|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6219 |
| Enzyme 1 Name |
Geranylgeranyl pyrophosphate synthetase |
| Enzyme 1 Synonyms |
- GGPP synthetase
- GGPPSase
- Geranylgeranyl diphosphate synthase[Includes: Dimethylallyltranstransferase
|
| Enzyme 1 Gene Name |
GGPS1 |
| Enzyme 1 Protein Sequence |
>Geranylgeranyl pyrophosphate synthetase
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS
LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL
ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL
GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
|
| Enzyme 1 Number of Residues |
300 |
| Enzyme 1 Molecular Weight |
34871 |
| Enzyme 1 Theoretical pI |
6.06 |
| Enzyme 1 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 1 General Function |
Coenzyme transport and metabolism |
| Enzyme 1 Specific Function |
Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
4520350  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O95749  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GGPPS_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>903 bp
ATGGAGAAGACTCAAGAAACAGTCCAAAGAATTCTTCTAGAACCCTATAAATACTTACTT
CAGTTACCAGGTAAACAAGTGAGAACCAAACTTTCACAGGCATTTAATCATTGGCTGAAA
GTTCCAGAGGACAAGCTACAGATTATTATTGAAGTGACAGAAATGTTGCATAATGCCAGT
TTACTCATCGATGATATTGAAGACAACTCAAAACTCCGACGTGGCTTTCCAGTGGCCCAC
AGCATCTATGGAATCCCATCTGTCATCAATTCTGCCAATTACGTGTATTTCCTTGGCTTG
GAGAAAGTCTTAACCCTTGATCACCCAGATGCAGTGAAGCTTTTTACCCGCCAGCTTTTG
GAACTCCATCAGGGACAAGGCCTAGATATTTACTGGAGGGATAATTACACTTGTCCCACT
GAAGAAGAATATAAAGCTATGGTGCTGCAGAAAACAGGTGGACTGTTTGGATTAGCAGTA
GGTCTCATGCAGTTGTTCTCTGATTACAAAGAAGATTTAAAACCGCTACTTAATACACTT
GGGCTCTTTTTCCAAATTAGGGATGATTATGCTAATCTACACTCCAAAGAATATAGTGAA
AACAAAAGTTTTTGTGAAGATCTGACAGAGGGAAAGTTCTCATTTCCTACTATTCATGCT
ATTTGGTCAAGGCCTGAAAGCACCCAGGTGCAGAATATCTTGCGCCAGAGAACAGAAAAC
ATAGATATAAAAAAATACTGTGTACATTATCTTGAGGATGTAGGTTCTTTTGAATACACT
CGTAATACCCTTAAAGAGCTTGAAGCTAAAGCCTATAAACAGATTGATGCACGTGGTGGG
AACCCTGAGCTAGTAGCCTTAGTAAAACACTTAAGTAAGATGTTCAAAGAAGAAAATGAA
TAA
|
| Enzyme 1 GenBank Gene ID |
AB017971  |
| Enzyme 1 GeneCard ID |
GGPS1  |
| Enzyme 1 GenAtlas ID |
GGPS1  |
| Enzyme 1 HGNC ID |
HGNC:4249  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1q43 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Ericsson J, Greene JM, Carter KC, Shell BK, Duan DR, Florence C, Edwards PA: Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression. J Lipid Res. 1998 Sep;39(9):1731-9. [PubMed
]
- Kuzuguchi T, Morita Y, Sagami I, Sagami H, Ogura K: Human geranylgeranyl diphosphate synthase. cDNA cloning and expression. J Biol Chem. 1999 Feb 26;274(9):5888-94. [PubMed
]
- Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed
]
- Kainou T, Kawamura K, Tanaka K, Matsuda H, Kawamukai M: Identification of the GGPS1 genes encoding geranylgeranyl diphosphate synthases from mouse and human. Biochim Biophys Acta. 1999 Mar 25;1437(3):333-40. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6220 |
| Enzyme 2 Name |
Farnesyl pyrophosphate synthetase |
| Enzyme 2 Synonyms |
- FPP synthetase
- FPS
- Farnesyl diphosphate synthetase[Includes: Dimethylallyltranstransferase
|
| Enzyme 2 Gene Name |
FDPS |
| Enzyme 2 Protein Sequence |
>Farnesyl pyrophosphate synthetase
MNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNR
GLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ
KPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQ
GNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQ
IQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVAR
VKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
|
| Enzyme 2 Number of Residues |
353 |
| Enzyme 2 Molecular Weight |
40533 |
| Enzyme 2 Theoretical pI |
4.80 |
| Enzyme 2 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 2 General Function |
Coenzyme transport and metabolism |
| Enzyme 2 Specific Function |
Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
182399  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P14324  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
FPPS_HUMAN  |
| Enzyme 2 PDB ID |
1YV5  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1062 bp
ATGAACGGAGACCAGAATTCAGATGTTTATGCCCAAGAAAAGCAGGATTTCGTTCAGCAC
TTCTCCCAGATCGTTAGGGTGCTGACTGAGGATGAGATGGGGCACCCAGAGATAGGAGAT
GCTATTGCCCGGCTCAAGGAGGTCCTGGAGTACAATGCCATTGGAGGCAAGTATAACCGG
GGTTTGACGGTGGTAGTAGCATTCCGGGAGCTGGTGGAGCCAAGGAAACAGGATGCTGAT
AGTCTCCAGCGGGCCTGGACTGTGGGCTGGTGTGTGGAACTGCTGCAAGCTTTCTTCCTG
GTGGCAGATGACATCATGGATTCATCCCTTACCCGCCGGGGACAGACCTGCTGGTATCAG
AAGCCGGGCGTGGGTTTGGATGCCATCAATGATGCTAACCTCCTGGAAGCATGTATCTAC
CGCCTGCTGAAGCTCTATTGCCGGGAGCAGCCCTATTACCTGAACCTGATCGAGCTCTTC
CTGCAGAGTTCCTATCAGACTGAGATTGGGCAGACCCTGGACCTCCTCACAGCCCCCCAG
GGCAATGTGGATCTTGTCAGATTCACTGAAAAGAGGTACAAATCTATTGTCAAGTACAAG
ACAGCTTTCTACTCCTTCTACCTTCCTATAGCTGCAGCCATGTACATGGCAGGAATTGAT
GGCGAGAAGGAGCACGCCAATGCCAAGAAGATCCTGCTGGAGATGGGGGAGTTCTTTCAG
ATTCAGGATGATTACCTTGACCTCTTTGGGGACCCCAGTGTGACCGGCAAAATTGGCACT
GACATCCAGGACAACAAATGCAGCTGGCTGGTGGTTCAGTGTCTGCAACGGGCCACTCCA
GAACAGTACCAGATCCTGAAGGAAAATTACGGGCAGAAGGAGGCTGAGAAAGTGGCCCGG
GTGAAGGCGCTATATGAGGAGCTGGATCTGCCAGCAGTGTTCTTGCAATATGAGGAAGAC
AGTTACAGCCACATTATGGCTCTCATTGAACAGTACGCAGCACCCCTGCCCCCAGCCGTC
TTTCTGGGGCTTGCGCGCAAAATCTACAAGCGGAGAAAGTGA
|
| Enzyme 2 GenBank Gene ID |
J05262  |
| Enzyme 2 GeneCard ID |
FDPS  |
| Enzyme 2 GenAtlas ID |
FDPS  |
| Enzyme 2 HGNC ID |
HGNC:3631  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1q22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Wilkin DJ, Kutsunai SY, Edwards PA: Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester. J Biol Chem. 1990 Mar 15;265(8):4607-14. [PubMed
]
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed
]
- Sheares BT, White SS, Molowa DT, Chan K, Ding VD, Kroon PA, Bostedor RG, Karkas JD: Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells. Biochemistry. 1989 Oct 3;28(20):8129-35. [PubMed
]
- Lefebvre L, Vanderplasschen A, Ciminale V, Heremans H, Dangoisse O, Jauniaux JC, Toussaint JF, Zelnik V, Burny A, Kettmann R, Willems L: Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase. J Virol. 2002 Feb;76(3):1400-14. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6304 |
| Enzyme 3 Name |
Diphosphomevalonate decarboxylase |
| Enzyme 3 Synonyms |
- Mevalonate pyrophosphate decarboxylase
- Mevalonate
- diphosphodecarboxylase
|
| Enzyme 3 Gene Name |
MVD |
| Enzyme 3 Protein Sequence |
>Diphosphomevalonate decarboxylase
MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDF
TEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPT
AAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKD
SIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEM
ARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKV
AYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAM
EPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA
|
| Enzyme 3 Number of Residues |
400 |
| Enzyme 3 Molecular Weight |
43405 |
| Enzyme 3 Theoretical pI |
7.25 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- diphosphomevalonate decarboxylase activity
- kinase activity
- lyase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- cellular metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- phosphate metabolism
- phosphorus metabolism
- phosphorylation
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 3 General Function |
Lipid transport and metabolism |
| Enzyme 3 Specific Function |
Performs the first committed step in the biosynthesis of isoprenes |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1235682  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P53602  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ERG19_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1203 bp
ATGGCCTCGGAGAAGCCGCTGGCGGCAGTCACTTGTACAGCGCCGGTCAACATCGCGGTC
ATCAAGTACTGGGGCAAGCGCGATGAAGAGCTGGTTCTGCCCATCAACTCCTCCCTGAGC
GTCACTCTGCACCAGGACCAGTTAAAAACCACCACAACAGCCGTCATCAGCAAGGACTTC
ACCGAGGACCGGATTTGGCTGAATGGCCGGGAGGAGGATGTGGGGCAGCCGAGGCTGCAG
GCCTGCCTGCGGGAGATCCGCTGCCTGGCCCGGAAGCGGAGGAACTCACGGGATGGGGAC
CCGCTGCCCTCCAGCCTCAGCTGCAAGGTGCACGTGGCATCGGTGAACAACTTCCCCACG
GCTGCGGGCCTGGCCTCCTCAGCGGCGGGCTATGCCTGCCTAGCCTACACCCTGGCCCGT
GTCTACGGCGTGGAGAGTGACCTCTCAGAAGTGGCTCGCCGGGGCTCAGGCAGCGCCTGC
CGGAGCCTGTATGGGGGCTTTGTGGAGTGGCAGATGGGAGAGCAGGCCGACGGGAAGGAC
AGCATCGCTCGGCAAGTGGCCCCCGAGTCACACTGGCCTGAACTCCGCGTGCTCATCCTT
GTGGTGAGCGCTGAGAAGAAGCTGACAGGCAGTACCGTGGGCATGCGGGCCAGTGTGGAG
ACCAGCCCCCTGCTTCGGTTCCGGGCCGAGTCCGTGGTGCCCGCGCGCATGGCGGAGATG
GCCCGCTGCATCCGGGAGCGAGACTTCCCCAGCTTCGCCCAGCTGACCATGAAGGACAGC
AACCAGTTCCACGCCACCTGCCTCGACACCTTCCCGCCCATCTCTTACCTCAATGCCATC
TCCTGGCGCATCATCCACCTGGTGCACCGCTTCAACGCCCACCACGGGGACACCAAGGTG
GCGTACACCTTTGACGCGGGCCCCAATGCCGTGATCTTCACCCTGGACGACACTGTGGCT
GAGTTTGTGGCTGCTGTGTGGCACGGCTTTCCCCCAGGCTCGAATGGAGACACGTTTCTG
AAGGGGCTGCAGGTGAGGCCGGCCCCTCTCTCAGCTGAGCTTCAGGCTGCGCTGGCCATG
GAGCCGACCCCCGGTGGGGTCAAATACATCATTGTCACTCAGGTGGGGCCAGGGCCTCAA
ATCCTGGATGACCCCTGCGCCCACCTCCTGGGTCCTGACGGCCTGCCGAAGCCAGCTGCC
TGA
|
| Enzyme 3 GenBank Gene ID |
U49260  |
| Enzyme 3 GeneCard ID |
MVD  |
| Enzyme 3 GenAtlas ID |
MVD  |
| Enzyme 3 HGNC ID |
HGNC:7529  |
| Enzyme 3 Chromosome Location |
16 |
| Enzyme 3 Locus |
16q24.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Toth MJ, Huwyler L: Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J Biol Chem. 1996 Apr 5;271(14):7895-8. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6836 |
| Enzyme 4 Name |
Isopentenyl-diphosphate Delta-isomerase 2 |
| Enzyme 4 Synonyms |
- IPP isomerase 2
- Isopentenyl pyrophosphate isomerase 2
- IPPI2
|
| Enzyme 4 Gene Name |
IDI2 |
| Enzyme 4 Protein Sequence |
>Isopentenyl-diphosphate Delta-isomerase 2
MSDINLDWVDRRQLQRLEEMLIVVDENDKVIGADTKRNCHLNENIEKGLLHRAFSVVLFN
TKNRILIQQRSDTKVTFPGYFTDSCSSHPLYNPAELEEKDAIGVRRAAQRRLQAELGIPG
EQISPEDIVFMTIYHHKAKSDRIWGEHEICYLLLVRKNVTLNPDPSETKSILYLSQEELW
ELLEREARGEVKVTPWLRTIAERFLYRWWPHLDDVTPFVELHKIHRV
|
| Enzyme 4 Number of Residues |
227 |
| Enzyme 4 Molecular Weight |
26753 |
| Enzyme 4 Theoretical pI |
6.43 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, transposing C=C bonds
- isomerase activity
- isopentenyl-diphosphate delta-isomerase activity
|
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- isopentenyl diphosphate = dimethylallyl diphosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
13540192  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9BXS1  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
IDI2_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>684 bp
ATGTCTGACATAAATCTTGACTGGGTTGACAGGCGTCAGTTGCAGCGCTTGGAGGAAATG
CTGATTGTTGTGGATGAGAATGATAAGGTTATTGGTGCCGACACCAAGAGGAATTGCCAT
CTGAACGAAAACATTGAGAAAGGGCTGCTGCACCGAGCCTTCAGCGTTGTCTTGTTTAAC
ACCAAGAATCGAATCCTGATACAGCAGAGGTCGGACACGAAAGTCACGTTTCCTGGGTAT
TTTACCGACTCCTGTAGTAGCCACCCATTATACAACCCAGCAGAACTGGAAGAAAAGGAT
GCCATCGGAGTGAGGAGGGCAGCCCAGAGGCGTCTGCAAGCAGAGCTGGGAATTCCTGGG
GAGCAGATTTCTCCAGAGGACATTGTGTTCATGACAATCTATCACCACAAGGCAAAATCA
GACAGAATTTGGGGAGAGCATGAAATTTGTTACCTTCTGCTTGTGAGGAAAAACGTCACT
CTGAACCCGGATCCCAGTGAAACGAAAAGCATCCTCTACCTGTCCCAGGAGGAGCTGTGG
GAGCTGCTGGAGAGGGAGGCGAGGGGTGAAGTCAAAGTCACCCCCTGGCTAAGAACCATT
GCCGAGAGGTTTCTGTACCGGTGGTGGCCTCACCTGGATGACGTGACCCCGTTTGTGGAG
CTTCACAAAATACACAGAGTGTGA
|
| Enzyme 4 GenBank Gene ID |
AF291755  |
| Enzyme 4 GeneCard ID |
IDI2  |
| Enzyme 4 GenAtlas ID |
IDI2  |
| Enzyme 4 HGNC ID |
HGNC:23487  |
| Enzyme 4 Chromosome Location |
10 |
| Enzyme 4 Locus |
10p15.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6837 |
| Enzyme 5 Name |
Isopentenyl-diphosphate Delta-isomerase 1 |
| Enzyme 5 Synonyms |
- IPP isomerase 1
- Isopentenyl pyrophosphate isomerase 1
- IPPI1
|
| Enzyme 5 Gene Name |
IDI1 |
| Enzyme 5 Protein Sequence |
>Isopentenyl-diphosphate Delta-isomerase 1
MPEINTNHLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVFLFN
TENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRAAQRRLKAELGIPL
EEVPPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRKNVTLNPDPNEIKSYCYVSKEELK
ELLKKAASGEIKITPWFKIIAATFLFKWWDNLNHLNQFVDHEKIYRM
|
| Enzyme 5 Number of Residues |
227 |
| Enzyme 5 Molecular Weight |
26319 |
| Enzyme 5 Theoretical pI |
6.31 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, transposing C=C bonds
- isomerase activity
- isopentenyl-diphosphate delta-isomerase activity
|
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 5 General Function |
Lipid transport and metabolism |
| Enzyme 5 Specific Function |
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- isopentenyl diphosphate = dimethylallyl diphosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
488750  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q13907  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
IDI1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>687 bp
ATGATGCCTGAAATAAACACTAACCACCTCGACAAGCAACAGGTTCAACTCCTGGCAGAG
ATGTGTATCCTTATTGATGAAAATGACAATAAAATTGGAGCTGAGACCAAGAAGAATTGT
CACCTGAACGAGAACATTGAGAAAGGATTATTGCATCGAGCTTTTAGTGTCTTCTTATTC
AACACCGAAAATAAGCTTCTGCTACAGCAAAGATCAGATGCTAAGATTACCTTTCCAGGT
TGTTTTACGAATACGTGTTGTAGTCATCCATTAAGCAATCCAGCCGAGCTTGAGGAAAGT
GACGCCCTTGGAGTGAGGCGAGCAGCACAGAGACGGCTGAAAGCTGAGCTAGGAATTCCC
TTGGAAGAGGTTCCTCCAGAAGAAATTAATTATTTAACACGAATTCACTACAAAGCTCAG
TCTGATGGTATCTGGGGTGAACATGAAATTGATTACATTTTGTTGGTGAGGAAGAATGTA
ACTTTGAATCCAGATCCCAATGAGATTAAAAGCTATTGTTATGTGTCAAAGGAAGAACTA
AAAGAACTTCTGAAAAAAGCAGCCAGTGGTGAAATTAAGATAACGCCATGGTTTAAAATT
ATTGCAGCGACTTTTCTCTTTAAATGGTGGGATAACTTAAATCATTTGAATCAGTTTGTT
GACCATGAGAAAATATACAGAATGTGA
|
| Enzyme 5 GenBank Gene ID |
X17025  |
| Enzyme 5 GeneCard ID |
IDI1  |
| Enzyme 5 GenAtlas ID |
IDI1  |
| Enzyme 5 HGNC ID |
HGNC:5387  |
| Enzyme 5 Chromosome Location |
10 |
| Enzyme 5 Locus |
10p15.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Xuan JW, Kowalski J, Chambers AF, Denhardt DT: A human promyelocyte mRNA transiently induced by TPA is homologous to yeast IPP isomerase. Genomics. 1994 Mar 1;20(1):129-31. [PubMed
]
- Hahn FM, Xuan JW, Chambers AF, Poulter CD: Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization. Arch Biochem Biophys. 1996 Aug 1;332(1):30-4. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
13006 |
| Enzyme 6 Name |
Farnesyl diphosphate synthase |
| Enzyme 6 Synonyms |
- Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
- Farnesyl diphosphate synthase
- Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase, isoform CRA_b
- cDNA FLJ76177, highly similar to Homo sapiens farnesyl diphosphate synthase
- farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
- FDPS, mRNA
|
| Enzyme 6 Gene Name |
FDPS |
| Enzyme 6 Protein Sequence |
>Farnesyl diphosphate synthase
MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRA
LCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAI
GGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLD
LLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLE
MGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKE
AEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
|
| Enzyme 6 Number of Residues |
419 |
| Enzyme 6 Molecular Weight |
48276 |
| Enzyme 6 Theoretical pI |
6.02 |
| Enzyme 6 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 6 General Function |
Coenzyme transport and metabolism |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
14603061  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q96G29  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q96G29_HUMAN  |
| Enzyme 6 PDB ID |
1YV5  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
BC010004  |
| Enzyme 6 GeneCard ID |
Q96G29  |
| Enzyme 6 GenAtlas ID |
FDPS  |
| Enzyme 6 HGNC ID |
HGNC:3631  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
15251 |
| Enzyme 7 Name |
TRNA isopentenyltransferase 1 variant (Fragment) |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
TRIT1 |
| Enzyme 7 Protein Sequence |
>TRNA isopentenyltransferase 1 variant (Fragment)
MASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVY
EGLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATALIEDIFARDKIPIVVG
GTNYYIESLLWKVLVNTKPQEMGTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAAKLHPH
DKRKVARSLQVFEETGISHSEFLHRQHTEEGGGPLGGPLKFSNPCILWLHADQAVLDERL
DKRVDDMLAAGLLEELRDFHRRYNQKNVSENSQDYQHGIFQSIGFKEFHEYLITEGKCTL
ETSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPIVPPVYGLEVSDVSKWEESVL
EPALEIVQSFIQGHKPTATPIKMPYNEAENKRSYHLCDLCDRIIIGDREWAAHIKSKSHL
NQLKKRRRLDSDAVNTIESQSVSPDHNKEPKEKGSPGQNDQELMCSV
|
| Enzyme 7 Number of Residues |
467 |
| Enzyme 7 Molecular Weight |
52729 |
| Enzyme 7 Theoretical pI |
8.16 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- nucleic acid binding
- nucleotide binding
- purine nucleotide binding
- tRNA isopentenyltransferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
- transferase activity, transferring alkyl or aryl (other than methyl) groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- RNA metabolism
- RNA processing
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- tRNA processing
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 7 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
62898688  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q53F11  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
Q53F11_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1404 bp
ATGGCGTCCGTGGCGGCTGCACGAGCAGTTCCCGTGGGCAGTGGGCTCAGGGGCCTGCAA
CGGACCCTACCTCTTGTAGTGATTCTCGGGGCCACGGGCACCGGCAAATCCACGCTGGCG
TTGCAGCTAGGCCAGCGGCTCGGCGGTGAGATCGTCAGCGCTGACTCCATGCAGGTCTAT
GAAGGCCTAGACATCATCACCAACAAGGTTTCTGCCCAAGAGCAGAGAATCTGCCGGCAC
CACATGATCAGCTTTGTGGATCCTCTTGTGACCAATTACACAGTGGTGGACTTCAGAAAT
AGAGCAACTGCTCTGATTGAAGATATATTTGCCCGAGACAAAATTCCTATTGTTGTGGGA
GGAACCAATTATTACATTGAATCTCTGCTCTGGAAAGTTCTTGTCAATACCAAGCCCCAG
GAGATGGGCACTGAGAAAGTGATTGACCGAAAAGTGGAGCTTGAAAAGGAGGATGGTCTT
GTACTTCACAAACGCCTAAGCCAGGTGGACCCAGAAATGGCTGCCAAGCTGCATCCACAT
GACAAACGCAAAGTGGCCAGGAGCTTGCAAGTTTTTGAAGAAACAGGAATCTCTCATAGT
GAATTTCTCCATCGTCAACATACGGAAGAAGGTGGTGGTCCCCTTGGAGGTCCTCTGAAG
TTCTCTAACCCTTGCATCCTTTGGCTTCATGCTGACCAGGCAGTTCTAGATGAGCGCTTG
GATAAGAGGGTGGATGACATGCTTGCTGCTGGGCTCTTGGAGGAACTAAGAGATTTTCAC
AGACGCTATAATCAGAAGAATGTTTCGGAAAATAGCCAGGACTATCAACATGGTATCTTC
CAATCAATTGGCTTCAAGGAATTTCACGAGTACCTGATCACTGAGGGAAAATGCACACTG
GAGACTAGTAACCAGCTTCTAAAGAAAGGTATTGAGGCTCTGAAACAAGTAACTAAGAGA
TATGCCCGGAAACAAAACCGATGGGTTAAAAACCGTTTTTTGAGCAGACCTGGTCCCATT
GTCCCCCCTGTCTATGGCTTAGAGGTATCTGATGTCTCGAAGTGGGAAGAGTCTGTTCTT
GAACCTGCTCTTGAAATCGTGCAAAGTTTCATCCAGGGCCACAAGCCTACAGCCACTCCA
ATAAAGATGCCATACAATGAAGCTGAGAACAAGAGAAGTTATCACCTGTGTGACCTCTGT
GATCGAATCATCATTGGGGATCGCGAATGGGCAGCGCACATAAAATCCAAATCCCACTTG
AACCAACTGAAGAAAAGAAGAAGATTGGACTCAGATGCTGTCAACACCATAGAAAGTCAG
AGTGTTTCCCCAGACCATAACAAAGAACCTAAAGAGAAGGGATCCCCAGGGCAGAATGAT
CAAGAGCTGATGTGCAGCGTTTAA
|
| Enzyme 7 GenBank Gene ID |
AK223478  |
| Enzyme 7 GeneCard ID |
Q53F11  |
| Enzyme 7 GenAtlas ID |
TRIT1  |
| Enzyme 7 HGNC ID |
HGNC:20286  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
16716 |
| Enzyme 8 Name |
cDNA FLJ56330, highly similar to Homo sapiens isopentenyl-diphosphate delta isomerase 1 (IDI1), mRNA (Isopentenyl-diphosphate delta isomerase 1, isoform CRA_b) |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
IDI1 |
| Enzyme 8 Protein Sequence |
>cDNA FLJ56330, highly similar to Homo sapiens isopentenyl-diphosphate delta isomerase 1 (IDI1), mRNA (Isopentenyl-diphosphate delta isomerase 1, isoform CRA_b)
MWRGLALARAIGCAARGRGQWAVRAADCAQSGRHPGPAVVCGRRLISVLEQIRHFVMMPE
INTNHLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVFLFNTEN
KLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRAAQRRLKAELGIPLEEV
PPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRKNVTLNPDPNEIKSYCYVSKEELKELL
KKAASGEIKITPWFKIIAATFLFKWWDNLNHLNQFVDHEKIYRM
|
| Enzyme 8 Number of Residues |
284 |
| Enzyme 8 Molecular Weight |
32486 |
| Enzyme 8 Theoretical pI |
7.97 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, transposing C=C bonds
- isomerase activity
- isopentenyl-diphosphate delta-isomerase activity
|
| Process |
- cellular lipid metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 8 General Function |
Lipid transport and metabolism |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
B4E155  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
B4E155_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
AK303669  |
| Enzyme 8 GeneCard ID |
B4E155  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
10 |
| Enzyme 8 Locus |
10p15.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |