATAATAATTCTCCAAGAT
AGAATGGTAAACAGCAAGCTCGCCACTGTGGAAGAATTAAAGGAAATTGGGGCTGAGGTG
AGGAAAGAAATTGATGATGCTGCCCAGTTTGCTACCACTGATCCTGAGCCACATTTGGAA
GAATTAGGCCATCACATCTACAGCAGTGATTCATCTTTTGAAGTTCGTGGTGCAAATCCA
TGGATCAAGTTTAAGTCCGTCAGTTAA
|
| Enzyme 24 GenBank Gene ID |
M86808  |
| Enzyme 24 GeneCard ID |
PDHA2  |
| Enzyme 24 GenAtlas ID |
PDHA2  |
| Enzyme 24 HGNC ID |
HGNC:8807  |
| Enzyme 24 Chromosome Location |
4 |
| Enzyme 24 Locus |
4q22-q23 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK: A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4. Genomics. 1990 Oct;8(2):225-32. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5281 |
| Enzyme 25 Name |
Glucosamine 6-phosphate N-acetyltransferase |
| Enzyme 25 Synonyms |
- Phosphoglucosamine transacetylase
- Phosphoglucosamine acetylase
|
| Enzyme 25 Gene Name |
GNPNAT1 |
| Enzyme 25 Protein Sequence |
>Glucosamine 6-phosphate N-acetyltransferase
MKPDETPMFDPSLLKEVDWSQNTATFSPAISPTHPGEGLVLRPLCTADLNRGFFKVLGQL
TETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVE
DVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENYMCR
RFLK
|
| Enzyme 25 Number of Residues |
184 |
| Enzyme 25 Molecular Weight |
20749 |
| Enzyme 25 Theoretical pI |
8.12 |
| Enzyme 25 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 25 General Function |
Transcription |
| Enzyme 25 Specific Function |
Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
21748766  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q96EK6  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
GNA1_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>555 bp
ATGAAACCTGATGAAACTCCTATGTTTGACCCAAGTCTACTCAAAGAAGTGGACTGGAGT
CAGAATACAGCTACATTTTCTCCAGCCATTTCCCCAACACATCCTGGAGAAGGCTTGGTT
TTGAGGCCTCTTTGTACTGCTGACTTAAATAGAGGTTTTTTTAAGGTATTGGGTCAGCTA
ACAGAGACTGGAGTTGTCAGCCCTGAACAATTTATGAAATCTTTTGAGCATATGAAGAAA
TCTGGGGATTATTATGTTACAGTTGTAGAAGATGTGACTCTAGGACAGATTGTTGCTACG
GCAACTCTGATTATAGAACATAAATTCATCCATTCCTGTGCTAAGAGAGGAAGAGTAGAA
GATGTTGTTGTTAGTGATGAATGCAGAGGAAAGCAGCTTGGCAAATTGTTATTATCAACC
CTTACTTTGCTAAGCAAGAAACTGAACTGTTACAAGATTACCCTTGAATGTCTACCACAA
AATGTTGGTTTCTATAAAAAGTTTGGATATACTGTATCTGAAGAAAACTACATGTGTCGG
AGGTTTCTAAAGTAA
|
| Enzyme 25 GenBank Gene ID |
AK090577  |
| Enzyme 25 GeneCard ID |
GNPNAT1  |
| Enzyme 25 GenAtlas ID |
GNPNAT1  |
| Enzyme 25 HGNC ID |
HGNC:19980  |
| Enzyme 25 Chromosome Location |
14 |
| Enzyme 25 Locus |
14q22.2 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5284 |
| Enzyme 26 Name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor |
| Enzyme 26 Synonyms |
- Pyruvate dehydrogenase complex E2 subunit
- PDCE2
- E2
- Dihydrolipoamide S- acetyltransferase component of pyruvate dehydrogenase complex
- PDC- E2
- 70 kDa mitochondrial autoantigen of primary biliary cirrhosis
- PBC
- M2 antigen complex 70 kDa subunit
|
| Enzyme 26 Gene Name |
DLAT |
| Enzyme 26 Protein Sequence |
>Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
MSPHCSTTYLRTLGRTTMFWKTTEGRDGKMAVQEFSEFGLLLQLLGSPGRRYYSLPPHQK
VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEG
TRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGS
SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLA
KILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTP
QPLAPTPSTPCPATPAGPKGRVFVDPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV
PSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN
MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV
AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGI
KNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLA
EFRKYLEKPITMLL
|
| Enzyme 26 Number of Residues |
614 |
| Enzyme 26 Molecular Weight |
65782 |
| Enzyme 26 Theoretical pI |
5.95 |
| Enzyme 26 GO Classification |
| Function |
- S-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- dihydrolipoyllysine-residue acetyltransferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- protein complex
- pyruvate dehydrogenase complex
|
|
| Enzyme 26 General Function |
Energy production and conversion |
| Enzyme 26 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
35360  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P10515  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
ODP2_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1848 bp
CGAGTGACCTCGCGATCTGGCCCGGCTCCCGCTCGTCGCAACAGCGTGACTACAGGGTAT
GGCGGGGTCCGGGCACTGTGCGGCTGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGC
TTACTGCTGCAGCTTTTGGGGTCGCCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAG
AAGGTTCCATTGCCTTCTCTTTCCCCCACAATGCAGGCAGGCACCATAGCCCGTTGGAAA
AAAAAAGAGGGGGACAAAATCAATGAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAA
GCCACTGTTGGATTTGAGAGCCTGGAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAA
GGTACCAGGGATGTTCCCATCGGAGCGATCATCTGTATCACAGTTGGCAAGCCTGAGGAT
ATTGAGGCCTTTAAAAATTATACACTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCC
CCAGCACCAACCCCTGCTGCCACTGCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGT
AGCTCATATCCCCCTCACATGCAGGTACTTCTTCCTGCCCTCTCTCCCACCATGACCATG
GGCACAGTTCAGAGATGGGAAAAAAAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTG
GCAGAGATAGAAACTGACAAAGCCACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTG
GCAAAAATCCTGGTCCCTGAAGGCACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATC
ATTGTAGAAAAAGAGGCAGATATATCAGCATTTGCTGACTATAGGCCAACCGAAGTAACA
GATTTAAAACCACAAGTGCCACCACCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACT
CCCCAGCCTTTAGCTCCTACACCTTCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAG
GGAAGGGTGTTTGTTAGCCCTCTTGCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTT
ACACAAGTAAAAGGGACAGGACCAGATGGTAGAATCACCAAGAAGGATATCGACTCTTTT
GTGCCTAGTAAAGTTGCTCCTGCTCCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATG
GCACCAGTTCCTACAGGTGTCTTCACAGATATCCCAATCAGCAACATTCGTCGGGTTATT
GCACAGCGATTAATGCAATCAAAGCAAACCATACCTCATTATTACCTTTCTATCGATGTA
AATATGGGAGAAGTTTTGTTGGTACGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGC
AAAATTTCTGTCAATGACTTCATCATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCC
GAAGCAAATTCTTCTTGGATGGACACAGTTATAAGACAAAATCATGTTGTTGATGTCAGT
GTTGCGGTCAGTACTCCTGCAGGACTCATCACACCTATTGTGTTTAATGCACATATAAAA
GGAGTGGAAACCATTGCTAATGATGTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAA
CTACAGCCACATGAATTCCAGGGTGGCACTTTTACGATCTCCAATTTAGGAATGTTTGGA
ATTAAGAATTTCTCTGCTATTATTAACCCACCTCAAGCATGTATTTTGGCAATTGGTGCT
TCAGAGGATAAACTGGTCCCTGCAGATAATGAAAAAGGGTTTGATGTGGCTAGCATGATG
TCTGTTACACTCAGTTGTGATCACCGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTT
GCTGAGTTTAGAAAGTACCTTGAAAAACCTATCACTATGTTGTTGTAA
|
| Enzyme 26 GenBank Gene ID |
Y00978  |
| Enzyme 26 GeneCard ID |
DLAT  |
| Enzyme 26 GenAtlas ID |
DLAT  |
| Enzyme 26 HGNC ID |
HGNC:2896  |
| Enzyme 26 Chromosome Location |
11 |
| Enzyme 26 Locus |
11q23.1 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed
]
- Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed
]
- Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5542 |
| Enzyme 27 Name |
Peroxisomal carnitine O-octanoyltransferase |
| Enzyme 27 Synonyms |
- COT
|
| Enzyme 27 Gene Name |
CROT |
| Enzyme 27 Protein Sequence |
>Peroxisomal carnitine O-octanoyltransferase
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
|
| Enzyme 27 Number of Residues |
612 |
| Enzyme 27 Molecular Weight |
70179 |
| Enzyme 27 Theoretical pI |
7.09 |
| Enzyme 27 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl- CoA, to its corresponding carnitine ester |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
- octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
6066280  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q9UKG9  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
OCTC_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1839 bp
ATGGAAAATCAATTGGCTAAATCAACTGAAGAACGAACATTTCAGTACCAGGATTCTCTT
CCATCACTGCCTGTTCCTTCACTTGAAGAATCATTAAAAAAATACCTTGAATCAGTGAAA
CCATTTGCAAATCAAGAAGAATATAAGAAAACTGAAGAAATAGTTCAAAAATTTCAAAGT
GGGATTGGAGAAAAATTGCACCAGAAATTGCTTGAAAGAGCAAAAGGAAAAAGAAATTGG
CTGGAAGAGTGGTGGCTGAATGTTGCCTATCTGGATGTTCGTATACCATCACAATTGAAT
GTCAACTTTGCGGGTCCTGCAGCTCATTTTGAACACTACTGGCCTCCAAAGGAAGGGACT
CAATTAGAAAGAGGAAGTATAACTCTTTGGCATAACTTGAACTACTGGCAGCTATTAAGA
AAAGAAAAGTTGCCTGTTCATAAAGTTGGAAATACTCCTCTAGATATGAATCAATTCCGA
ATGCTATTTTCTACCTGCAAGGTTCCAGGAATTACTAGAGACTCCATTATGAATTATTTT
AGGACTGAGAGTGAAGGGCGTTCCCCAAACCACATTGTAGTGCTGTGTCGAGGCCGAGCT
TTTGTCTTTGATGTAATACATGAAGGATGTTTGGTCACCCCGCCAGAGCTTCTCAGACAA
CTGACATATATCCACAAGAAGTGCCATAGTGAACCTGATGGACCTGGGATTGCAGCATTA
ACTAGTGAGGAGCGAACTCGATGGGCTAAGGCACGAGAATATCTGATTGGTCTTGATCCA
GAGAACTTGGCTTTGTTAGAAAAAATTCAGAGTAGTTTACTGGTATATTCCATGGAGGAT
AGCAGTCCACATGTAACACCAGAGGATTATTCTGAGATTATTGCAGCCATCCTTATTGGA
GATCCAACAGTACGCTGGGGTGACAAATCCTATAACTTGATTTCCTTTTCTAATGGAGTA
TTTGGCTGTAATTGTGATCATGCTCCTTTTGATGCAATGATTATGGTGAACATCAGTTAT
TATGTGGATGAGAAAATTTTTCAGAATGAAGGAAGATGGAAGGGTTCAGAGAAGGTACGA
GATATACCACTTCCAGAAGAGCTCATTTTCATTGTGGATGAGAAAGTTTTAAATGACATC
AACCAAGCTAAAGCCCAGTATCTCAGGGAGGCATCTGATCTACAGATTGCGGCTTATGCC
TTTACATCTTTTGGCAAAAAGCTAACCAAGAACAAGATGCTTCACCCGGATACGTTTATT
CAGCTTGCACTTCAGCTGGCCTATTACAGACTTCATGGACACCCTGGTTGTTGCTATGAA
ACAGCTATGACAAGACATTTTTATCATGGCCGTACAGAGACTATGCGATCATGCACAGTT
GAAGCAGTGAGGTGGTGCCAGTCCATGCAGGATCCTTCTGTCAATCTTCGTGAGCGGCAG
CAAAAGATGTTACAAGCTTTTGCAAAGCATAATAAAATGATGAAAGATTGTTCAGCTGGA
AAAGGATTTGATCGTCACCTTTTAGGTCTCTTACTCATAGCAAAAGAGGAAGGTCTTCCT
GTTCCAGAACTCTTTACGGACCCACTTTTTTCCAAAAGCGGAGGAGGTGGAAATTTTGTT
CTCTCAACAAGTCTGGTTGGCTATTTACGAGTCCAGGGAGTGGTAGTTCCCATGGTACAC
AATGGTTATGGATTTTTCTACCATATCAGAGATGACAGGTTTGTTGTGGCCTGTTCAGCC
TGGAAATCCTGTCCCGAGACTGATGCGGAAAAGCTAGTTCAGCTGACTTTTTGTGCTTTT
CATGATATGATACAGCTGATGAACTCTACTCATCTTTAG
|
| Enzyme 27 GenBank Gene ID |
AF168793  |
| Enzyme 27 GeneCard ID |
CROT  |
| Enzyme 27 GenAtlas ID |
CROT  |
| Enzyme 27 HGNC ID |
HGNC:2366  |
| Enzyme 27 Chromosome Location |
7 |
| Enzyme 27 Locus |
7q21.1 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Ferdinandusse S, Mulders J, IJlst L, Denis S, Dacremont G, Waterham HR, Wanders RJ: Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids. Biochem Biophys Res Commun. 1999 Sep 16;263(1):213-8. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5543 |
| Enzyme 28 Name |
Carnitine O-palmitoyltransferase I, muscle isoform |
| Enzyme 28 Synonyms |
- CPT I
- CPTI-M
- Carnitine palmitoyltransferase 1B
- Carnitine palmitoyltransferase I-like protein
|
| Enzyme 28 Gene Name |
CPT1B |
| Enzyme 28 Protein Sequence |
>Carnitine O-palmitoyltransferase I, muscle isoform
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
|
| Enzyme 28 Number of Residues |
772 |
| Enzyme 28 Molecular Weight |
87802 |
| Enzyme 28 Theoretical pI |
8.77 |
| Enzyme 28 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
1621202  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q92523  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
CPT1B_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>2319 bp
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCTCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTGCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGC
AAGGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCGAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
|
| Enzyme 28 GenBank Gene ID |
D87812  |
| Enzyme 28 GeneCard ID |
CPT1B  |
| Enzyme 28 GenAtlas ID |
CPT1B  |
| Enzyme 28 HGNC ID |
HGNC:2329  |
| Enzyme 28 Chromosome Location |
22 |
| Enzyme 28 Locus |
22q13.33 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Yamazaki N, Shinohara Y, Shima A, Yamanaka Y, Terada H: Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1996 Jun 7;1307(2):157-61. [PubMed
]
- Zhu H, Shi J, de Vries Y, Arvidson DN, Cregg JM, Woldegiorgis G: Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. Arch Biochem Biophys. 1997 Nov 1;347(1):53-61. [PubMed
]
- Britton CH, Mackey DW, Esser V, Foster DW, Burns DK, Yarnall DP, Froguel P, McGarry JD: Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Genomics. 1997 Feb 15;40(1):209-11. [PubMed
]
- van der Leij FR, Takens J, van der Veen AY, Terpstra P, Kuipers JR: Localization and intron usage analysis of the human CPT1B gene for muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1997 May 30;1352(2):123-8. [PubMed
]
- Yamazaki N, Yamanaka Y, Hashimoto Y, Shinohara Y, Shima A, Terada H: Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I. FEBS Lett. 1997 Jun 16;409(3):401-6. [PubMed
]
- Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5544 |
| Enzyme 29 Name |
Carnitine O-palmitoyltransferase I, liver isoform |
| Enzyme 29 Synonyms |
- CPT I
- CPTI-L
- Carnitine palmitoyltransferase 1A
|
| Enzyme 29 Gene Name |
CPT1A |
| Enzyme 29 Protein Sequence |
>Carnitine O-palmitoyltransferase I, liver isoform
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPS
SWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIV
TMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVK
DTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYI
YLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGST
IPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREME
QQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTL
DETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPI
VAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLL
ANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREG
RTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCL
YVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGGGFGPVADDGY
GVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK
|
| Enzyme 29 Number of Residues |
773 |
| Enzyme 29 Molecular Weight |
88369 |
| Enzyme 29 Theoretical pI |
8.84 |
| Enzyme 29 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
755646  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P50416  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
CPT1A_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>2322 bp
ATGGCAGAAGCTCACCAAGCTGTGGCCTTTCAGTTCACGGTCACTCCGGACGGGATTGAC
CTGCGGCTGAGCCATGAAGCTCTTAGACAAATCTATCTCTCTGGACTTCATTCCTGGAAA
AAGAAGTTCATCAGATTCAAGAACGGCATCATCACTGGCGTGTACCCGGCAAGCCCCTCC
AGTTGGCTTATCGTGGTGGTGGGCGTGATGACAACGATGTACGCCAAGATCGACCCCTCG
TTAGGAATAATTGCAAAAATCAATCGGACTCTGGAAACGGCCAACTGCATGTCCAGCCAG
ACGAAGAACGTGGTCAGCGGCGTGCTGTTTGGCACCGGCCTGTGGGTGGCCCTCATCGTC
ACCATGCGCTACTCCCTGAAAGTGCTGCTCTCCTACCACGGGTGGATGTTCACTGAGCAC
GGCAAGATGAGTCGTGCCACCAAGATCTGGATGGGTATGGTCAAGATCTTTTCAGGCCGA
AAACCCATGTTGTACAGCTTCCAGACATCGCTGCCTCGCCTGCCGGTCCCGGCTGTCAAA
GACACTGTGAACAGGTATCTACAGTCGGTGAGGCCTCTTATGAAGGAAGAAGACTTCAAA
CGGATGACAGCACTTGCTCAAGATTTTGCTGTCGGTCTTGGACCAAGATTACAGTGGTAT
TTGAAGTTAAAATCCTGGTGGGCTACAAATTACGTGAGCGACTGGTGGGAGGAGTACATC
TACCTCCGAGGACGAGGGCCGCTCATGGTGAACAGCAACTATTATGCCATGGATCTGCTG
TATATCCTTCCAACTCACATTCAGGCAGCAAGAGCCGGCAACGCCATCCATGCCATCCTG
CTTTACAGGCGCAAACTGGACCGGGAGGAAATCAAACCAATTCGTCTTTTGGGATCCACG
ATTCCACTCTGCTCCGCTCAGTGGGAGCGGATGTTTAATACTTCCCGGATCCCAGGAGAG
GAGACAGACACCATCCAGCACATGAGAGACAGCAAGCACATCGTCGTGTACCATCGAGGA
CGCTACTTCAAGGTCTGGCTCTACCATGATGGGCGGCTGCTGAAGCCCCGGGAGATGGAG
CAGCAGATGCAGAGGATCCTGGACAATACCTCGGAGCCTCAGCCCGGGGAGGCCAGGCTG
GCAGCCCTCACCGCAGGAGACAGAGTTCCCTGGGCCAGGTGTCGTCAGGCCTATTTTGGA
CGTGGGAAAAATAAGCAGTCTCTTGATGCTGTGGAGAAAGCAGCGTTCTTCGTGACGTTA
GATGAAACTGAAGAAGGATACAGAAGTGAAGACCCGGATACGTCAATGGACAGCTACGCC
AAATCTCTACTACACGGCCGATGTTACGACAGGTGGTTTGACAAGTCGTTCACGTTTGTT
GTCTTCAAAAACGGGAAGATGGGCCTCAACGCTGAACACTCCTGGGCAGATGCGCAGATC
GTGGCCCACCTTTGGGAGTACGTCATGTCCATTGACAGCCTCCAGCTGGGCTATGCGGAG
GATGGGCACTGCAAAGGCGACATCAATCCGAACATTCCGTACCCCACCAGGCTGCAGTGG
GACATCCCGGGGGAATGTCAAGAGGTTATAGAGACCTCCCTGAACACCGCAAATCTTCTG
GCAAACGACGTGGATTTCCATTCCTTCCCATTCGTAGCCTTTGGTAAAGGAATCATCAAG
AAATGTCGCACGAGCCCAGACACCTTTGTGCAGCTGGCCCTCCAGCTGGCGCACTACAAG
GACATGGGCAAGTTTTGCCTCACATACGAGGCCTCCATGACCCGGCTCTTCCGAGAGGGG
AGGACGGAGACCGTGCGCTCCTGCACCACTGAGTCATGCGACTTCGTGCGGGCCATGGTG
GACCCGGCCCAGACGGTGGAACAGAGGCTGAAGTTGTTCAAGTTGGCGTCTGAGAAGCAT
CAGCATATGTATCGCCTCGCCATGACCGGCTCTGGGATCGATCGTCACCTCTTCTGCCTT
TACGTGGTGTCTAAATATCTCGCTGTGGAGTCCCCTTTCCTTAAGGAAGTTTTATCTGAG
CCTTGGAGATTATCAACAAGCCAGACCCCTCAGCAGCAAGTGGAGCTGTTTGACTTGGAG
AATAACCCAGAGTACGTGTCCAGCGGAGGGGGCTTTGGACCGGTTGCTGATGACGGCTAT
GGTGTGTCGTACATCCTTGTGGGAGAGAACCTCATCAATTTCCACATTTCTTCCAAGTTC
TCTTGCCCTGAGACGGATTCTCATCGCTTTGGAAGGCACCTGAAAGAAGCAATGACTGAC
ATCATCACTTTGTTTGGTCTCAGTTCTAATTCCAAAAAGTAA
|
| Enzyme 29 GenBank Gene ID |
L39211  |
| Enzyme 29 GeneCard ID |
CPT1A  |
| Enzyme 29 GenAtlas ID |
CPT1A  |
| Enzyme 29 HGNC ID |
HGNC:2328  |
| Enzyme 29 Chromosome Location |
11 |
| Enzyme 29 Locus |
11q13.1-q13.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Britton CH, Schultz RA, Zhang B, Esser V, Foster DW, McGarry JD: Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):1984-8. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5677 |
| Enzyme 30 Name |
2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor |
| Enzyme 30 Synonyms |
- Alpha-ketoglutarate dehydrogenase
|
| Enzyme 30 Gene Name |
OGDH |
| Enzyme 30 Protein Sequence |
>2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFEAGLRMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRNPAAAPATGNKKTH
|
| Enzyme 30 Number of Residues |
1002 |
| Enzyme 30 Molecular Weight |
113477 |
| Enzyme 30 Theoretical pI |
7.08 |
| Enzyme 30 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
- oxoglutarate dehydrogenase (succinyl-transferring) activity
- thiamin pyrophosphate binding
- vitamin binding
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Energy production and conversion |
| Enzyme 30 Specific Function |
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
531241  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q02218  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
ODO1_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>3009 bp
ATGTTTCATTTAAGGACTTGTGCTGCTAAGTTGAGGCCATTGACGGCTTCCCAGACTGTT
AAGACATTTTCACAAAACAGACCAGCAGCAGCTAGGACATTTCAACAGATTCGGTGCTAT
TCTGCACCTGTTGCTGCTGAGCCCTTTCTCAGTGGGACTAGTTCGAACTATGTGGAGGAG
ATGTACTGTGCTTGGCTGGAAAACCCCAAAAGTGTACATAAGTCATGGGACATTTTTTTT
CGCAACACGAATGCCGGAGCCCCACCGGGCACTGCCTACCAGAGTCCCCTTCCCCTGAGC
CGAGGCTCCCTGGCTGCTGTGGCCCATGCACAGTCCCTGGTAGAAGCACAGCCCAACGTG
GACAAGCTCGTGGAGGACCACCTGGCAGTGCAGTCACTCATCAGGGCATATCAGATACGA
GGGCACCATGTAGCACAGCTGGACCCCCTGGGGATTTTGGATGCTGATCTGGACTCCTCC
GTGCCCGCTGACATTATCTCATCCACAGACAAACTTGGGTTCTATGGCCTGGATGAGTCT
GACCTCGACAAGGTCTTCCACTTGCCCACCACCACTTTCATCGGGGGACAGGAATCAGCA
CTTCCTCTGCGGGAGATCATCCGTCGGCTGGAGATGGCCTACTGCCAGCATATTGGGGTG
GAGTTCATGTTCATCAATGACCTGGAGCAGTGCCAGTGGATCCGGCAGAAGTTTGAGACC
CCTGGGATCATGCAGTTCACAAATGAGGAGAAACGGACCCTGCTGGCCAGGCTTGTGCGG
TCCACCAGGTTTGAGGAGTTCCTACAGCGGAAGTGGTCCTCTGAGAAGCGCTTTGGTCTA
GAAGGCTGCGAGGTACTGATCCCTGCCCTCAAGACCATCATTGACAAGTCTAGTGAGAAT
GGCGTGGACTACGTGATCATGGGCATGCCACACAGAGGGCGGCTGAACGTGCTTGCAAAT
GTCATCAGGAAGGAGCTGGAACAGATCTTCTGTCAATTCGATTCAAAGCTGGAGGCAGCT
GATGAGGGCTCCGGAGATGTGAAGTACCACCTGGGCATGTATCACCGCAGGATCAATCGT
GTCACCGACAGGAACATTACCTTGTCCTTGGTGGCCAACCCTTCCCACCTTGAGGCCGCT
GACCCCGTGGTGATGGGCAAGACCAAAGCCGAACAGTTTTACTGTGGCGACACTGAAGGG
AAAAAGGTCATGTCCATCCTGTTGCATGGGGATGCTGCATTTGCTGGCCAGGGCATTGTG
TACGAGACCTTCCACCTCAGCGACCTGCCATCCTACACAACTCATGGCACCGTGCACGTG
GTCGTCAACAACCAGATCGGCTTCACCACCGACCCTCGGATGGCCCGCTCCTCCCCCTAC
CCCACTGACGTGGCCCGAGTGGTGAATGCCCCCATTTTCCACGTGAACTCAGATGACCCC
GAGGCTGTCATGTACGTGTGCAAAGTGGCGGCCGAGTGGAGGAGCACCTTCCACAAGGAC
GTGGTTGTCGATTTGGTGTGTTACCGGCGCAACGGCCACAACGAGATGGATGAGCCCATG
TTCACGCAGCCGCTCATGTACAAGCAGATCCGCAAGCAGAAGCCTGTGTTACAGAAGTAC
GCTGAGCTGCTGGTGTCGCAGGGTGTGGTCAACCAGCCTGAGTATGAGGAGGAAATTTCC
AAGTATGATAAGATCTGTGAGGAAGCTTTTGCCAGATCTAAAGATGAGAAGATCTTGCAC
ATTAAGCACTGGCTGGACTCTCCCTGGCCTGGCTTCTTCACCCTGGACGGGCAGCCCAGG
AGCATGTCCTGCCCCTCCACGGGTCTGACGGAGGATATTCTGACACACATCGGGAATGTG
GCTAGTTCTGTGCCTGTGGAAAACTTTACTATTCATGGAGGGCTGAGCCGGATCTTGAAG
ACTCGTGGGGAAATGGTGAAGAACCGGACTGTGGACTGGGCTCTAGCGGAGTACATGGCG
TTTGGCTCGCTCCTGAAGGAGGGCATCCACATTCGGCTGAGCGGCCAGGACGTGGAGCGG
GGCACATTCAGCCACCGCCACCATGTGCTCCATGACCAGAATGTGGACAAGAGAACCTGC
ATCCCCATGAACCATCTCTGGCCCAATCAGGCCCCCTATACTGTGTGCAACAGCTCACTG
TCTGAGTACGGCGTGCTGGGCTTTGAAGCTGGGCTTCGCATGGCCAGTCCTAATGCCCTG
GTCCTCTGGGAAGCCCAATTTGGTGACTTCCACAACACGGCCCAGTGTATCATCGACCAG
TTCATCTGCCCGGGACAAGCCAAGTGGGTGCGGCAGAATGGCATCGTGTTGCTGCTGCCC
CATGGCATGGAGGGCATGGGTCCAGAACATTCCTCCGCCCGCCCAGAGCGGTTCTTGCAG
ATGTGCAACGATGACCCAGATGTCCTGCCAGACCTTAAAGAAGCCAACTTCGACATCAAT
CAGCTATATGACTGCAATTGGGTTGTTGTCAACTGCTCCACTCCTGGCAACTTCTTCCAC
GTGCTACGACGCCAGATCCTGCTGCCATTCCGGAAGCCGTTAATTATCTTCACCCCCAAA
TCCCTGTTGCGCCACCCCGAGGCCAGATCCAGCTTTGATGAGATGCTTCCAGGAACCCAC
TTCCAGCGGGTGATCCCAGAAGATGGCCCTGCAGCTCAGAACCCAGAAAATGTCAAAAGG
CTTCTCTTCTGCACCGGCAAAGTGTATTATGACCTCACCCGGGAGCGCAAAGCACGCGAC
ATGGTGGGGCAGGTGGCCATCACAAGGATTGAGCAGCTGTCGCCATTCCCCTTTGACCTC
CTGCTGAAGGAGGTGCAGAAGTACCCCAATGCTGAGCTGGCCTGGTGCCAGGAGGAGCAC
AAGAACCAAGGCTACTATGACTACGTGAAGCCAAGACTTCGGACCACCATCAGCCGCGCC
AAGCCCGTCTGGTATGCCGGCCGGAACCCAGCGGCTGCTCCAGCCACCGGCAACAAGAAG
ACCCACTGA
|
| Enzyme 30 GenBank Gene ID |
D10523  |
| Enzyme 30 GeneCard ID |
OGDH  |
| Enzyme 30 GenAtlas ID |
OGDH  |
| Enzyme 30 HGNC ID |
HGNC:8124  |
| Enzyme 30 Chromosome Location |
7 |
| Enzyme 30 Locus |
7p14-p13 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Koike K, Urata Y, Goto S: Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1963-7. [PubMed
]
- Koike K: The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14. Gene. 1995 Jul 4;159(2):261-6. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5746 |
| Enzyme 31 Name |
Sterol O-acyltransferase 2 |
| Enzyme 31 Synonyms |
- Cholesterol acyltransferase 2
- Acyl coenzyme A:cholesterol acyltransferase 2
- ACAT-2
|
| Enzyme 31 Gene Name |
SOAT2 |
| Enzyme 31 Protein Sequence |
>Sterol O-acyltransferase 2
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQL
RELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHF
RTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLA
PYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFL
MKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKN
FAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLH
CWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARG
VAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTM
LFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
|
| Enzyme 31 Number of Residues |
522 |
| Enzyme 31 Molecular Weight |
59897 |
| Enzyme 31 Theoretical pI |
8.71 |
| Enzyme 31 GO Classification |
Not Available |
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- acyl-CoA + cholesterol = CoA + cholesterol ester
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 124-144
155-175
200-220
262-282
304-324
344-366
437-457
472-492
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
3746535  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
O75908  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
SOAT2_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1569 bp
ATGGAGCCAGGCGGGGCCCGTCTGCGTCTGCAGAGGACAGAAGGGCTGGGAGGGGAGCGG
GAGCGCCAACCCTGTGGAGATGGAAACACTGAGACGCACAGAGCCCCGGACTTGGTACAA
TGGACCCGACACATGGAGGCTGTGAAGGCACAATTGCTGGAGCAAGCGCAGGGACAACTG
AGGGAGCTGCTGGATCGGGCCATGCGGGAGGCTATACAATCCTACCCATCACAAGACAAA
CCTCTGCCCCCACCTCCCCCAGGTTCCTTGAGCAGGACCCAGGAGCCATCCCTGGGGAAA
CAGAAAGTTTTCATCATCCGCAAGTCCCTGCTTGATGAGCTGATGGAGGTGCAGCATTTC
CGCACCATCTACCACATGTTCATCGCTGGCCTGTGTGTCTTCATCATCAGCACCCTGGCC
ATCGACTTCATTGATGAGGGCAGGCTGCTGCTGGAGTTTGACCTACTGATCTTCAGCTTC
GGACAGCTGCCATTGGCGCTGGTGACCTGGGTGCCCATGTTTCTGTCCACCCTGTTGGCG
CCGTACCAGGCCCTACGGCTGTGGGCCAGGGGCACCTGGACGCAGGCGACGGGCCTGGGC
TGTGCGCTGCTAGCCGCCCACGCCGTGGTGCTCTGCGCGCTGCCGGTCCACGTGGCCGTG
GAGCATCAGCTCCCGCCGGCCTCCCGTTGTGTCCTGGTCTTCGAGCAGGTTAGGTTCCTG
ATGAAAAGCTACTCCTTCCTGAGAGAGGCTGTGCCTGGGACCCTTCGTGCCAGACGAGGT
GAGGGGATCCAGGCCCCCAGTTTCTCCAGCTACCTCTACTTCCTCTTCTGCCCAACACTC
ATCTACAGGGAGACTTACCCTAGGACGCCCTATGTCAGGTGGAATTATGTGGCCAAGAAC
TTTGCCCAGGCCCTGGGATGTGTGCTCTATGCCTGCTTCATCCTGGGCCGCCTCTGTGTT
CCTGTCTTTGCCAACATGAGCCGAGAGCCCTTCAGCACCCGTGCCCTGGTGCTCTCTATC
CTGCATGCCACGTTGCCAGGCATCTTCATGCTGCTGCTCATCTTCTTTGCCTTCCTCCAT
TGCTGGCTCAACGCCTTTGCCGAGATGCTACGATTTGGAGACAGGATGTTCTACCGGGAC
TGGTGGAACTCAACGTCCTTCTCCAACTACTACCGCACTTGGAACGTGGTGGTCCATGAC
TGGCTGTACAGCTACGTGTATCAGGATGGGCTGCGGCTCCTTGGTGCCCGGGCCCGAGGG
GTAGCCATGCTGGGTGTGTTCCTGGTCTCCGCAGTGGCCCATGAGTATATCTTCTGCTTC
GTCCTGGGGTTCTTCTATCCCGTCATGCTGATACTCTTCCTTGTCATTGGAGGAATGTTG
AACTTCATGATGCATGACCAGCGCACCGGCCCGGCATGGAACGTGCTGATGTGGACCATG
CTGTTTCTAGGCCAGGGAATCCAGGTCAGCCTGTACTGCCAGGAGTGGTACGCACGGCGG
CACTGCCCCTTACCCCAGGCAACTTTCTGGGGGCTGGTGACACCTCGATCTTGGTCCTGC
CATACCTAG
|
| Enzyme 31 GenBank Gene ID |
AF059203  |
| Enzyme 31 GeneCard ID |
SOAT2  |
| Enzyme 31 GenAtlas ID |
SOAT2  |
| Enzyme 31 HGNC ID |
HGNC:11178  |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed
]
- Chang CC, Sakashita N, Ornvold K, Lee O, Chang ET, Dong R, Lin S, Lee CY, Strom SC, Kashyap R, Fung JJ, Farese RV Jr, Patoiseau JF, Delhon A, Chang TY: Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine. J Biol Chem. 2000 Sep 8;275(36):28083-92. [PubMed
]
- Katsuren K, Tamura T, Arashiro R, Takata K, Matsuura T, Niikawa N, Ohta T: Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia. Biochim Biophys Acta. 2001 Apr 30;1531(3):230-40. [PubMed
]
- Song BL, Qi W, Yang XY, Chang CC, Zhu JQ, Chang TY, Li BL: Organization of human ACAT-2 gene and its cell-type-specific promoter activity. Biochem Biophys Res Commun. 2001 Mar 30;282(2):580-8. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5751 |
| Enzyme 32 Name |
Sterol O-acyltransferase 1 |
| Enzyme 32 Synonyms |
- Cholesterol acyltransferase 1
- Acyl coenzyme A:cholesterol acyltransferase 1
- ACAT-1
|
| Enzyme 32 Gene Name |
SOAT1 |
| Enzyme 32 Protein Sequence |
>Sterol O-acyltransferase 1
MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEE
LKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGK
IFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGK
FPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPT
YVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYF
LFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSAR
VLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTW
NVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFM
FFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVR
PRSWTCRYVF
|
| Enzyme 32 Number of Residues |
550 |
| Enzyme 32 Molecular Weight |
64735 |
| Enzyme 32 Theoretical pI |
9.18 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 Specific Function |
Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- acyl-CoA + cholesterol = CoA + cholesterol ester
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
- 141-159
320-341
361-382
470-490
498-518
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
4878022  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P35610  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
SOAT1_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1653 bp
ATGGTGGGTGAAGAGAAGATGTCTCTAAGAAACCGGCTGTCAAAGTCCAGGGAAAATCCT
GAGGAAGATGAAGACCAGAGAAACCCTGCAAAGGAGTCCCTAGAGACACCTAGTAATGGT
CGAATTGACATAAAACAGTTGATAGCAAAGAAGATAAAGTTGACAGCAGAGGCAGAGGAA
TTGAAGCCATTTTTTATGAAGGAAGTTGGCAGTCACTTTGATGATTTTGTGACCAATCTC
ATTGAAAAGTCAGCATCATTAGATAATGGTGGGTGCGCTCTCACAACCTTTTCTGTTCTT
GAAGGAGAGAAAAACAACCATAGAGCGAAGGATTTGAGAGCACCTCCAGAACAAGGAAAG
ATTTTTATTGCAAGGCGCTCTCTCTTAGATGAACTGCTTGAAGTGGACCACATCAGAACA
ATATATCACATGTTTATTGCCCTCCTCATTCTCTTTATCCTCAGCACACTTGTAGTAGAT
TACATTGATGAAGGAAGGCTGGTGCTTGAGTTCAGCCTCCTGTCTTATGCTTTTGGCAAA
TTTCCTACCGTTGTTTGGACCTGGTGGATCATGTTCCTGTCTACATTTTCAGTTCCCTAT
TTTCTGTTTCAACATTGGGCCACTGGCTATAGCAAGAGTTCTCATCCGCTGATCCGTTCT
CTCTTCCATGGCTTTCTTTTCATGATCTTCCAGATTGGAGTTCTAGGTTTTGGACCAACA
TATGTTGTGTTAGCATATACACTGCCACCAGCTTCCCGGTTCATCATTATATTCGAGCAG
ATTCGTTTTGTAATGAAGGCCCACTCATTTGTCAGAGAGAACGTGCCTCGGGTACTAAAT
TCAGCTAAGGAGAAATCAAGCACTGTTCCAATACCTACAGTCAACCAGTATTTGTACTTC
TTATTTGCTCCTACCCTTATCTACCGTGACAGCTATCCCAGGAATCCCACTGTAAGATGG
GGTTATGTCGCTATGAAGTTTGCACAGGTCTTTGGTTGCTTTTTCTATGTGTACTACATC
TTTGAAAGGCTTTGTGCCCCCTTGTTTCGGAATATCAAACAGGAGCCCTTCAGCGCTCGT
GTTCTGGTCCTATGTGTATTTAACTCCATCTTGCCAGGTGTGCTGATTCTCTTCCTTACT
TTTTTTGCCTTTTTGCACTGCTGGCTCAATGCCTTTGCTGAGATGTTACGCTTTGGTGAC
AGGATGTTCTATAAGGATTGGTGGAACTCCACGTCATACTCCAACTATTATAGAACCTGG
AATGTGGTGGTCCATGACTGGCTATATTACTATGCTTACAAGGACTTTCTCTGGTTTTTC
TCCAAGAGATTCAAATCTGCTGCCATGTTAGCTGTCTTTGCTGTATCTGCTGTAGTACAC
GAATATGCCTTGGCTGTTTGCTTGAGCTTTTTCTATCCCGTGCTCTTCGTGCTCTTCATG
TTCTTTGGAATGGCTTTCAACTTCATTGTCAATGATAGTCGGAAAAAGCCGATTTGGAAT
GTTCTGATGTGGACTTCTCTTTTCTTGGGCAATGGAGTCTTACTCTGCTTTTATTCTCAA
GAATGGTATGCACGTCGGCACTGTCCTCTGAAAAATCCCACATTTTTGGATTATGTCCGG
CCACGTTCCTGGACTTGTCGTTACGTGTTTTAG
|
| Enzyme 32 GenBank Gene ID |
L21934  |
| Enzyme 32 GeneCard ID |
SOAT1  |
| Enzyme 32 GenAtlas ID |
SOAT1  |
| Enzyme 32 HGNC ID |
HGNC:11177  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Chang CC, Huh HY, Cadigan KM, Chang TY: Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells. J Biol Chem. 1993 Oct 5;268(28):20747-55. [PubMed
]
- Lin S, Cheng D, Liu MS, Chen J, Chang TY: Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains. J Biol Chem. 1999 Aug 13;274(33):23276-85. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5762 |
| Enzyme 33 Name |
N-acetylglutamate synthase, mitochondrial precursor |
| Enzyme 33 Synonyms |
- Amino-acid acetyltransferase[Contains: N-acetylglutamate synthase long form
- N-acetylglutamate synthase short form
- N-acetylglutamate synthase conserved domain form]
|
| Enzyme 33 Gene Name |
NAGS |
| Enzyme 33 Protein Sequence |
>N-acetylglutamate synthase, mitochondrial precursor
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
|
| Enzyme 33 Number of Residues |
534 |
| Enzyme 33 Molecular Weight |
58157 |
| Enzyme 33 Theoretical pI |
9.12 |
| Enzyme 33 GO Classification |
| Function |
- N-acetyltransferase activity
- acetylglutamate kinase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- amino acid and derivative metabolism
- amino acid biosynthesis
- amino acid metabolism
- arginine biosynthesis
- arginine metabolism
- cellular metabolism
- metabolism
- physiological process
- urea cycle intermediate metabolism
|
| Component |
| — |
|
| Enzyme 33 General Function |
Amino acid transport and metabolism |
| Enzyme 33 Specific Function |
Plays a role in the regulation of ureagenesis by producing variable amounts of N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
- acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
Not Available |
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
22651769  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q8N159  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
NAGS_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1605 bp
ATGGCGACGGCGCTGATGGCTGTGGTTCTGCGGGCAGCTGCTGTAGCCCCGAGGCTGAGA
GGCCGGGGAGGCACTGGGGGCGCCCGAAGGCTGAGCTGTGGCGCGCGGCGGCGGGCGGCG
AGGGGCACCAGCCCGGGGCGCCGGCTCAGCACCGCCTGGTCGCAGCCCCAGCCCCCGCCC
GAGGAGTACGCGGGCGCGGACGACGTCTCCCAGTCGCCCGTCGCCGAGGAGCCGTCGTGG
GTGCCGAGTCCCAGGCCCCCGGTGCCCCACGAGTCCCCAGAGCCTCCTTCGGGCCGCTCG
CTGGTGCAGCGGGACATCCAGGCCTTCCTGAACCAGTGCGGGGCCAGCCCTGGGGAGGCG
CGCCACTGGCTCACGCAGTTCCAGACCTGCCATCACTCCGCGGACAAGCCCTTCGCCGTC
ATCGAGGTGGACGAGGAGGTGCTCAAGTGCCAGCAGGGCGTATCCAGTCTGGCCTTTGCC
CTGGCCTTCTTGCAGCGCATGGACATGAAGCCGCTGGTGGTCCTGGGGCTGCCGGCCCCT
ACGGCTCCCTCGGGCTGTCTTTCCTTCTGGGAGGCCAAGGCGCAGCTGGCCAAGAGCTGC
AAGGTGCTGGTAGACGCGCTTCGACACAACGCCGCCGCTGCTGTGCCATTTTTTGGCGGC
GGGTCTGTGCTACGCGCTGCCGAGCCGGCTCCCCATGCCAGCTACGGCGGCATCGTCTCG
GTGGAGACAGACCTGCTGCAGTGGTGCCTGGAGTCGGGCAGCATCCCCATCCTGTGCCCC
ATCGGGGAGACGGCCGCGCGCCGCTCCGTGCTTCTCGACTCCCTGGAGGTGACCGCGTCG
CTGGCCAAGGCGCTGCGGCCCACCAAAATCATCTTCCTCAATAACACAGGCGGCCTGCGC
GACAGCAGTCATAAGGTCCTGAGTAACGTGAACCTGCCCGCCGACCTGGACCTGGTGTGC
AACGCCGAGTGGGTGAGCACAAAAGAACGGCAGCAGATGCGGCTCATCGTGGACGTGCTC
AGCCGCCTGCCCCACCACTCCTCGGCCGTCATCACCGCCGCTAGCACGCTGCTCACTGAG
CTCTTTAGCAACAAGGGGTCCGGGACCCTGTTCAAGAACGCCGAGCGAATGCTACGGGTG
CGCAGCCTGGACAAGCTGGACCAGGGCCGTCTAGTGGACCTGGTCAACGCCAGCTTCGGC
AAGAAGCTCAGGGACGACTACCTGGCCTCGCTGCGCCCGCGGCTGCACTCCATCTACGTC
TCCGAGGGGTACAACGCCGCCGCCATTCTGACCATGGAGCCCGTCCTGGGGGGCACCCCG
TACCTGGACAAATTTGTGGTGAGCTCCAGCCGCCAGGGCCAAGGCTCCGGCCAGATGCTG
TGGGAGTGCCTGCGGCGGGACCTTCAGACACTTTTCTGGCGCTCCCGGGTCACCAACCCC
ATCAATCCCTGGTACTTCAAACACAGTGATGGCAGCTTCTCCAACAAGCAGTGGATCTTC
TTCTGGTTTGGCCTGGCTGATATCCGGGACTCCTATGAGTTGGTCAACCACGCCAAGGGA
CTGCCAGACTCCTTTCACAAGCCAGCTTCTGACCCAGGCAGCTGA
|
| Enzyme 33 GenBank Gene ID |
AY116537  |
| Enzyme 33 GeneCard ID |
NAGS  |
| Enzyme 33 GenAtlas ID |
NAGS  |
| Enzyme 33 HGNC ID |
HGNC:17996  |
| Enzyme 33 Chromosome Location |
17 |
| Enzyme 33 Locus |
17q21.31 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Haberle J, Schmidt E, Pauli S, Kreuder JG, Plecko B, Galler A, Wermuth B, Harms E, Koch HG: Mutation analysis in patients with N-acetylglutamate synthase deficiency. Hum Mutat. 2003 Jun;21(6):593-7. [PubMed
]
- Caldovic L, Morizono H, Gracia Panglao M, Gallegos R, Yu X, Shi D, Malamy MH, Allewell NM, Tuchman M: Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun. 2002 Dec 13;299(4):581-6. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5821 |
| Enzyme 34 Name |
Bile acid CoA:amino acid N-acyltransferase |
| Enzyme 34 Synonyms |
- BAT
- BACAT
- Glycine N-choloyltransferase
- Long-chain fatty-acyl-CoA hydrolase
|
| Enzyme 34 Gene Name |
BAAT |
| Enzyme 34 Protein Sequence |
>Bile acid CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
|
| Enzyme 34 Number of Residues |
418 |
| Enzyme 34 Molecular Weight |
46300 |
| Enzyme 34 Theoretical pI |
7.00 |
| Enzyme 34 GO Classification |
| Function |
- CoA hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 34 General Function |
Not Available |
| Enzyme 34 Specific Function |
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs |
| Enzyme 34 Pathways |
- Bile Acid Biosynthesis (map00120
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 34 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
532505  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q14032  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
BAAT_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
|
| Enzyme 34 GenBank Gene ID |
L34081  |
| Enzyme 34 GeneCard ID |
BAAT  |
| Enzyme 34 GenAtlas ID |
BAAT  |
| Enzyme 34 HGNC ID |
HGNC:932  |
| Enzyme 34 Chromosome Location |
9 |
| Enzyme 34 Locus |
9q22.3 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed
]
- Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5842 |
| Enzyme 35 Name |
Long-chain-fatty-acid--CoA ligase 4 |
| Enzyme 35 Synonyms |
- Long-chain acyl-CoA synthetase 4
- LACS 4
|
| Enzyme 35 Gene Name |
ACSL4 |
| Enzyme 35 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
|
| Enzyme 35 Number of Residues |
711 |
| Enzyme 35 Molecular Weight |
79189 |
| Enzyme 35 Theoretical pI |
8.51 |
| Enzyme 35 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Lipid transport and metabolism |
| Enzyme 35 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates |
| Enzyme 35 Pathways |
|
| Enzyme 35 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
Not Available |
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
3158351  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O60488  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
ACSL4_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>2013 bp
ATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGCTCT
GTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGATAAA
TTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAAATC
CTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTTGGG
AATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGTGGA
CTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGGGCC
GAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTATAT
GCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTATCTG
ATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGTTGT
GTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAAGGA
TTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTGGGC
ATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGTTCT
ACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACAGGC
CAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCTTTG
GCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATTGGA
TATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAAGGA
GACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGAATT
TATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTCAAG
ATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGCAAT
CTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTGTCT
GGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGCCCA
ATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTAACT
GACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAAGAC
TGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTAATT
GGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGATTAT
TCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCATCCC
GATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGAGAG
TATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAACATC
TGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAGAAA
AGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGCAAT
AATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATGAAA
TTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCTGAA
ACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTACCTC
AAAGACATTGAACGAATGTATGGGGGCAAATAA
|
| Enzyme 35 GenBank Gene ID |
AF030555  |
| Enzyme 35 GeneCard ID |
ACSL4  |
| Enzyme 35 GenAtlas ID |
ACSL4  |
| Enzyme 35 HGNC ID |
HGNC:3571  |
| Enzyme 35 Chromosome Location |
X |
| Enzyme 35 Locus |
Xq22.3-q23 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed
]
- Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed
]
- Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5849 |
| Enzyme 36 Name |
Long-chain-fatty-acid--CoA ligase 1 |
| Enzyme 36 Synonyms |
- Long-chain acyl-CoA synthetase 1
- LACS 1
- Palmitoyl-CoA ligase 1
- Long-chain fatty acid CoA ligase 2
- Long-chain acyl-CoA synthetase 2
- LACS 2
- Acyl-CoA synthetase 1
- ACS1
- Palmitoyl-CoA ligase 2
|
| Enzyme 36 Gene Name |
ACSL1 |
| Enzyme 36 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
|
| Enzyme 36 Number of Residues |
698 |
| Enzyme 36 Molecular Weight |
77944 |
| Enzyme 36 Theoretical pI |
7.16 |
| Enzyme 36 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Lipid transport and metabolism |
| Enzyme 36 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
219900  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P33121  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
ACSL1_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>2097 bp
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
|
| Enzyme 36 GenBank Gene ID |
D10040  |
| Enzyme 36 GeneCard ID |
ACSL1  |
| Enzyme 36 GenAtlas ID |
ACSL1  |
| Enzyme 36 HGNC ID |
HGNC:3569  |
| Enzyme 36 Chromosome Location |
4 |
| Enzyme 36 Locus |
4q34-q35 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed
]
- Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed
]
- Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5894 |
| Enzyme 37 Name |
Long-chain-fatty-acid--CoA ligase 6 |
| Enzyme 37 Synonyms |
- Long-chain acyl-CoA synthetase 6
- LACS 6
|
| Enzyme 37 Gene Name |
ACSL6 |
| Enzyme 37 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
|
| Enzyme 37 Number of Residues |
697 |
| Enzyme 37 Molecular Weight |
77753 |
| Enzyme 37 Theoretical pI |
7.46 |
| Enzyme 37 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Lipid transport and metabolism |
| Enzyme 37 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid |
| Enzyme 37 Pathways |
|
| Enzyme 37 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
Not Available |
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
5702202  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9UKU0  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
ACSL6_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>2094 bp
ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA
|
| Enzyme 37 GenBank Gene ID |
AF129166  |
| Enzyme 37 GeneCard ID |
ACSL6  |
| Enzyme 37 GenAtlas ID |
ACSL6  |
| Enzyme 37 HGNC ID |
HGNC:16496  |
| Enzyme 37 Chromosome Location |
Not Available |
| Enzyme 37 Locus |
Not Available |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed
]
- Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5916 |
| Enzyme 38 Name |
Long-chain-fatty-acid--CoA ligase 5 |
| Enzyme 38 Synonyms |
- Long-chain acyl-CoA synthetase 5
- LACS 5
|
| Enzyme 38 Gene Name |
ACSL5 |
| Enzyme 38 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
|
| Enzyme 38 Number of Residues |
683 |
| Enzyme 38 Molecular Weight |
75992 |
| Enzyme 38 Theoretical pI |
6.91 |
| Enzyme 38 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Lipid transport and metabolism |
| Enzyme 38 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
Not Available |
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
6174680  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q9ULC5  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
ACSL5_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>2052 bp
ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG
|
| Enzyme 38 GenBank Gene ID |
AB033899  |
| Enzyme 38 GeneCard ID |
ACSL5  |
| Enzyme 38 GenAtlas ID |
ACSL5  |
| Enzyme 38 HGNC ID |
HGNC:16526  |
| Enzyme 38 Chromosome Location |
10 |
| Enzyme 38 Locus |
10q25.1-q25.2 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5919 |
| Enzyme 39 Name |
Long-chain-fatty-acid--CoA ligase 3 |
| Enzyme 39 Synonyms |
- Long-chain acyl-CoA synthetase 3
- LACS 3
|
| Enzyme 39 Gene Name |
ACSL3 |
| Enzyme 39 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
|
| Enzyme 39 Number of Residues |
720 |
| Enzyme 39 Molecular Weight |
80421 |
| Enzyme 39 Theoretical pI |
8.51 |
| Enzyme 39 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 39 General Function |
Lipid transport and metabolism |
| Enzyme 39 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
Not Available |
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
4165018  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
O95573  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
ACSL3_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>2163 bp
ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA
|
| Enzyme 39 GenBank Gene ID |
D89053  |
| Enzyme 39 GeneCard ID |
ACSL3  |
| Enzyme 39 GenAtlas ID |
ACSL3  |
| Enzyme 39 HGNC ID |
HGNC:3570  |
| Enzyme 39 Chromosome Location |
2 |
| Enzyme 39 Locus |
2q34-q35 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed
]
- Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
6170 |
| Enzyme 40 Name |
Serine palmitoyltransferase 2 |
| Enzyme 40 Synonyms |
- Long chain base biosynthesis protein 2
- LCB 2
- Serine-palmitoyl-CoA transferase 2
- SPT 2
|
| Enzyme 40 Gene Name |
SPTLC2 |
| Enzyme 40 Protein Sequence |
>Serine palmitoyltransferase 2
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFN
EAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFEN
FYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLG
FARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA
TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQ
PRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV
EYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQII
TSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIG
AFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYS
RHRLVPLLDRPFDETTYEETED
|
| Enzyme 40 Number of Residues |
562 |
| Enzyme 40 Molecular Weight |
62925 |
| Enzyme 40 Theoretical pI |
7.85 |
| Enzyme 40 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Coenzyme transport and metabolism |
| Enzyme 40 Specific Function |
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2) |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
2564249  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
O15270  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
LCB2_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1689 bp
ATGCGGCCGGAGCCCGGAGGCTGCTGCTGCCGCCGCACGGTGCGGGCGAATGGCTGCGTG
GCGAACGGGGAAGTACGGAACGGGTACGTGAGGAGCAGCGCTGCAGCCGCAGCCGCAGCC
GCCGCCGGCCAGATCCATCATGTTACACAAAATGGAGGACTATATAAAAGACCGTTTAAT
GAAGCTTTTGAAGAAACACCAATGCTGGTTGCTGTGCTCACGTATGTGGGGTATGGCGTA
CTCACCCTCTTTGGATATCTTCGAGATTTCTTGAGGTATTGGAGAATTGAAAAGTGTCAC
CATGCAACAGAAAGAGAAGAACAAAAGGACTTTGTGTCATTGTATCAAGATTTTGAAAAC
TTTTATACAAGGAATCTGTACATGAGGATAAGAGACAACTGGAATCGGCCAATCTGTAGT
GTGCCTGGAGCCAGGGTGGACATCATGGAGAGACAGTCTCATGATTATAACTGGTCCTTC
AAGTATACAGGGAATATAATAAAGGGTGTTATAAACATGGGTTCCTACAACTATCTTGGA
TTTGCACGGAATACTGGATCATGTCAAGAAGCAGCCGCCAAAGTCCTTGAGGAGTATGGA
GCTGGAGTGTGCAGTACTCGGCAGGAAATTGGAAACCTGGACAAGCATGAAGAACTAGAG
GAGCTTGTAGCAAGGTTCTTAGGAGTAGAAGCTGCTATGGCGTATGGCATGGGATTTGCA
ACGAATTCAATGAACATTCCTGCTCTTGTTGGCAAAGGTTGCCTGATTCTGAGTGATGAA
CTGAACCATGCATCACTGGTTCTGGGAGCCAGACTGTCAGGAGCAACCATTAGAATCTTC
AAACACAACAATATGCAAAGCCTAGAGAAGCTATTGAAAGATGCCATTGTTTATGGTCAG
CCTCGGACACGAAGGCCCTGGAAGAAAATTCTCATCCTTGTGGAAGGAATATATAGCATG
GAGGGATCTATTGTTCGTCTTCCTGAAGTGATTGCCCTCAAGAAGAAATACAAGGCATAC
TTGTATCTGGATGAGGCTCACAGCATTGGCGCCCTGGGCCCCACAGGCCGGGGTGTGGTG
GAGTACTTTGGCCTGGATCCCGAGGATGTGGATGTTATGATGGGAACGTTCACAAAGAGT
TTTGGTGCTTCTGGAGGATATATTGGAGGCAAGAAGGAGCTGATAGACTACCTGCGAACA
CATTCTCATAGTGCAGTGTATGCCACGTCATTGTCACCTCCTGTAGTGGAGCAGATCATC
ACCTCCATGAAGTGCATCATGGGGCAGGATGGCACCAGCCTTGGTAAAGAGTGTGTACAA
CAGTTAGCTGAAAACACCAGGTATTTCAGGAGACGCCTGAAAGAGATGGGCTTCATCATC
TATGGAAATGAAGACTCTCCAGTAGTGCCTTTGATGCTCTACATGCCTGCCAAAATTGGC
GCCTTTGGACGGGAGATGCTGAAGCGGAACATCGGTGTCGTTGTGGTTGGATTTCCTGCC
ACCCCAATTATTGAGTCCAGAGCCAGGTTTTGCCTGTCAGCAGCTCATACCAAAGAAATA
CTTGATACTGCTTTAAAGGAGATAGATGAAGTTGGGGACCTATTGCAGCTGAAGTATTCC
CGTCATCGGTTGGTACCTCTACTGGACAGGCCCTTTGACGAGACGACGTATGAAGAAACA
GAAGACTGA
|
| Enzyme 40 GenBank Gene ID |
Y08686  |
| Enzyme 40 GeneCard ID |
SPTLC2  |
| Enzyme 40 GenAtlas ID |
SPTLC2  |
| Enzyme 40 HGNC ID |
HGNC:11278  |
| Enzyme 40 Chromosome Location |
14 |
| Enzyme 40 Locus |
14q24.3-q31 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Nagiec MM, Lester RL, Dickson RC: Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Gene. 1996 Oct 24;177(1-2):237-41. [PubMed
]
- Takeda J, Yano H, Eng S, Zeng Y, Bell GI: A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones. Hum Mol Genet. 1993 Nov;2(11):1793-8. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
6171 |
| Enzyme 41 Name |
Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor |
| Enzyme 41 Synonyms |
- Succinyl-CoA synthetase subunit alpha
- SCS- alpha
|
| Enzyme 41 Gene Name |
SUCLG1 |
| Enzyme 41 Protein Sequence |
>Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
|
| Enzyme 41 Number of Residues |
333 |
| Enzyme 41 Molecular Weight |
35048 |
| Enzyme 41 Theoretical pI |
9.24 |
| Enzyme 41 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 41 General Function |
Energy production and conversion |
| Enzyme 41 Specific Function |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
Not Available |
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
9409794  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
P53597  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
SUCA_HUMAN  |
| Enzyme 41 PDB ID |
1EUC  |
| Enzyme 41 PDB File |
Show |
| Enzyme 41 3D Structure |
|
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1002 bp
ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA
|
| Enzyme 41 GenBank Gene ID |
AF104921  |
| Enzyme 41 GeneCard ID |
SUCLG1  |
| Enzyme 41 GenAtlas ID |
SUCLG1  |
| Enzyme 41 HGNC ID |
HGNC:11449  |
| Enzyme 41 Chromosome Location |
2 |
| Enzyme 41 Locus |
2p11.2 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
6173 |
| Enzyme 42 Name |
Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor |
| Enzyme 42 Synonyms |
- Succinyl-CoA synthetase, betaG chain
- SCS-betaG
- GTP- specific succinyl-CoA synthetase subunit beta
|
| Enzyme 42 Gene Name |
SUCLG2 |
| Enzyme 42 Protein Sequence |
>Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
|
| Enzyme 42 Number of Residues |
432 |
| Enzyme 42 Molecular Weight |
46511 |
| Enzyme 42 Theoretical pI |
6.18 |
| Enzyme 42 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 42 General Function |
Energy production and conversion |
| Enzyme 42 Specific Function |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
| Enzyme 42 Pathways |
|
| Enzyme 42 Reactions |
- GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
Not Available |
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
133777003  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q96I99  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
SUCB2_HUMAN  |
| Enzyme 42 PDB ID |
1EUC  |
| Enzyme 42 PDB File |
Show |
| Enzyme 42 3D Structure |
|
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1155 bp
ATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTTGTAGCAGACACTGCAAATGAAGCT
CTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATTGTTTTAAAAGCCCAGATCTTAGCT
GGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTGAAAGGAGGTGTTCATTTAACAAAA
GACCCTAATGTTGTGGGACAGCTGGCTAAACAGATGATTGGGTACAATCTAGCGACAAAA
CAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTGATGGTTGCTGAAGCCTTGGATATT
TCCAGAGAAACCTACCTGGCAATTCTGATGGACCGGTCCTGCAATGGCCCCGTGCTGGTG
GGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTGGCTGCTTCAAACCCGGAGCTCATT
TTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAGGACAGCCAAGCTCAGCGGATGGCC
GAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAGGCTGCAGATCAAATTACGAAGCTG
TATAATCTCTTCCTGAAAATTGATGCTACTCAGGTGGAAGTGAATCCCTTTGGTGAAACT
CCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATAAACTTTGATGACAACGCAGAATTC
CGACAAAAAGACATATTTGCTATGGACGACAAATCAGAGAATGAGCCCATTGAAAATGAA
GCTGCCAAATATGATCTAAAATACATAGGACTAGATGGGAACATTGCCTGCTTTGTGAAT
GGTGCTGGGCTCGCCATGGCTACTTGTGATATCATTTTCCTTAATGGTGGGAAGCCAGCC
AACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCTCAAGTATATCAAGCATTCAAATTG
CTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTCAATATATTTGGTGGTATCGTCAAC
TGTGCCATCATTGCCAATGGGATCACCAAAGCCTGCCGGGAGCTAGAACTCAAGGTGCCC
CTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAGGCCCAGAAGATACTCAACAACAGC
GGACTCCCCATTACTTCAGCCATTGACCTGGAGGATGCAGCCAAGAAGGCTGTGGCCAGT
GTGGCCAAGAAGTGA
|
| Enzyme 42 GenBank Gene ID |
BC007716  |
| Enzyme 42 GeneCard ID |
SUCLG2  |
| Enzyme 42 GenAtlas ID |
SUCLG2  |
| Enzyme 42 HGNC ID |
HGNC:11450  |
| Enzyme 42 Chromosome Location |
3 |
| Enzyme 42 Locus |
3p14.1 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
6198 |
| Enzyme 43 Name |
3-hydroxy-3-methylglutaryl-coenzyme A reductase |
| Enzyme 43 Synonyms |
- HMG-CoA reductase
|
| Enzyme 43 Gene Name |
HMGCR |
| Enzyme 43 Protein Sequence |
>3-hydroxy-3-methylglutaryl-coenzyme A reductase
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSS
DIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTG
LNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIG
VGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFAR
VLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR
IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVT
QKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNS
SLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
|
| Enzyme 43 Number of Residues |
888 |
| Enzyme 43 Molecular Weight |
97477 |
| Enzyme 43 Theoretical pI |
6.72 |
| Enzyme 43 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA reductase (NADPH) activity
- hydroxymethylglutaryl-CoA reductase (NADPH) activity
- hydroxymethylglutaryl-CoA reductase (NADPH) activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- biosynthesis
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 43 General Function |
Lipid transport and metabolism |
| Enzyme 43 Specific Function |
This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis |
| Enzyme 43 Pathways |
|
| Enzyme 43 Reactions |
- (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
Not Available |
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
306865  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P04035  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
HMDH_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>2667 bp
ATGTTGTCAAGACTTTTTCGAATGCATGGCCTCTTTGTGGCCTCCCATCCCTGGGAAGTC
ATAGTGGGGACAGTGACACTGACCATCTGCATGATGTCCATGAACATGTTTACTGGTAAC
AATAAGATCTGTGGTTGGAATTATGAATGTCCAAAGTTTGAAGAGGATGTTTTGAGCAGT
GACATTATAATTCTGACAATAACACGATGCATAGCCATCCTGTATATTTACTTCCAGTTC
CAGAATTTACGTCAACTTGGATCAAAATATATTTTGGGTATTGCTGGCCTTTTCACAATT
TTCTCAAGTTTTGTATTCAGTACAGTTGTCATTCACTTCTTAGACAAAGAATTGACAGGC
TTGAATGAAGCTTTGCCCTTTTTCCTACTTTTGATTGACCTTTCCAGAGCAAGCACATTA
GCAAAGTTTGCCCTCAGTTCCAACTCACAGGATGAAGTAAGGGAAAATATTGCTCGTGGA
ATGGCAATTTTAGGTCCTACGTTTACCCTCGATGCTCTTGTTGAATGTCTTGTGATTGGA
GTTGGTACCATGTCAGGGGTACGTCAGCTTGAAATTATGTGCTGCTTTGGCTGCATGTCA
GTTCTTGCCAACTACTTCGTGTTCATGACTTTCTTCCCAGCTTGTGTGTCCTTGGTATTA
GAGCTTTCTCGGGAAAGCCGCGAGGGTCGTCCAATTTGGCAGCTCAGCCATTTTGCCCGA
GTTTTAGAAGAAGAAGAAAATAAGCCGAATCCTGTAACTCAGAGGGTCAAGATGATTATG
TCTCTAGGCTTGGTTCTTGTTCATGCTCACAGTCGCTGGATAGCTGATCCTTCTCCTCAA
AACAGTACAGCAGATACTTCTAAGGTTTCATTAGGACTGGATGAAAATGTGTCCAAGAGA
ATTGAACCAAGTGTTTCCCTCTGGCAGTTTTATCTCTCTAAAATGATCAGCATGGATATT
GAACAAGTTATTACCCTAAGTTTAGCTCTCCTTCTGGCTGTCAAGTACATCTTCTTTGAA
CAAACAGAGACAGAATCTACACTCTCATTAAAAAACCCTATCACATCTCCTGTAGTGACA
CAAAAGAAAGTCCCAGACAATTGTTGTAGACGTGAACCTATGCTGGTCAGAAATAACCAG
AAATGTGATTCAGTAGAGGAAGAGACAGGGATAAACCGAGAAAGAAAAGTTGAGGTTATA
AAACCCTTAGTGGCTGAAACAGATACCCCAAACAGAGCTACATTTGTGGTTGGTAACTCC
TCCTTACTCGATACTTCATCAGTACTGGTGACACAGGAACCTGAAATTGAACTTCCCAGG
GAACCTCGGCCTAATGAAGAATGTCTACAGATACTTGGGAATGCAGAGAAAGGTGCAAAA
TTCCTTAGTGATGCTGAGATCATCCAGTTAGTCAATGCTAAGCATATCCCAGCCTACAAG
TTGGAAACTCTGATGGAAACTCATGAGCGTGGTGTATCTATTCGCCGACAGTTACTTTCC
AAGAAGCTTTCAGAACCTTCTTCTCTCCAGTACCTACCTTACAGGGATTATAATTACTCC
TTGGTGATGGGAGCTTGTTGTGAGAATGTTATTGGATATATGCCCATCCCTGTTGGAGTG
GCAGGACCCCTTTGCTTAGATGAAAAAGAATTTCAGGTTCCAATGGCAACAACAGAAGGT
TGTCTTGTGGCCAGCACCAATAGAGGCTGCAGAGCAATAGGTCTTGGTGGAGGTGCCAGC
AGCCGAGTCCTTGCAGATGGGATGACTCGTGGCCCAGTTGTGCGTCTTCCACGTGCTTGT
GACTCTGCAGAAGTGAAAGCCTGGCTCGAAACATCTGAAGGGTTCGCAGTGATAAAGGAG
GCATTTGACAGCACTAGCAGATTTGCACGTCTACAGAAACTTCATACAAGTATAGCTGGA
CGCAACCTTTATATCCGTTTCCAGTCCAGGTCAGGGGATGCCATGGGGATGAACATGATT
TCAAAGGGTACAGAGAAAGCACTTTCAAAACTTCACGAGTATTTCCCTGAAATGCAGATT
CTAGCCGTTAGTGGTAACTATTGTACTGACAAGAAACCTGCTGCTATAAATTGGATAGAG
GGAAGAGGAAAATCTGTTGTTTGTGAAGCTGTCATTCCAGCCAAGGTTGTCAGAGAAGTA
TTAAAGACTACCACAGAGGCTATGATTGAGGTCAACATTAACAAGAATTTAGTGGGCTCT
GCCATGGCTGGGAGCATAGGAGGCTACAACGCCCATGCAGCAAACATTGTCACCGCCATC
TACATTGCCTGTGGACAGGATGCAGCACAGAATGTTGGTAGTTCAAACTGTATTACTTTA
ATGGAAGCAAGTGGTCCCACAAATGAAGATTTATATATCAGCTGCACCATGCCATCTATA
GAGATAGGAACGGTGGGTGGTGGGACCAACCTACTACCTCAGCAAGCCTGTTTGCAGATG
CTAGGTGTTCAAGGAGCATGCAAAGATAATCCTGGGGAAAATGCCCGGCAGCTTGCCCGA
ATTGTGTGTGGGACCGTAATGGCTGGGGAATTGTCACTTATGGCAGCATTGGCAGCAGGA
CATCTTGTCAAAAGTCACATGATTCACAACAGGTCGAAGATCAATTTACAAGACCTCCAA
GGAGCTTGCACCAAGAAGACAGCCTGA
|
| Enzyme 43 GenBank Gene ID |
M11058  |
| Enzyme 43 GeneCard ID |
HMGCR  |
| Enzyme 43 GenAtlas ID |
HMGCR  |
| Enzyme 43 HGNC ID |
HGNC:5006  |
| Enzyme 43 Chromosome Location |
5 |
| Enzyme 43 Locus |
5q13.3-q14 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Luskey KL, Stevens B: Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J Biol Chem. 1985 Aug 25;260(18):10271-7. [PubMed
]
- Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
6335 |
| Enzyme 44 Name |
Cytosolic acyl coenzyme A thioester hydrolase |
| Enzyme 44 Synonyms |
- Long chain acyl-CoA thioester hydrolase
- CTE-II
- CTE-IIa
- Brain acyl-CoA hydrolase
- Acyl-CoA thioesterase 7
|
| Enzyme 44 Gene Name |
ACOT7 |
| Enzyme 44 Protein Sequence |
>Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
|
| Enzyme 44 Number of Residues |
380 |
| Enzyme 44 Molecular Weight |
41797 |
| Enzyme 44 Theoretical pI |
8.66 |
| Enzyme 44 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 44 General Function |
Lipid transport and metabolism |
| Enzyme 44 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
Not Available |
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
2780414  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
O00154  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
BACH_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1017 bp
ATGTCGGGCCCAGACGTCGAGACGCCGTCCGCCATCCAGATCTGCCGGATCATGCGGCCA
GATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATCGAGGAG
GCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGTGTGGCC
GCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAGGTGGCG
CATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTCAACGTG
ATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTGTGGTAT
GTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTGTATTCC
CGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAGCGCATG
GAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCGAACACT
GTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACCCTGCAC
GGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATCGTGGCT
GCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTTCATGAC
AAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGCAATAAG
TCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAGAAGCGC
TACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGGTCGCTG
CCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAAGGCAAA
GGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCCTAG
|
| Enzyme 44 GenBank Gene ID |
D88894  |
| Enzyme 44 GeneCard ID |
ACOT7  |
| Enzyme 44 GenAtlas ID |
ACOT7  |
| Enzyme 44 HGNC ID |
HGNC:24157  |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
1p36.31-p36.11 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
6336 |
| Enzyme 45 Name |
Acyl-coenzyme A thioesterase 2 |
| Enzyme 45 Synonyms |
- Acyl-CoA thioesterase 2
- Peroxisomal acyl-coenzyme A thioester hydrolase 2a
- Peroxisomal long-chain acyl-coA thioesterase 2
- ZAP128
- CTE-Ia
|
| Enzyme 45 Gene Name |
ACOT2 |
| Enzyme 45 Protein Sequence |
>Acyl-coenzyme A thioesterase 2
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGREGTIP
SKV
|
| Enzyme 45 Number of Residues |
483 |
| Enzyme 45 Molecular Weight |
53257 |
| Enzyme 45 Theoretical pI |
8.93 |
| Enzyme 45 GO Classification |
| Function |
- CoA hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 45 General Function |
Not Available |
| Enzyme 45 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate
|
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
887376  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P49753  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
ACOT2_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>937 bp
CCCCCGGGCTGCAGGAATTCCTGAATTCAAAATGGCCTCATCTCCTGCTGTCCTTCGAGC
GTCCCGGCTGTACCAATGGAGCCTGAAGAGTTCGGCGCAGTTCCTGGGGTCTCCACAGCT
GAGGCAGAACCTGGGCCCTTTCCTGGGATTGTGGACATGTTCGGGAACTGGAGGTGGCCT
GCTGGAGTATCGGGCTAGTCTGCTGGCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTA
TTATAACTATGAAGACCTCCCCAAGACCATGGAGACGCTCCATCTGGAGTACTTTGAAGA
AGCCATGAACTACTTGCTCAGTCATCCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGG
AATTTCCAAAGGGGGTGAGCTCTGCCTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGC
TGCTGTCGTCATCAACGGCTCTGTGGCCAATGTTGGGGGAACCTTACACTACAAGGGCGA
GACCCTGCCCCCTGTGGGCGTCAACAGAAATCGCATCAAGGTGACCAAAGATGGCTATGC
AGACATTGTGGATGTCCTGAACAGCCCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCC
TGTGGAAAGGGCAGAGAGCACCTTCCTGTTCCTGGTAGGTCAGGATGACCACAACTGGAA
GAGTGAGTTCTATGCTAATGAGGCCTGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCC
CCAGATCATCTGTTACCCAGAGACAGGGCACTATATTGAGCCTCCTTACTTCCCCCTGTG
TCGGGCTTCCCTGCATGCCTTGGTGGGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGC
TCATGCCATGGCTCAGGTGGATGCTTGGAAACAACTCCAGACTTTCTTCCACAAACACTT
GGGTGGCCACGAGGGGACAATCCCATCAAAAGTGTAA
|
| Enzyme 45 GenBank Gene ID |
L40401  |
| Enzyme 45 GeneCard ID |
ACOT2  |
| Enzyme 45 GenAtlas ID |
ACOT2  |
| Enzyme 45 HGNC ID |
HGNC:18431  |
| Enzyme 45 Chromosome Location |
14 |
| Enzyme 45 Locus |
14q24.3 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed
]
- Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
6338 |
| Enzyme 46 Name |
Acyl-coenzyme A thioesterase 8 |
| Enzyme 46 Synonyms |
- Choloyl-coenzyme A thioesterase
- Acyl-CoA thioesterase 8
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- PTE-1
- Peroxisomal long-chain acyl-coA thioesterase 1
- HIV-Nef-associated acyl coA thioesterase
- Thioesterase II
- hTE
- hACTEIII
- hACTE-III
- PTE-2
|
| Enzyme 46 Gene Name |
ACOT8 |
| Enzyme 46 Protein Sequence |
>Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
|
| Enzyme 46 Number of Residues |
319 |
| Enzyme 46 Molecular Weight |
35915 |
| Enzyme 46 Theoretical pI |
7.60 |
| Enzyme 46 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolism
- carboxylic acid metabolism
- cellular metabolism
- fatty acid metabolism
- metabolism
- organic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 46 General Function |
Lipid transport and metabolism |
| Enzyme 46 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
2318125  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
O14734  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
ACOT8_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
|
| Enzyme 46 GenBank Gene ID |
AF014404  |
| Enzyme 46 GeneCard ID |
ACOT8  |
| Enzyme 46 GenAtlas ID |
ACOT8  |
| Enzyme 46 HGNC ID |
HGNC:15919  |
| Enzyme 46 Chromosome Location |
20 |
| Enzyme 46 Locus |
20q13.12 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed
]
- Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed
]
- Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
6339 |
| Enzyme 47 Name |
Palmitoyl-protein thioesterase 1 precursor |
| Enzyme 47 Synonyms |
- PPT-1
- Palmitoyl-protein hydrolase 1
|
| Enzyme 47 Gene Name |
PPT1 |
| Enzyme 47 Protein Sequence |
>Palmitoyl-protein thioesterase 1 precursor
MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEK
KIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQF
LRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERL
VQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVD
SEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAH
IIPFLG
|
| Enzyme 47 Number of Residues |
306 |
| Enzyme 47 Molecular Weight |
34194 |
| Enzyme 47 Theoretical pI |
6.50 |
| Enzyme 47 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-(protein) hydrolase activity
- thiolester hydrolase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein modification
|
| Component |
| — |
|
| Enzyme 47 General Function |
Not Available |
| Enzyme 47 Specific Function |
Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
- palmitoyl[protein] + H2O = palmitate + protein
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
Not Available |
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
1160967  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P50897  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
PPT1_HUMAN  |
| Enzyme 47 PDB ID |
1EXW  |
| Enzyme 47 PDB File |
Show |
| Enzyme 47 3D Structure |
|
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>921 bp
ATGGCGTCGCCCGGCTGCCTGTGGCTCTTGGCTGTGGCTCTCCTGCCATGGACCTGCGCT
TCTCGGGCGCTGCAGCATCTGGACCCGCCGGCGCCGCTGCCGTTGGTGATCTGGCATGGG
ATGGGAGACAGCTGTTGCAATCCCTTAAGCATGGGTGCTATTAAAAAAATGGTGGAGAAG
AAAATACCTGGAATTTACGTCTTATCTTTAGAGATTGGGAAGACCCTGATGGAGGACGTG
GAGAACAGCTTCTTCTTGAATGTCAATTCCCAAGTAACAACAGTGTGTCAGGCACTTGCT
AAGGATCCTAAATTGCAGCAAGGCTACAATGCTATGGGATTCTCCCAGGGAGGCCAATTT
CTGAGGGCAGTGGCTCAGAGATGCCCTTCACCTCCCATGATCAATCTGATCTCGGTTGGG
GGACAACATCAAGGTGTTTTTGGACTCCCTCGATGCCCAGGAGAGAGCTCTCACATCTGT
GACTTCATCCGAAAAACACTGAATGCTGGGGCGTACTCCAAAGTTGTTCAGGAACGCCTC
GTGCAAGCCGAATACTGGCATGACCCCATAAAGGAGGATGTGTATCGCAACCACAGCATC
TTCTTGGCAGATATAAATCAGGAGCGGGGTATCAATGAGTCCTACAAGAAAAACCTGATG
GCCCTGAAGAAGTTTGTGATGGTGAAATTCCTCAATGATTCCATTGTGGACCCTGTAGAT
TCGGAGTGGTTTGGATTTTACAGAAGTGGCCAAGCCAAGGAAACCATTCCCTTACAGGAG
ACCTCCCTGTACACACAGGACCGCCTGGGGCTAAAGGAAATGGACAATGCAGGACAGCTA
GTGTTTCTGGCTACAGAAGGGGACCATCTTCAGTTGTCTGAAGAATGGTTTTATGCCCAC
ATCATACCATTCCTTGGATGA
|
| Enzyme 47 GenBank Gene ID |
L42809  |
| Enzyme 47 GeneCard ID |
PPT1  |
| Enzyme 47 GenAtlas ID |
PPT1  |
| Enzyme 47 HGNC ID |
HGNC:9325  |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
1p32 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L: Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. [PubMed
]
- Crews CM, Lane WS, Schreiber SL: Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4316-9. [PubMed
]
- Schriner JE, Yi W, Hofmann SL: cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics. 1996 Jun 15;34(3):317-22. [PubMed
]
- Lu JY, Verkruyse LA, Hofmann SL: Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10046-50. [PubMed
]
- Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed
]
- Mitchison HM, Hofmann SL, Becerra CH, Munroe PB, Lake BD, Crow YJ, Stephenson JB, Williams RE, Hofman IL, Taschner PE, Martin JJ, Philippart M, Andermann E, Andermann F, Mole SE, Gardiner RM, O'Rawe AM: Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits. Hum Mol Genet. 1998 Feb;7(2):291-7. [PubMed
]
- Das AK, Becerra CH, Yi W, Lu JY, Siakotos AN, Wisniewski KE, Hofmann SL: Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. J Clin Invest. 1998 Jul 15;102(2):361-70. [PubMed
]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
6839 |
| Enzyme 48 Name |
Dihydroxyacetone phosphate acyltransferase |
| Enzyme 48 Synonyms |
- DHAP-AT
- DAP-AT
- Glycerone-phosphate O-acyltransferase
- Acyl- CoA:dihydroxyacetonephosphateacyltransferase
|
| Enzyme 48 Gene Name |
GNPAT |
| Enzyme 48 Protein Sequence |
>Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
|
| Enzyme 48 Number of Residues |
680 |
| Enzyme 48 Molecular Weight |
77189 |
| Enzyme 48 Theoretical pI |
6.52 |
| Enzyme 48 GO Classification |
| Function |
- O-acetyltransferase activity
- O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- glycerone-phosphate O-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- biosynthesis
- cellular lipid metabolism
- ether lipid biosynthesis
- glycerolipid biosynthesis
- lipid biosynthesis
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
- cell
- membrane
- microbody membrane
- organelle membrane
- peroxisomal membrane
|
|
| Enzyme 48 General Function |
Lipid transport and metabolism |
| Enzyme 48 Specific Function |
Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate |
| Enzyme 48 Pathways |
|
| Enzyme 48 Reactions |
- acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
2584769  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
O15228  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
GNPAT_HUMAN  |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAGTCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
|
| Enzyme 48 GenBank Gene ID |
AJ002190  |
| Enzyme 48 GeneCard ID |
GNPAT  |
| Enzyme 48 GenAtlas ID |
GNPAT  |
| Enzyme 48 HGNC ID |
HGNC:4416  |
| Enzyme 48 Chromosome Location |
1 |
| Enzyme 48 Locus |
1q42.11-42.3 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed
]
- Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed
]
- Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
6873 |
| Enzyme 49 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma |
| Enzyme 49 Synonyms |
- 1- AGP acyltransferase 3
- 1-AGPAT 3
- Lysophosphatidic acid acyltransferase gamma
- LPAAT-gamma
- 1-acylglycerol-3-phosphate O- acyltransferase 3
|
| Enzyme 49 Gene Name |
AGPAT3 |
| Enzyme 49 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
|
| Enzyme 49 Number of Residues |
376 |
| Enzyme 49 Molecular Weight |
43381 |
| Enzyme 49 Theoretical pI |
8.91 |
| Enzyme 49 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 49 General Function |
Lipid transport and metabolism |
| Enzyme 49 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 49 Pathways |
|
| Enzyme 49 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
Not Available |
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
8886001  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q9NRZ7  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
PLCC_HUMAN  |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>1131 bp
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCATACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
|
| Enzyme 49 GenBank Gene ID |
AF156774  |
| Enzyme 49 GeneCard ID |
AGPAT3  |
| Enzyme 49 GenAtlas ID |
AGPAT3  |
| Enzyme 49 HGNC ID |
HGNC:326  |
| Enzyme 49 Chromosome Location |
Not Available |
| Enzyme 49 Locus |
Not Available |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
6875 |
| Enzyme 50 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase beta |
| Enzyme 50 Synonyms |
- 1- AGP acyltransferase 2
- 1-AGPAT 2
- Lysophosphatidic acid acyltransferase beta
- LPAAT-beta
- 1-acylglycerol-3-phosphate O- acyltransferase 2
|
| Enzyme 50 Gene Name |
AGPAT2 |
| Enzyme 50 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase beta
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
|
| Enzyme 50 Number of Residues |
278 |
| Enzyme 50 Molecular Weight |
30915 |
| Enzyme 50 Theoretical pI |
9.22 |
| Enzyme 50 GO Classification |
| Function |
- 1-acylglycerol-3-phosphate O-acyltransferase activity
- O-acyltransferase activity
- acylglycerol O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 50 General Function |
Lipid transport and metabolism |
| Enzyme 50 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 50 Pathways |
|
| Enzyme 50 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
Not Available |
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
2282590  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
O15120  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
PLCB_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>837 bp
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
|
| Enzyme 50 GenBank Gene ID |
AF000237  |
| Enzyme 50 GeneCard ID |
AGPAT2  |
| Enzyme 50 GenAtlas ID |
AGPAT2  |
| Enzyme 50 HGNC ID |
HGNC:325  |
| Enzyme 50 Chromosome Location |
9 |
| Enzyme 50 Locus |
9q34.3 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed
]
- Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed
]
- West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed
]
- Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
7284 |
| Enzyme 51 Name |
Bifunctional coenzyme A synthase |
| Enzyme 51 Synonyms |
- CoA synthase
- NBP
- POV-2[Includes: Phosphopantetheine adenylyltransferase
- Pantetheine-phosphate adenylyltransferase
- PPAT
- Dephospho-CoA pyrophosphorylase
- Dephospho-CoA kinase
- DPCK
- Dephosphocoenzyme A kinase
- DPCOAK]
|
| Enzyme 51 Gene Name |
COASY |
| Enzyme 51 Protein Sequence |
>Bifunctional coenzyme A synthase
MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQA
TFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQT
LDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPV
AGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPEL
LQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINR
FRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYV
IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGI
INRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQ
NLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHI
TQRQVEKAWALLQKRIPKTHQALD
|
| Enzyme 51 Number of Residues |
564 |
| Enzyme 51 Molecular Weight |
62330 |
| Enzyme 51 Theoretical pI |
6.99 |
| Enzyme 51 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleotide binding
- nucleotidyltransferase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 51 General Function |
Not Available |
| Enzyme 51 Specific Function |
Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopan |