|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5313 |
| Enzyme 1 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 1 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase
- ATPDase
- Lymphoid cell activation antigen
- Ecto-apyrase
- CD39 antigen
|
| Enzyme 1 Gene Name |
ENTPD1 |
| Enzyme 1 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 1 Number of Residues |
510 |
| Enzyme 1 Molecular Weight |
57965 |
| Enzyme 1 Theoretical pI |
6.29 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
765256  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
|
| Enzyme 1 GenBank Gene ID |
S73813  |
| Enzyme 1 GeneCard ID |
ENTPD1  |
| Enzyme 1 GenAtlas ID |
ENTPD1  |
| Enzyme 1 HGNC ID |
HGNC:3363  |
| Enzyme 1 Chromosome Location |
10 |
| Enzyme 1 Locus |
10q24 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed
]
- Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed
]
- Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed
]
- Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed
]
- Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed
]
- Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed
]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed
]
- Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5314 |
| Enzyme 2 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 2 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative NF-kappa-B-activating protein 107
- Putative MAPK-activating protein PM09
|
| Enzyme 2 Gene Name |
CANT1 |
| Enzyme 2 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 2 Number of Residues |
401 |
| Enzyme 2 Molecular Weight |
44840 |
| Enzyme 2 Theoretical pI |
5.98 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
22218108  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 2 PDB ID |
1S1D  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
|
| Enzyme 2 GenBank Gene ID |
AF328554  |
| Enzyme 2 GeneCard ID |
CANT1  |
| Enzyme 2 GenAtlas ID |
CANT1  |
| Enzyme 2 HGNC ID |
HGNC:19721  |
| Enzyme 2 Chromosome Location |
17 |
| Enzyme 2 Locus |
17q25.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed
]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed
]
- Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5338 |
| Enzyme 3 Name |
Nucleoside diphosphate kinase, mitochondrial precursor |
| Enzyme 3 Synonyms |
- NDP kinase, mitochondrial
- NDK
- nm23-H4
- Nucleoside diphosphate kinase D
- NDPKD
|
| Enzyme 3 Gene Name |
NME4 |
| Enzyme 3 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 3 Number of Residues |
187 |
| Enzyme 3 Molecular Weight |
20659 |
| Enzyme 3 Theoretical pI |
10.75 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 3 General Function |
Nucleotide transport and metabolism |
| Enzyme 3 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1945762  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 3 PDB ID |
1EHW  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 3 GenBank Gene ID |
Y07604  |
| Enzyme 3 GeneCard ID |
NME4  |
| Enzyme 3 GenAtlas ID |
NME4  |
| Enzyme 3 HGNC ID |
HGNC:7852  |
| Enzyme 3 Chromosome Location |
16 |
| Enzyme 3 Locus |
16p13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
- Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5340 |
| Enzyme 4 Name |
Ribonucleoside-diphosphate reductase large subunit |
| Enzyme 4 Synonyms |
- Ribonucleoside-diphosphate reductase M1 subunit
- Ribonucleotide reductase large chain
|
| Enzyme 4 Gene Name |
RRM1 |
| Enzyme 4 Protein Sequence |
>Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
|
| Enzyme 4 Number of Residues |
792 |
| Enzyme 4 Molecular Weight |
90071 |
| Enzyme 4 Theoretical pI |
7.16 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH2 groups
- oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- protein complex
- ribonucleoside-diphosphate reductase complex
|
|
| Enzyme 4 General Function |
Nucleotide transport and metabolism |
| Enzyme 4 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
36065  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P23921  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
RIR1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
|
| Enzyme 4 GenBank Gene ID |
X59543  |
| Enzyme 4 GeneCard ID |
RRM1  |
| Enzyme 4 GenAtlas ID |
RRM1  |
| Enzyme 4 HGNC ID |
HGNC:10451  |
| Enzyme 4 Chromosome Location |
11 |
| Enzyme 4 Locus |
11p15.5 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed
]
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed
]
- Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed
]
- Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5341 |
| Enzyme 5 Name |
Nucleoside diphosphate kinase A |
| Enzyme 5 Synonyms |
- NDK A
- NDP kinase A
- Tumor metastatic process-associated protein
- Metastasis inhibition factor nm23
- nm23-H1
- Granzyme A-activated DNase
- GAAD
|
| Enzyme 5 Gene Name |
NME1 |
| Enzyme 5 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 5 Number of Residues |
152 |
| Enzyme 5 Molecular Weight |
17149 |
| Enzyme 5 Theoretical pI |
6.11 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 5 General Function |
Nucleotide transport and metabolism |
| Enzyme 5 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
35068  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 5 PDB ID |
1JXV  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
|
| Enzyme 5 GenBank Gene ID |
X17620  |
| Enzyme 5 GeneCard ID |
NME1  |
| Enzyme 5 GenAtlas ID |
NME1  |
| Enzyme 5 HGNC ID |
HGNC:7849  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17q21.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed
]
- Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed
]
- Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed
]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed
]
- Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed
]
- Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed
]
- Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed
]
- Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed
]
- Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5342 |
| Enzyme 6 Name |
Nucleoside diphosphate kinase 7 |
| Enzyme 6 Synonyms |
- NDK 7
- NDP kinase 7
- nm23-H7
|
| Enzyme 6 Gene Name |
NME7 |
| Enzyme 6 Protein Sequence |
>Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 6 Number of Residues |
376 |
| Enzyme 6 Molecular Weight |
42492 |
| Enzyme 6 Theoretical pI |
6.44 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 6 General Function |
Nucleotide transport and metabolism |
| Enzyme 6 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
4960169  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9Y5B8  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
NDK7_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 6 GenBank Gene ID |
AF153191  |
| Enzyme 6 GeneCard ID |
NME7  |
| Enzyme 6 GenAtlas ID |
NME7  |
| Enzyme 6 HGNC ID |
HGNC:20461  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
1q24 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5343 |
| Enzyme 7 Name |
Ribonucleoside-diphosphate reductase M2 subunit |
| Enzyme 7 Synonyms |
- Ribonucleotide reductase small subunit
- Ribonucleotide reductase small chain
|
| Enzyme 7 Gene Name |
RRM2 |
| Enzyme 7 Protein Sequence |
>Ribonucleoside-diphosphate reductase M2 subunit
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
|
| Enzyme 7 Number of Residues |
389 |
| Enzyme 7 Molecular Weight |
44878 |
| Enzyme 7 Theoretical pI |
5.05 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH2 groups
- oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
|
| Process |
- cellular metabolism
- deoxyribonucleoside diphosphate metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside diphosphate metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Nucleotide transport and metabolism |
| Enzyme 7 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
36155  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P31350  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
RIR2_HUMAN  |
| Enzyme 7 PDB ID |
1H0N  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
|
| Enzyme 7 GenBank Gene ID |
X59618  |
| Enzyme 7 GeneCard ID |
RRM2  |
| Enzyme 7 GenAtlas ID |
RRM2  |
| Enzyme 7 HGNC ID |
HGNC:10452  |
| Enzyme 7 Chromosome Location |
2 |
| Enzyme 7 Locus |
2p25-p24 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed
]
- Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5344 |
| Enzyme 8 Name |
Nucleoside diphosphate kinase B |
| Enzyme 8 Synonyms |
- NDK B
- NDP kinase B
- nm23-H2
- C-myc purine-binding transcription factor PUF
|
| Enzyme 8 Gene Name |
NME2 |
| Enzyme 8 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 8 Number of Residues |
152 |
| Enzyme 8 Molecular Weight |
17298 |
| Enzyme 8 Theoretical pI |
8.69 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 8 General Function |
Nucleotide transport and metabolism |
| Enzyme 8 Specific Function |
Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3) |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
4467843  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 8 PDB ID |
1NSK  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 8 GenBank Gene ID |
X58965  |
| Enzyme 8 GeneCard ID |
NME2  |
| Enzyme 8 GenAtlas ID |
NME2  |
| Enzyme 8 HGNC ID |
HGNC:7850  |
| Enzyme 8 Chromosome Location |
17 |
| Enzyme 8 Locus |
17q21.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed
]
- Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed
]
- Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed
]
- Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5345 |
| Enzyme 9 Name |
Nucleoside diphosphate kinase 3 |
| Enzyme 9 Synonyms |
- NDK 3
- NDP kinase 3
- Nucleoside diphosphate kinase C
- NDPKC
- nm23-H3
- DR-nm23
|
| Enzyme 9 Gene Name |
NME3 |
| Enzyme 9 Protein Sequence |
>Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
|
| Enzyme 9 Number of Residues |
169 |
| Enzyme 9 Molecular Weight |
19015 |
| Enzyme 9 Theoretical pI |
7.97 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 9 General Function |
Nucleotide transport and metabolism |
| Enzyme 9 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
1051256  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q13232  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
NDK3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>507 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
|
| Enzyme 9 GenBank Gene ID |
U29656  |
| Enzyme 9 GeneCard ID |
NME3  |
| Enzyme 9 GenAtlas ID |
NME3  |
| Enzyme 9 HGNC ID |
HGNC:7851  |
| Enzyme 9 Chromosome Location |
16 |
| Enzyme 9 Locus |
16q13 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5346 |
| Enzyme 10 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 10 Synonyms |
- NDK 6
- NDP kinase 6
- nm23-H6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
|
| Enzyme 10 Gene Name |
NME6 |
| Enzyme 10 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 10 Number of Residues |
186 |
| Enzyme 10 Molecular Weight |
21142 |
| Enzyme 10 Theoretical pI |
8.49 |
| Enzyme 10 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
3228530  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 10 GenBank Gene ID |
AF051941  |
| Enzyme 10 GeneCard ID |
NME6  |
| Enzyme 10 GenAtlas ID |
NME6  |
| Enzyme 10 HGNC ID |
HGNC:20567  |
| Enzyme 10 Chromosome Location |
3 |
| Enzyme 10 Locus |
3p21 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6009 |
| Enzyme 11 Name |
6-phosphofructokinase type C |
| Enzyme 11 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme C
- PFK-C
- 6- phosphofructokinase, platelet type
|
| Enzyme 11 Gene Name |
PFKP |
| Enzyme 11 Protein Sequence |
>6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
|
| Enzyme 11 Number of Residues |
784 |
| Enzyme 11 Molecular Weight |
85597 |
| Enzyme 11 Theoretical pI |
7.60 |
| Enzyme 11 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 11 General Function |
Carbohydrate transport and metabolism |
| Enzyme 11 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
560105  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q01813  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
K6PP_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
|
| Enzyme 11 GenBank Gene ID |
D25328  |
| Enzyme 11 GeneCard ID |
PFKP  |
| Enzyme 11 GenAtlas ID |
PFKP  |
| Enzyme 11 HGNC ID |
HGNC:8878  |
| Enzyme 11 Chromosome Location |
10 |
| Enzyme 11 Locus |
10p15.3-p15.2 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed
]
- Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6033 |
| Enzyme 12 Name |
6-phosphofructokinase, liver type |
| Enzyme 12 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme B
- PFK-B
|
| Enzyme 12 Gene Name |
PFKL |
| Enzyme 12 Protein Sequence |
>6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
|
| Enzyme 12 Number of Residues |
780 |
| Enzyme 12 Molecular Weight |
85020 |
| Enzyme 12 Theoretical pI |
7.54 |
| Enzyme 12 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 12 General Function |
Carbohydrate transport and metabolism |
| Enzyme 12 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
35431  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P17858  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
K6PL_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
|
| Enzyme 12 GenBank Gene ID |
X15573  |
| Enzyme 12 GeneCard ID |
PFKL  |
| Enzyme 12 GenAtlas ID |
PFKL  |
| Enzyme 12 HGNC ID |
HGNC:8876  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed
]
- Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6037 |
| Enzyme 13 Name |
6-phosphofructokinase, muscle type |
| Enzyme 13 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme A
- PFK-A
- Phosphofructokinase-M
|
| Enzyme 13 Gene Name |
PFKM |
| Enzyme 13 Protein Sequence |
>6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
|
| Enzyme 13 Number of Residues |
780 |
| Enzyme 13 Molecular Weight |
85184 |
| Enzyme 13 Theoretical pI |
8.07 |
| Enzyme 13 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 13 General Function |
Carbohydrate transport and metabolism |
| Enzyme 13 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
1101758  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P08237  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
K6PF_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
|
| Enzyme 13 GenBank Gene ID |
M59741  |
| Enzyme 13 GeneCard ID |
PFKM  |
| Enzyme 13 GenAtlas ID |
PFKM  |
| Enzyme 13 HGNC ID |
HGNC:8877  |
| Enzyme 13 Chromosome Location |
12 |
| Enzyme 13 Locus |
12q13.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed
]
- Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed
]
- Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed
]
- Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed
]
- Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed
]
- Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed
]
- Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed
]
- Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed
]
- Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6041 |
| Enzyme 14 Name |
Pyruvate kinase isozymes R/L |
| Enzyme 14 Synonyms |
- R-type/L-type pyruvate kinase
- Red cell/liver pyruvate kinase
- Pyruvate kinase 1
|
| Enzyme 14 Gene Name |
PKLR |
| Enzyme 14 Protein Sequence |
>Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
|
| Enzyme 14 Number of Residues |
574 |
| Enzyme 14 Molecular Weight |
61831 |
| Enzyme 14 Theoretical pI |
7.83 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Carbohydrate transport and metabolism |
| Enzyme 14 Specific Function |
ATP + pyruvate = ADP + phosphoenolpyruvate |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
3327365  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P30613  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
KPYR_HUMAN  |
| Enzyme 14 PDB ID |
1LIU  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
|
| Enzyme 14 GenBank Gene ID |
AB015983  |
| Enzyme 14 GeneCard ID |
PKLR  |
| Enzyme 14 GenAtlas ID |
PKLR  |
| Enzyme 14 HGNC ID |
HGNC:9020  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
1q21 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed
]
- Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed
]
- Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed
]
- Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed
]
- Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed
]
- Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed
]
- Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed
]
- Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed
]
- Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed
]
- Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed
]
- Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed
]
- Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed
]
- Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed
]
- Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed
]
- Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed
]
- Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed
]
- Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed
]
- Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6159 |
| Enzyme 15 Name |
Ectonucleoside triphosphate diphosphohydrolase 4 |
| Enzyme 15 Synonyms |
- NTPDase 4
- Uridine-diphosphatase
- UDPase
- Lysosomal apyrase-like protein of 70 kDa
|
| Enzyme 15 Gene Name |
ENTPD4 |
| Enzyme 15 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
|
| Enzyme 15 Number of Residues |
616 |
| Enzyme 15 Molecular Weight |
70256 |
| Enzyme 15 Theoretical pI |
8.39 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
3153211  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9Y227  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
ENTP4_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1830 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGG
CGACTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCT
ACAGACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGG
TCTCGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGAT
ATCAGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATT
TCAGAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTT
GCTGCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACG
GCTGGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACC
GATATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGG
AAACAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCAT
ATTGAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAA
GCCATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATA
GCGTACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTG
GGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGG
TTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAA
AAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCC
TGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGA
GGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAAC
GAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAA
TTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGAC
TACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTACTGTGCAACAAAGTGGTCCATT
TTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAG
TATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCT
GTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACC
CTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGAGACATCCAGCAGGAGGCC
TTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTTGTCTACAACCACTACCTGTTC
TCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTGTACCTGCTGCGGCTGCGGCGC
ATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCCCTCTGGATGGAGGAGGGCCTT
CCCGCCCAGAATGCCCCAGGGACCTTGTGA
|
| Enzyme 15 GenBank Gene ID |
AF016032  |
| Enzyme 15 GeneCard ID |
ENTPD4  |
| Enzyme 15 GenAtlas ID |
ENTPD4  |
| Enzyme 15 HGNC ID |
HGNC:14573  |
| Enzyme 15 Chromosome Location |
8 |
| Enzyme 15 Locus |
8p21.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed
]
- Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed
]
- Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed
]
- Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6160 |
| Enzyme 16 Name |
Ectonucleoside triphosphate diphosphohydrolase 6 |
| Enzyme 16 Synonyms |
- NTPDase 6
- CD39 antigen-like 2
|
| Enzyme 16 Gene Name |
ENTPD6 |
| Enzyme 16 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 6
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
|
| Enzyme 16 Number of Residues |
484 |
| Enzyme 16 Molecular Weight |
53248 |
| Enzyme 16 Theoretical pI |
9.52 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
3335098  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O75354  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
ENTP6_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1455 bp
ATGAAAAAAGGTATCCGTTATGAAACTTCCAGAAAAACGAGCTACATTTTTCAGCAGCCG
CAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGCCTGCGGGTG
GCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTTGCCTACATC
AAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCAGCCCCGGGG
GCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGGCACGAGGTC
TTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTCTTCCAGTTC
ACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCAGTGAAGCCA
GGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGGGAACTACTG
GATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTGGTCCTCAAG
GCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTGCAGAAGGTG
AAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCCATCATGAAC
GGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGCAGCTTGAAA
ACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACTCAGATCGCC
TTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTGACGGCACTG
CGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTCGGGCTGATG
TCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGATGGAAAGGAG
TTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCAGAAGTCACG
TACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCTGCCAGAGTG
TCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTGGACTTCTAT
GCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCGGAGAAGGGA
GGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGGACCCTGGAG
ACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGCCTGCTACTC
CAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATTGACAATGTT
GAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAACAGACAGAAG
AGTCCAGCCTCATAG
|
| Enzyme 16 GenBank Gene ID |
AF039916  |
| Enzyme 16 GeneCard ID |
ENTPD6  |
| Enzyme 16 GenAtlas ID |
ENTPD6  |
| Enzyme 16 HGNC ID |
HGNC:3368  |
| Enzyme 16 Chromosome Location |
20 |
| Enzyme 16 Locus |
20p11.2-p11.22 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [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
]
- Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE: CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry. 2000 Oct 24;39(42):12916-23. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6161 |
| Enzyme 17 Name |
Ectonucleoside triphosphate diphosphohydrolase 5 precursor |
| Enzyme 17 Synonyms |
- NTPDase 5
- Nucleoside diphosphatase
- CD39 antigen-like 4
- ER-UDPase
|
| Enzyme 17 Gene Name |
ENTPD5 |
| Enzyme 17 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 5 precursor
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
|
| Enzyme 17 Number of Residues |
428 |
| Enzyme 17 Molecular Weight |
47518 |
| Enzyme 17 Theoretical pI |
6.29 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Likely to promote reglycosylation reactions involved in glycoproteins folding and quality control in the endoplasmic reticulum. Hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
3335102  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O75356  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
ENTP5_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACTTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
|
| Enzyme 17 GenBank Gene ID |
AF039918  |
| Enzyme 17 GeneCard ID |
ENTPD5  |
| Enzyme 17 GenAtlas ID |
ENTPD5  |
| Enzyme 17 HGNC ID |
HGNC:3367  |
| Enzyme 17 Chromosome Location |
14 |
| Enzyme 17 Locus |
14q24 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6586 |
| Enzyme 18 Name |
Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor |
| Enzyme 18 Synonyms |
- PNPase 1
- Polynucleotide phosphorylase-like protein
- PNPase old-35
- 3'-5' RNA exonuclease OLD35
|
| Enzyme 18 Gene Name |
PNPT1 |
| Enzyme 18 Protein Sequence |
>Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISS
GKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRRE
IGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLS
DIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQD
FCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFT
DYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCD
GRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKD
KNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESN
GSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYN
GDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASR
KENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEA
RDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHP
TALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSS
NSQ
|
| Enzyme 18 Number of Residues |
783 |
| Enzyme 18 Molecular Weight |
85952 |
| Enzyme 18 Theoretical pI |
7.86 |
| Enzyme 18 GO Classification |
| Function |
- 3'-5' exonuclease activity
- 3'-5'-exoribonuclease activity
- RNA binding
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotidyltransferase activity
- polyribonucleotide nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- RNA catabolism
- RNA metabolism
- RNA processing
- cellular metabolism
- mRNA catabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 18 Specific Function |
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
20372922  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q8TCS8  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PNPT1_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>2352 bp
ATGGCGGCCTGCAGGTACTGCTGCTCGTGCCTCCGGCTCCGGCCCCTGAGCGATGGTCCT
TTCCTTCTGCCACGGCGGGATCGGGCACTCACCCAGTTGCAAGTGCGAGCACTATGGAGT
AGCGCAGGGTCTCGAGCTGTGGCCGTGGACTTAGGCAACAGGAAATTAGAAATATCTTCT
GGAAAGCTGGCCAGATTTGCAGATGGCTCTGCTGTAGTACAGTCAGGTGACACTGCAGTA
ATGGTCACAGCGGTCAGTAAAACAAAACCTTCCCCTTCCCAGTTTATGCCTTTGGTGGTT
GACTACAGACAAAAAGCTGCTGCAGCAGGTAGAATTCCCACAAACTATCTGAGAAGAGAG
GTTGGTACTTCTGATAAAGAAATTCTAACAAGTCGAATAATAGATCGTTCAATTAGACCG
CTCTTTCCAGCTGGCTACTTCTATGATACACAGGTTCTGTGTAATCTGTTAGCAGTAGAT
GGTGTAAATGAGCCTGATGTCCTAGCAATTAATGGCGCTTCCGTAGCCCTCTCATTATCA
GATATTCCTTGGAATGGACCTGTTGGGGCAGTACGAATAGGAATAATTGATGGAGAATAT
GTTGTTAACCCAACAAGAAAAGAAATGTCTTCTAGTACTTTAAATTTAGTGGTTGCTGGA
GCACCTAAAAGTCAGATTGTCATGTTGGAAGCCTCTGCAGAGAACATTTTACAGCAGGAC
TTTTGCCATGCTATCAAAGTGGGAGTGAAATATACCCAACAAATAATTCAGGGCATTCAG
CAGTTGGTAAAAGAAACTGGTGTTACCAAGAGGACACCTCAGAAGTTATTTACCCCTTCG
CCAGAGATTGTGAAATATACTCATAAACTTGCTATGGAGAGACTCTATGCAGTTTTTACA
GATTACGAGCATGACAAAGTTTCCAGAGATGAAGCTGTTAACAAAATAAGATTAGATACG
GAGGAACAACTAAAAGAAAAATTTCCAGAAGCCGATCCATATGAAATAATAGAATCCTTC
AATGTTGTTGCAAAGGAAGTTTTTAGAAGTATTGTTTTGAATGAATACAAAAGGTGCGAT
GGTCGGGATTTGACTTCACTTAGGAATGTAAGTTGTGAGGTAGATATGTTTAAAACCCTT
CATGGATCAGCATTATTTCAAAGAGGACAAACACAGGTGCTTTGTACCGTTACATTTGAT
TCATTAGAATCTGGTATTAAGTCAGATCAAGTTATAACAGCTATAAATGGGATAAAAGAT
AAAAATTTCATGCTGCACTACGAGTTTCCTCCTTATGCAACTAATGAAATTGGCAAAGTC
ACTGGTTTAAATAGAAGAGAACTTGGGCATGGTGCTCTTGCTGAGAAAGCTTTGTATCCT
GTTATTCCCCGAGATTTTCCTTTCACCATAAGAGTTACATCTGAAGTCCTAGAGTCAAAT
GGGTCATCTTCTATGGCATCTGCATGTGGCGGAAGTTTAGCATTAATGGATTCAGGGGTT
CCAATTTCATCTGCTGTTGCAGGCGTAGCAATAGGATTGGTCACCAAAACCGATCCTGAG
AAGGGTGAAATAGAAGATTATCGTTTGCTGACAGATATTTTGGGAATTGAAGATTACAAT
GGTGACATGGACTTCAAAATAGCTGGCACTAATAAAGGAATAACTGCATTACAGGCTGAT
ATTAAATTACCTGGAATACCAATAAAAATTGTGATGGAGGCTATTCAACAAGCTTCAGTG
GCAAAAAAGGAGATATTACAGATCATGAACAAAACTATTTCAAAACCTCGAGCATCTAGA
AAAGAAAATGGACCTGTTGTAGAAACTGTTCAGGTTCCATTATCAAAACGAGCAAAATTT
GTTGGACCTGGTGGCTATAACTTAAAAAAACTTCAGGCTGAAACAGGTGTAACTATTAGT
CAGGTGGATGAAGAAACGTTTTCTGTATTTGCACCAACACCCAGTGCTATGCATGAGGCA
AGAGACTTCATTACTGAAATCTGCAAGGATGATCAGGAGCAGCAATTAGAATTTGGAGCA
GTATATACCGCCACAATAACTGAAATCAGAGATACTGGTGTAATGGTAAAATTATATCCA
AATATGACTGCGGTACTGCTTCATAACACACAACTTGATCAACGAAAGATTAAACATCCT
ACTGCCCTAGGATTAGAAGTTGGCCAAGAAATTCAGGTGAAATACTTTGGACGTGACCCA
GCCGATGGAAGAATGAGGCTTTCTCGAAAAGTGCTTCAGTCGCCAGCTACAACCGTGGTC
AGAACTTTGAATGACAGAAGTAGTATTGTAATGGGAGAACCTATTTCACAGTCATCATCT
AATTCTCAGTGA
|
| Enzyme 18 GenBank Gene ID |
AJ458465  |
| Enzyme 18 GeneCard ID |
PNPT1  |
| Enzyme 18 GenAtlas ID |
PNPT1  |
| Enzyme 18 HGNC ID |
HGNC:23166  |
| Enzyme 18 Chromosome Location |
2 |
| Enzyme 18 Locus |
2p15 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ: Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol. 2002 Nov 1;323(4):653-63. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
13094 |
| Enzyme 19 Name |
Ribonucleoside-diphosphate reductase subunit M2 B |
| Enzyme 19 Synonyms |
- TP53- inducible ribonucleotide reductase M2 B
- p53-inducible ribonucleotide reductase small subunit 2-like protein
- p53R2
|
| Enzyme 19 Gene Name |
RRM2B |
| Enzyme 19 Protein Sequence |
>Ribonucleoside-diphosphate reductase subunit M2 B
MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQ
ASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA
RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRK
STFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQ
YLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFS
KVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
|
| Enzyme 19 Number of Residues |
351 |
| Enzyme 19 Molecular Weight |
40737 |
| Enzyme 19 Theoretical pI |
4.61 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH2 groups
- oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
|
| Process |
- cellular metabolism
- deoxyribonucleoside diphosphate metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside diphosphate metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Nucleotide transport and metabolism |
| Enzyme 19 Specific Function |
Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294] ALL_REAC R04294 > R02017 R02018 R02019 R02024
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
7229086  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q7LG56  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
RIR2B_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AB036063  |
| Enzyme 19 GeneCard ID |
Q7LG56  |
| Enzyme 19 GenAtlas ID |
RRM2B  |
| Enzyme 19 HGNC ID |
HGNC:17296  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y: A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature. 2000 Mar 2;404(6773):42-9. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
13097 |
| Enzyme 20 Name |
LOC129607 protein |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
LOC129607 |
| Enzyme 20 Protein Sequence |
>LOC129607 protein
RGPLSGPLLGRRGVCAGAMAPPRRFVLELPDCTLAHFALGADAPGDADAPDPRLAALLGP
PERSYSLCVPVTPDAGCGARVRAARLHQRLLHQLRRGPFQRCQLLRLLCYCPGGQAGGAQ
QGFLLRDPLDDPDTRQALLELLGACQEAPRPHLGEFEADPRGQLWQRLWEVQDGRRLQVG
CAQVVPVPEPPLHPVVPDLPSSVVFPDREAARAVLEECTSFIPEARAVLDLVDQCPKQIQ
KGKFQVVAIEGLDATGKTTVTQSVADSLKAVLLKSPPSCIGQWRKIFDDEPTIIRRAFYS
LGNYIVASEIAKESAKSPVIVDRYWHSTATYAIATEVSGGLQHLPPAHHPVYQWPEDLLK
PDLILLLTVSPEERLQRLQGRGMEKTREEAELEANSVFRQKVEMSYQRMENPGCHVVDAS
PSREKVLQTVLSLIQNSFSGP
|
| Enzyme 20 Number of Residues |
441 |
| Enzyme 20 Molecular Weight |
48417 |
| Enzyme 20 Theoretical pI |
6.83 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- thymidylate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- dTDP biosynthesis
- dTTP biosynthesis
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine deoxyribonucleoside diphosphate biosynthesis
- pyrimidine deoxyribonucleoside triphosphate biosynthesis
- pyrimidine nucleoside diphosphate biosynthesis
- pyrimidine nucleoside triphosphate biosynthesis
- pyrimidine nucleotide biosynthesis
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 20 General Function |
Nucleotide 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 |
59808649  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q5EBM0  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
Q5EBM0_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
BC089425  |
| Enzyme 20 GeneCard ID |
Q5EBM0  |
| Enzyme 20 GenAtlas ID |
CMPK2  |
| Enzyme 20 HGNC ID |
HGNC:27015  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
13379 |
| Enzyme 21 Name |
Ectonucleoside triphosphate diphosphohydrolase 8 |
| Enzyme 21 Synonyms |
- NTPDase 8
- NTPDase8
- E-NTPDase 8
|
| Enzyme 21 Gene Name |
ENTPD8 |
| Enzyme 21 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
|
| Enzyme 21 Number of Residues |
495 |
| Enzyme 21 Molecular Weight |
53904 |
| Enzyme 21 Theoretical pI |
4.96 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085] ALL_REAC R00085
- (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
59003409  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q5MY95  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
ENTP8_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCCGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTGCAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
|
| Enzyme 21 GenBank Gene ID |
AY903953  |
| Enzyme 21 GeneCard ID |
Q5MY95  |
| Enzyme 21 GenAtlas ID |
ENTPD8  |
| Enzyme 21 HGNC ID |
HGNC:24860  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
14489 |
| Enzyme 22 Name |
Putative nucleoside diphosphate kinase |
| Enzyme 22 Synonyms |
- NDK
- NDP kinase
|
| Enzyme 22 Gene Name |
NME2P1 |
| Enzyme 22 Protein Sequence |
>Putative nucleoside diphosphate kinase
MQCGLVGKIIKRFEQKGFRLVAMKFLPASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVA
MVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLRFK
PEELVDYKSCAHDWVYE
|
| Enzyme 22 Number of Residues |
137 |
| Enzyme 22 Molecular Weight |
15529 |
| Enzyme 22 Theoretical pI |
8.83 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 22 General Function |
Nucleotide transport and metabolism |
| Enzyme 22 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331] ALL_REAC R00331 > R00124 R00156 R00330 R00570 R00722 R01137 R01857 R02093 R02326 R02331 R03530
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
2935619  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
O60361  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
NDK8_HUMAN  |
| Enzyme 22 PDB ID |
1NSK  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>414 bp
ATGCAGTGCGGCCTGGTGGGCAAGATCATCAAGCGCTTCGAGCAGAAGGGGTTCCGCCTC
GTGGCCATGAAGTTCCTCCCGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTG
AAGGACCGCCCATTCTTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTCGTGGCC
ATGGTCTGGGAGGGGCTGAACGTCGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAAT
CCAGCAGATTCTAAGCCAGGCACCATTCGTGGGGACTTTTGCATTCAGGTTGGCAGGAAC
ATCATTCATGGCAGTGATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTACGGTTTAAG
CCTGAAGAACTGGTTGACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 22 GenBank Gene ID |
AC004263  |
| Enzyme 22 GeneCard ID |
O60361  |
| Enzyme 22 GenAtlas ID |
NME2P1  |
| Enzyme 22 HGNC ID |
HGNC:31358  |
| Enzyme 22 Chromosome Location |
12 |
| Enzyme 22 Locus |
12q24.31 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
14500 |
| Enzyme 23 Name |
Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15 |
| Enzyme 23 Synonyms |
- 8-oxo-dGTPase NUDT15
- Nucleoside diphosphate-linked moiety X motif 15
- Nudix motif 15
|
| Enzyme 23 Gene Name |
NUDT15 |
| Enzyme 23 Protein Sequence |
>Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
MTASAQPRGRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEECA
QRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSEPKNVEPEKNESW
EWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVGYKGNHL
|
| Enzyme 23 Number of Residues |
164 |
| Enzyme 23 Molecular Weight |
18609 |
| Enzyme 23 Theoretical pI |
6.08 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Nucleotide transport and metabolism |
| Enzyme 23 Specific Function |
Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8- oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. Its substrate specificity in vivo however remains unclear |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
7023325  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9NV35  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
NUD15_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>495 bp
ATGACGGCCAGCGCACAGCCGCGCGGGCGGCGGCCAGGAGTCGGAGTCGGAGTCGTGGTG
ACCAGCTGCAAGCATCCGCGTTGCGTCCTCCTGGGGAAGAGGAAAGGCTCGGTTGGAGCT
GGCAGTTTCCAACTCCCTGGAGGTCATCTGGAGTTCGGTGAAACCTGGGAAGAATGTGCT
CAAAGGGAAACCTGGGAAGAAGCAGCTCTTCACCTGAAAAATGTTCACTTTGCCTCAGTT
GTGAATTCTTTCATTGAGAAGGAGAATTACCATTATGTTACTATATTAATGAAAGGAGAA
GTGGATGTGACTCATGATTCAGAACCAAAGAATGTAGAGCCTGAAAAAAATGAAAGTTGG
GAGTGGGTTCCTTGGGAAGAACTACCTCCCCTGGACCAGCTTTTCTGGGGACTGCGTTGT
TTAAAAGAACAAGGCTATGATCCATTTAAAGAAGATCTGAACCATCTGGTGGGATACAAA
GGAAATCATCTCTAG
|
| Enzyme 23 GenBank Gene ID |
AK001818  |
| Enzyme 23 GeneCard ID |
Q9NV35  |
| Enzyme 23 GenAtlas ID |
NUDT15  |
| Enzyme 23 HGNC ID |
HGNC:23063  |
| Enzyme 23 Chromosome Location |
13 |
| Enzyme 23 Locus |
13q14.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
14501 |
| Enzyme 24 Name |
Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor |
| Enzyme 24 Synonyms |
- Nudix motif 17
|
| Enzyme 24 Gene Name |
NUDT17 |
| Enzyme 24 Protein Sequence |
>Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
MAEVRVQLLLSRRPESVSFARSVCGLLGAGPGLGTWPIHCSLKRGRLVLSSRPFPGASAR
LPLQRPPFCPFAALEERPRVPGAELPTDRGVDLGVAVILQSSDKTVLLTRRARTLSVSPN
LWVPPGGHVELEEELLDGGLRELWEESGLHLPQGQFSWVPLGLWESAYPPRLSWGLPKYH
HIVLYLLVISQESQQQLQARIQPNPNEVSALMWLTPDVAAAVAAAEDGTETPGLLPQDLP
PSVLAVELEEDGRARPLVLHMSTLLRMIPTMAEDKERVSTGTKFALKLWLQHLGR
|
| Enzyme 24 Number of Residues |
295 |
| Enzyme 24 Molecular Weight |
32448 |
| Enzyme 24 Theoretical pI |
6.89 |
| Enzyme 24 GO Classification |
Not Available |
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P0C025  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
NUD17_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
Not Available |
| Enzyme 24 GenBank Gene ID |
AL160282  |
| Enzyme 24 GeneCard ID |
P0C025  |
| Enzyme 24 GenAtlas ID |
NUDT17  |
| Enzyme 24 HGNC ID |
HGNC:26618  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
14502 |
| Enzyme 25 Name |
Nucleoside diphosphate-linked moiety X motif 18 |
| Enzyme 25 Synonyms |
- Nudix motif 18
|
| Enzyme 25 Gene Name |
Not Available |
| Enzyme 25 Protein Sequence |
>Nucleoside diphosphate-linked moiety X motif 18
MRISFKAGVYVPHPTGHVTFITLWWNEKKGIWDMINSGNAIVCLRQQRDSGSRGRPRASV
TSPDCRVTVAYPGGATRPAGKMTSPSELLQTSARSGSWRAGGGWETSRAHGTDRRQKPGG
VRWAPDPCPPSSRAAPGGPAPSVNAAGRPIRAGRGAAQPISGQSSRALPRSRALPRSREL
PARCRRDWERAPQRTLARGSAQSVCEDPARRPPGDPMASEGLAGALASVLAGQGSSVHSC
DSAPAGEPPAPVRLRKNVCYVVLAVFLSEQDEVLLIQEAKRECRGSWYLPAGRMEPGETI
VEALQREVKEEAGLHCEPETLLSVEERGPSWVRFVFLARPTGGILKTSKEADAESLQAAW
YPRTSLPTPLRAHDILHLVELAAQYRQQARHPLILPQELPCDLVCQRLVATFTSAQTVWV
LVGTVGMPHLPVTACGLDPVEQRGGMKMAVLRLLQECLTLHHLVVEIKGLLGLQHLGRDH
SDGICLNVLVTVAFRSPGIQDEPPKVRGENFSWWKVMEEDLQSQLLQRLQGSSVVPVNR
|
| Enzyme 25 Number of Residues |
539 |
| Enzyme 25 Molecular Weight |
58665 |
| Enzyme 25 Theoretical pI |
9.42 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Nucleotide transport and metabolism |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
34530231  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q6ZVK8  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
Q6ZVK8_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1620 bp
ATGCGAATCTCCTTCAAGGCAGGGGTTTATGTCCCCCACCCCACGGGCCATGTGACATTT
ATAACTCTTTGGTGGAATGAGAAGAAAGGTATTTGGGATATGATCAACTCCGGCAATGCC
ATTGTGTGTTTACGGCAACAGCGGGACAGTGGTTCCAGGGGGCGGCCCCGGGCCTCCGTG
ACGTCACCGGATTGTCGCGTCACCGTCGCCTACCCCGGCGGCGCAACGCGCCCTGCAGGA
AAGATGACGTCACCGTCGGAGCTCCTGCAGACCAGTGCGCGCTCGGGGAGTTGGCGAGCG
GGTGGCGGCTGGGAGACGTCCCGAGCGCACGGGACTGACAGGCGGCAGAAGCCGGGCGGG
GTCCGCTGGGCTCCGGACCCGTGCCCCCCCAGTTCCAGGGCGGCCCCGGGCGGCCCCGCC
CCCTCGGTGAATGCCGCGGGCCGGCCAATCCGGGCAGGCCGCGGCGCCGCGCAGCCTATC
AGCGGCCAGAGCTCGCGTGCGCTTCCGCGTTCGCGTGCGCTTCCGCGTTCTCGTGAGCTC
CCGGCCCGCTGCCGCAGGGACTGGGAGCGGGCTCCGCAGCGCACTCTAGCCCGCGGCTCG
GCTCAGTCGGTCTGCGAGGATCCGGCCCGCCGCCCCCCGGGGGACCCGATGGCCTCGGAG
GGCCTGGCGGGGGCGCTGGCTTCCGTGCTGGCTGGCCAGGGGTCCAGCGTGCACAGCTGC
GACTCGGCGCCGGCCGGGGAGCCGCCGGCGCCCGTGCGGCTGCGGAAGAACGTGTGCTAC
GTGGTGCTGGCCGTGTTCCTCAGCGAGCAGGATGAGGTGCTACTGATCCAGGAGGCCAAG
AGGGAGTGCCGGGGGTCGTGGTACCTGCCTGCGGGGAGAATGGAGCCAGGGGAGACCATC
GTGGAGGCGCTGCAGCGGGAGGTGAAGGAGGAGGCGGGGCTGCACTGTGAGCCCGAGACA
CTGCTGTCCGTGGAGGAGCGGGGCCCCTCCTGGGTCCGCTTCGTGTTCCTCGCTCGCCCC
ACAGGTGGAATTCTCAAGACTTCCAAGGAGGCCGATGCGGAGTCCCTGCAGGCTGCCTGG
TACCCACGGACCTCCCTGCCCACTCCGCTGCGAGCCCATGACATCCTGCACCTGGTTGAA
CTAGCCGCCCAGTATCGCCAGCAAGCCAGGCACCCTCTCATTCTGCCCCAAGAGCTACCC
TGTGATCTGGTCTGCCAGCGGCTCGTGGCTACCTTTACCAGCGCCCAGACAGTGTGGGTG
TTAGTGGGCACAGTGGGGATGCCTCACTTGCCTGTCACTGCCTGTGGCCTCGACCCTGTG
GAGCAGAGGGGTGGCATGAAGATGGCCGTCCTGCGGCTGCTGCAGGAGTGTCTGACCCTG
CACCACTTGGTGGTGGAGATCAAGGGGTTGCTTGGACTGCAGCACCTGGGCCGAGATCAC
AGTGATGGCATCTGTTTGAATGTGCTGGTGACCGTGGCTTTTCGGAGCCCAGGGATCCAG
GATGAACCCCCAAAAGTTCGGGGTGAGAACTTCTCTTGGTGGAAGGTGATGGAGGAAGAC
CTGCAAAGCCAGCTCCTCCAGCGGCTTCAGGGATCCTCTGTTGTCCCAGTGAACAGATAG
|
| Enzyme 25 GenBank Gene ID |
AK124446  |
| Enzyme 25 GeneCard ID |
Q6ZVK8  |
| Enzyme 25 GenAtlas ID |
NUDT18  |
| Enzyme 25 HGNC ID |
HGNC:26194  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
Not Available |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
14507 |
| Enzyme 26 Name |
Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor |
| Enzyme 26 Synonyms |
- Nudix motif 8
|
| Enzyme 26 Gene Name |
NUDT8 |
| Enzyme 26 Protein Sequence |
>Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
MLPDCLSAEGELRCRRLLAGATARLRARPASAAVLVPLCSVRGVPALLYTLRSSRLTGRH
KGDVSFPGGKCDPADQDVVHTALRETREELGLAVPEEHVWGLLRPVYDPQKATVVPVLAG
VGPLDPQSLRPNSEEVDEVFALPLAHLLQTQNQGYTHFCRGGHFRYTLPVFLHGPHRVWG
LTAVITEFALQLLAPGTYQPRLAGLTCSGAEGLARPKQPLASPCQASSTPGLNKGL
|
| Enzyme 26 Number of Residues |
236 |
| Enzyme 26 Molecular Weight |
25371 |
| Enzyme 26 Theoretical pI |
8.50 |
| Enzyme 26 GO Classification |
Not Available |
| Enzyme 26 General Function |
Replication, recombination and repair |
| Enzyme 26 Specific Function |
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
34529139  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q8WV74  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
NUDT8_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>711 bp
ATGCTGCCCGACTGCCTGTCGGCCGAGGGCGAGCTGCGCTGCCGCCGGCTGCTGGCAGGG
GCCACGGCCCGGCTCCGCGCGCGGCCCGCGTCGGCCGCGGTGCTCGTGCCGCTCTGCTCA
GTGCGTGGGGTCCCGGCGCTGCTGTACACGCTGCGGTCCAGCCGCCTGACCGGGAGGCAC
AAGGGCGACGTCAGTTTCCCAGGCGGCAAGTGCGACCCGGCTGACCAAGATGTGGTGCAC
ACGGCCCTGCGGGAAACCCGGGAGGAGCTGGGCCTGGCAGTGCCCGAGGAGCACGTGTGG
GGCCTGCTGCGGCCTGTGTATGATCCGCAAAAGGCCACCGTGGTGCCAGTGCTTGCTGGT
GTAGGCCCACTGGATCCCCAGAGCCTCAGGCCCAACTCGGAGGAGGTAGATGAGGTGTTT
GCACTGCCGCTGGCCCACCTGCTGCAGACGCAGAATCAGGGCTATACCCACTTCTGCCGG
GGTGGCCACTTCCGCTACACACTACCCGTCTTCCTGCATGGACCACACCGGGTCTGGGGC
CTCACAGCTGTCATCACTGAGTTTGCCCTGCAGCTGCTGGCACCTGGTACCTACCAGCCC
CGCCTGGCCGGCCTGACCTGCTCAGGGGCTGAGGGTCTGGCCCGCCCTAAGCAGCCCCTG
GCTTCACCCTGTCAGGCCAGCTCCACTCCAGGACTGAATAAAGGTCTTTGA
|
| Enzyme 26 GenBank Gene ID |
AK123561  |
| Enzyme 26 GeneCard ID |
Q8WV74  |
| Enzyme 26 GenAtlas ID |
NUDT8  |
| Enzyme 26 HGNC ID |
HGNC:8055  |
| Enzyme 26 Chromosome Location |
11 |
| Enzyme 26 Locus |
11q13.2 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
14908 |
| Enzyme 27 Name |
Transmembrane protein 15 |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
TMEM15 |
| Enzyme 27 Protein Sequence |
>Transmembrane protein 15
MTRECPSPAPGPGAPLSGSVLAEAAVVFAVVLSIHATVWDRYSWCAVALAVQAFYVQYKW
DRLLQQGSAVFQFRMSANSGLLPASMVMPLLGLVMKERCQTAGNPFFERFGIVVAATGMA
VALFSSVLALGITRPVPTNTCVILGLAGGVIIYIMKHSLSVGEVIEVLEVLLIFVYLNMI
LLYLLPRCFTPGEALLVLGGISFVLNQLIKRSLTLVESQGDPVDFFLLVVVVGMVLMGIF
FSTLFVFMDSGTWASSIFFHLMTCVLSLGVVLPWLHRLIRRNPLLWLLQFLFQTDTRIYL
LAYWSLLATLACLVVLYQNAKRSSSESKKHQAPTIARKYFHLIVVATYIPGIIFDRPLLY
VAATVCLAVFIFLEYVRYFRIKPLGHTLRSFLSLFLDERDSGPLILTHIYLLLGMSLPIW
LIPRPCTQKGSLGGARALVPYAGVLAVGVGDTVASIFGSTMGEIRWPGTKKTFEGTMTSI
FAQIISVALILIFDSGVDLNYSYAWILGSISTVSLLEAYTTQIDNLLLPLYLLILLMA
|
| Enzyme 27 Number of Residues |
538 |
| Enzyme 27 Molecular Weight |
59269 |
| Enzyme 27 Theoretical pI |
8.71 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- phosphatidate cytidylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 27 General Function |
Lipid transport and metabolism |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
- 14-34
75-95
112-132
135-155
164-184
189-209
225-245
255-275
298-318
352-372
402-422
437-457
473-493
496-516
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
40789043  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q9UPQ8  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
TMM15_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1635 bp
AGCCCCAGGTCTAGAGATATGACCCGAGAGTGCCCATCTCCGGCCCCGGGGCCTGGGGCT
CCGCTGAGTGGATCGGTGCTGGCAGAGGCGGCAGTAGTGTTTGCAGTGGTGCTGAGCATC
CACGCAACCGTATGGGACCGATACTCGTGGTGCGCCGTGGCCCTCGCAGTGCAGGCGTTC
TACGTCCAATACAAGTGGGACCGGCTGCTACAGCAGGGAAGCGCCGTCTTCCAGTTCCGA
ATGTCCGCAAACAGTGGCCTATTGCCCGCCTCCATGGTCATGCCTTTGCTTGGACTAGTC
ATGAAGGAGCGGTGCCAGACTGCTGGGAACCCGTTCTTTGAGCGTTTTGGCATTGTGGTG
GCAGCCACTGGCATGGCAGTGGCCCTCTTCTCATCAGTGTTGGCGCTCGGCATCACTCGC
CCAGTGCCAACCAACACTTGTGTCATCTTGGGCTTGGCTGGAGGTGTTATCATTTATATC
ATGAAGCACTCGTTGAGCGTGGGGGAGGTGATCGAAGTCCTGGAAGTCCTTCTGATCTTC
GTTTATCTCAACATGATCCTGCTGTACCTGCTGCCCCGCTGCTTCACCCCTGGTGAGGCA
CTGCTGGTATTGGGTGGCATTAGCTTTGTCCTCAACCAGCTCATCAAGCGCTCTCTGACA
CTGGTGGAAAGTCAGGGGGACCCAGTGGACTTCTTCCTGCTGGTGGTGGTAGTAGGGATG
GTACTCATGGGCATTTTCTTCAGCACTCTGTTTGTCTTCATGGACTCAGGCACCTGGGCC
TCCTCCATCTTCTTCCACCTCATGACCTGTGTGCTGAGCCTTGGTGTGGTCCTACCCTGG
CTGCACCGGCTCATCCGCAGGAATCCCCTGCTCTGGCTTCTTCAGTTTCTCTTCCAGACA
GACACCCGCATCTACCTCCTAGCCTATTGGTCTCTGCTGGCCACCTTGGCCTGCCTGGTG
GTGCTGTACCAGAATGCCAAGCGGTCATCTTCCGAGTCCAAGAAGCACCAGGCCCCCACC
ATCGCCCGAAAGTATTTCCACCTCATTGTGGTAGCCACCTACATCCCAGGTATCATCTTT
GACCGGCCACTGCTCTATGTAGCCGCCACTGTATGCCTGGCGGTCTTCATCTTCCTGGAG
TATGTGCGCTACTTCCGCATCAAGCCTTTGGGTCACACTCTACGGAGCTTCCTGTCCCTT
TTTCTGGATGAACGAGACAGTGGACCACTCATTCTGACACACATCTACCTGCTCCTGGGC
ATGTCTCTTCCCATCTGGCTGATCCCCAGACCCTGCACACAGAAGGGTAGCCTGGGAGGA
GCCAGGGCCCTCGTCCCCTATGCCGGTGTCCTGGCTGTGGGTGTGGGTGATACTGTGGCC
TCCATCTTCGGTAGCACCATGGGGGAGATCCGCTGGCCTGGAACCAAAAAGACTTTTGAG
GGGACCATGACATCTATATTTGCGCAGATCATTTCTGTAGCTCTGATCTTAATCTTTGAC
AGTGGAGTGGACCTAAACTACAGTTATGCTTGGATTTTGGGGTCCATCAGCACTGTGTCC
CTCCTGGAAGCATACACTACACAGATAGACAATCTCCTTCTGCCTCTCTACCTCCTGATA
TTGCTGATGGCCTAG
|
| Enzyme 27 GenBank Gene ID |
AB029017  |
| Enzyme 27 GeneCard ID |
Q9UPQ8  |
| Enzyme 27 GenAtlas ID |
DOLK  |
| Enzyme 27 HGNC ID |
HGNC:23406  |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed
]
- 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 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
15191 |
| Enzyme 28 Name |
cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a) |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
NME7 |
| Enzyme 28 Protein Sequence |
>cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 28 Number of Residues |
376 |
| Enzyme 28 Molecular Weight |
42492 |
| Enzyme 28 Theoretical pI |
6.44 |
| Enzyme 28 GO Classification |
Not Available |
| Enzyme 28 General Function |
Nucleotide transport and metabolism |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
Not Available |
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
158254838  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 28 GenBank Gene ID |
AK290701  |
| Enzyme 28 GeneCard ID |
A8K3T6  |
| Enzyme 28 GenAtlas ID |
Not Available |
| Enzyme 28 HGNC ID |
Not Available |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
16437 |
| Enzyme 29 Name |
cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b) |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
ENTPD3 |
| Enzyme 29 Protein Sequence |
>cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 29 Number of Residues |
529 |
| Enzyme 29 Molecular Weight |
59106 |
| Enzyme 29 Theoretical pI |
6.40 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
Not Available |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
B2R8D0  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
B2R8D0_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
Not Available |
| Enzyme 29 GenBank Gene ID |
AK313322  |
| Enzyme 29 GeneCard ID |
B2R8D0  |
| Enzyme 29 GenAtlas ID |
Not Available |
| Enzyme 29 HGNC ID |
Not Available |
| Enzyme 29 Chromosome Location |
Not Available |
| Enzyme 29 Locus |
Not Available |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
16476 |
| Enzyme 30 Name |
cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e) |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
PKM2 |
| Enzyme 30 Protein Sequence |
>cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
|
| Enzyme 30 Number of Residues |
531 |
| Enzyme 30 Molecular Weight |
57938 |
| Enzyme 30 Theoretical pI |
7.94 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Carbohydrate transport and metabolism |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
Not Available |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
B2R5N8  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
B2R5N8_HUMAN  |
| Enzyme 30 PDB ID |
1F3X  |
| Enzyme 30 PDB File |
Show |
| Enzyme 30 3D Structure |
|
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
Not Available |
| Enzyme 30 GenBank Gene ID |
AK312253  |
| Enzyme 30 GeneCard ID |
B2R5N8  |
| Enzyme 30 GenAtlas ID |
Not Available |
| Enzyme 30 HGNC ID |
Not Available |
| Enzyme 30 Chromosome Location |
15 |
| Enzyme 30 Locus |
15q22 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
Not Available |
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
17697 |
| Enzyme 31 Name |
Nucleoside diphosphate kinase |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
NME4 |
| Enzyme 31 Protein Sequence |
>Nucleoside diphosphate kinase
MKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSA
EAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
|
| Enzyme 31 Number of Residues |
117 |
| Enzyme 31 Molecular Weight |
12978.5 |
| Enzyme 31 Theoretical pI |
6.80 |
| Enzyme 31 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 31 General Function |
Nucleotide transport and metabolism |
| Enzyme 31 Specific Function |
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
123243687  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
A2IDD0  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
A2IDD0_HUMAN  |
| Enzyme 31 PDB ID |
1EHW  |
| Enzyme 31 PDB File |
Show |
| Enzyme 31 3D Structure |
|
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>471 bp
ATGGCGCTGAAAGCAAAGAAGGAAGCTCCTGCCTCTCCTGAAGCCGAAGCCAAAGCGAAG
GCTTTAAAGGCCAAGAAGGCAGCGTTGAAAGGTGTCCACAGCCACATAAAAAAGAAGACC
CGCACGTCACTCACCTTCCAGCGGCCCAAGACACTGCGACGCCGGAGGCGGCCTGAATAT
CCTTGGAAGAGCACCCCCAGGAGAAACAAGCTTGGCCACTATGCTGTCATCAAGTTTCCG
CTGACCACGGAGTCGGCCGTGAAGAGGACAGAAGAAAACAACACGCTTTTGTTCACTGTG
GATGTTAAAGCCAACAAGCACCAGATCAAACAGGCTGTGAAGAAGCTCTATGACGGTGAT
GTGGCCGAGGTCACCACCCTGATTCCGCCTGATGGAGAGAAGAAGGCATGTGTTCGACTG
GCTCCTGATTACGATGCGTTGGATGTTGCCAACAAAATTGGGATCATCTAA
|
| Enzyme 31 GenBank Gene ID |
Z97634  |
| Enzyme 31 GeneCard ID |
NME4  |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
HGNC:7852  |
| Enzyme 31 Chromosome Location |
1 |
| Enzyme 31 Locus |
16p13.3 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |