We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for dADP (HMDB01508)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:49
Accession Number HMDB01508
Secondary Accession Numbers Not Available
Common Name dADP
Description Deoxyadenosine diphosphate has been identified in the mononuclear cells of a patient affected with in inherited adenosine deaminase deficiency (OMIM 102700) (PMID 6980023), and in in mononuclear cells of hemodialyzed patients. (PMID 11461945)
Synonyms
  1. 2'-deoxyadenosine-5'-diphosphate
  2. dADP
  3. deoxyadenosine diphosphate
Chemical IUPAC Name [[(2R,3S,5R)-5-(6-aminopurin-9-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C10H15N5O9P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • DNA component
Application
Source
  • Endogenous
Average Molecular Weight 411.202
Monoisotopic Molecular Weight 411.034485
Isomeric SMILES NC1=NC=NC2=C1N=CN2C1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(O)=O)O1
Canonical SMILES NC1=NC=NC2=C1N=CN2C1CC(O)C(COP(O)(=O)OP(O)(O)=O)O1
KEGG Compound ID C00206 Link Image
BioCyc ID DADP Link Image
BiGG ID 34254 Link Image
Wikipedia Link deoxyadenosine diphosphate Link Image
NuGOwiki Link HMDB01508 Link Image
Metagene Link HMDB01508 Link Image
METLIN ID 6286 Link Image
PubChem Compound 188966 Link Image
PubChem Substance 3506 Link Image
ChEBI ID 16174 Link Image
CAS Registry Number 2793-06-8
InChI Identifier InChI=1/C10H15N5O9P2/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(23-7)2-22-26(20,21)24-25(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7-/m0/s1
Synthesis Reference Nara, Takashi; Misawa, Masanaru. Bacterial phosphorylation of 5'-deoxyadenosine monophosphate to di- or triphosphate. Jpn. Tokkyo Koho (1971), 2 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.80 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.57 [Predicted by ALOGPS]; -3.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location
Tissue References
Cartilage
Epidermis
Fibroblasts
Neuron
Platelet
Skeletal Muscle
Spleen
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Cartwright PH, Ilchyshyn A, Ilderton E, Yardley HJ: Modulation of phospholipase A2 activity in extracts of lesion-free psoriatic epidermis by alkaline phosphatase and a protein phosphatase inhibitor. Br J Dermatol. 1988 Mar;118(3):333-8. [PubMed Link Image]
  2. Doherty M, Belcher C, Regan M, Jones A, Ledingham J: Association between synovial fluid levels of inorganic pyrophosphate and short term radiographic outcome of knee osteoarthritis. Ann Rheum Dis. 1996 Jul;55(7):432-6. [PubMed Link Image]
  3. Chen SD, Kao CH, Poon SK: Radionuclide imaging in primary amyloidosis with liver involvement. Clin Nucl Med. 1998 Jun;23(6):374-6. [PubMed Link Image]
  4. Yepes M, Moore E, Brown SA, Hanscom HN, Smith EP, Lawrence DA, Winkles JA: Progressive ankylosis (Ank) protein is expressed by neurons and Ank immunohistochemical reactivity is increased by limbic seizures. Lab Invest. 2003 Jul;83(7):1025-32. [PubMed Link Image]
  5. Blackburn MR, Datta SK, Kellems RE: Adenosine deaminase-deficient mice generated using a two-stage genetic engineering strategy exhibit a combined immunodeficiency. J Biol Chem. 1998 Feb 27;273(9):5093-100. [PubMed Link Image]
  6. Beltran J, Marty-Delfaut E, Bencardino J, Rosenberg ZS, Steiner G, Aparisi F, Padron M: Chondrocalcinosis of the hyaline cartilage of the knee: MRI manifestations. Skeletal Radiol. 1998 Jul;27(7):369-74. [PubMed Link Image]
  7. Grubenmann CE, Frank CG, Kjaergaard S, Berger EG, Aebi M, Hennet T: ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum Mol Genet. 2002 Sep 15;11(19):2331-9. [PubMed Link Image]
  8. Rother E, Brandl R, Baker DL, Goyal P, Gebhard H, Tigyi G, Siess W: Subtype-selective antagonists of lysophosphatidic Acid receptors inhibit platelet activation triggered by the lipid core of atherosclerotic plaques. Circulation. 2003 Aug 12;108(6):741-7. Epub 2003 Jul 28. [PubMed Link Image]
  9. Collins ML, Eng S, Hoh R, Hellerstein MK: Measurement of mitochondrial DNA synthesis in vivo using a stable isotope-mass spectrometric technique. J Appl Physiol. 2003 Jun;94(6):2203-11. Epub 2003 Jan 31. [PubMed Link Image]
  10. Cavusoglu Y, Entok E, Gorenek B, Kudaiberdieva G, Unalir A, Goktekin O, Birdane A, Ata N, Timuralp B: Reversible myoglobinuric renal failure following rhabdomyolysis as a rare complication of cardioversion. Pacing Clin Electrophysiol. 2003 Feb;26(2 Pt 1):645-6. [PubMed Link Image]
  11. Zaka R, Williams CJ: Role of the progressive ankylosis gene in cartilage mineralization. Curr Opin Rheumatol. 2006 Mar;18(2):181-6. [PubMed Link Image]
  12. Johnson K, Hashimoto S, Lotz M, Pritzker K, Goding J, Terkeltaub R: Up-regulated expression of the phosphodiesterase nucleotide pyrophosphatase family member PC-1 is a marker and pathogenic factor for knee meniscal cartilage matrix calcification. Arthritis Rheum. 2001 May;44(5):1071-81. [PubMed Link Image]
  13. Imbach T, Schenk B, Schollen E, Burda P, Stutz A, Grunewald S, Bailie NM, King MD, Jaeken J, Matthijs G, Berger EG, Aebi M, Hennet T: Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie. J Clin Invest. 2000 Jan;105(2):233-9. [PubMed Link Image]
  14. Ryan LM, Rosenthal AK: Metabolism of extracellular pyrophosphate. Curr Opin Rheumatol. 2003 May;15(3):311-4. [PubMed Link Image]
  15. Wikipedia Link Image
Metabolic Enzymes
  1. Nucleoside diphosphate kinase, mitochondrial precursor
  2. Ribonucleoside-diphosphate reductase large subunit
  3. Nucleoside diphosphate kinase A
  4. Ribonucleoside-diphosphate reductase M2 subunit
  5. Nucleoside diphosphate kinase B
  6. Nucleoside diphosphate kinase 6
  7. Glucokinase
  8. Hexokinase-3
  9. Hexokinase-2
  10. Adenylate kinase isoenzyme 1
  11. Putative adenylate kinase 7
  12. Adenylate kinase isoenzyme 5
  13. Pyruvate kinase isozymes R/L
  14. Uridine-cytidine kinase 2
  15. Ribonucleoside-diphosphate reductase subunit M2 B
  16. Uridine/cytidine kinase-like 1
  17. cDNA FLJ78347, highly similar to Homo sapiens adenylate kinase 2 (AK2), transcript variant AK2A, mRNA (Adenylate kinase 2, isoform CRA_d)
  18. 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)
  19. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  20. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  21. cDNA, FLJ94180, Homo sapiens adenylate kinase 3 (AK3), mRNA (AK3L2 protein)
  22. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 1 [top]
Enzyme 1 ID 5338
Enzyme 1 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 1 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 1 Gene Name NME4
Enzyme 1 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 1 Number of Residues 187
Enzyme 1 Molecular Weight 20659
Enzyme 1 Theoretical pI 10.75
Enzyme 1 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 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-15
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1945762 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 1 PDB ID 1EHW Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 1 GenBank Gene ID Y07604 Link Image
Enzyme 1 GeneCard ID NME4 Link Image
Enzyme 1 GenAtlas ID NME4 Link Image
Enzyme 1 HGNC ID HGNC:7852 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5340
Enzyme 2 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 2 Synonyms
  1. Ribonucleoside-diphosphate reductase M1 subunit
  2. Ribonucleotide reductase large chain
Enzyme 2 Gene Name RRM1
Enzyme 2 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 2 Number of Residues 792
Enzyme 2 Molecular Weight 90071
Enzyme 2 Theoretical pI 7.16
Enzyme 2 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 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 36065 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID X59543 Link Image
Enzyme 2 GeneCard ID RRM1 Link Image
Enzyme 2 GenAtlas ID RRM1 Link Image
Enzyme 2 HGNC ID HGNC:10451 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11p15.5
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5341
Enzyme 3 Name Nucleoside diphosphate kinase A
Enzyme 3 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 3 Gene Name NME1
Enzyme 3 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 3 Number of Residues 152
Enzyme 3 Molecular Weight 17149
Enzyme 3 Theoretical pI 6.11
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
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 35068 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 3 PDB ID 1JXV Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 3 GenBank Gene ID X17620 Link Image
Enzyme 3 GeneCard ID NME1 Link Image
Enzyme 3 GenAtlas ID NME1 Link Image
Enzyme 3 HGNC ID HGNC:7849 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5343
Enzyme 4 Name Ribonucleoside-diphosphate reductase M2 subunit
Enzyme 4 Synonyms
  1. Ribonucleotide reductase small subunit
  2. Ribonucleotide reductase small chain
Enzyme 4 Gene Name RRM2
Enzyme 4 Protein Sequence >Ribonucleoside-diphosphate reductase M2 subunit
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 4 Number of Residues 389
Enzyme 4 Molecular Weight 44878
Enzyme 4 Theoretical pI 5.05
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
  • cellular metabolism
  • deoxyribonucleoside diphosphate metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside diphosphate metabolism
  • nucleotide metabolism
  • physiological process
Component
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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 36155 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 4 PDB ID 1H0N Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID X59618 Link Image
Enzyme 4 GeneCard ID RRM2 Link Image
Enzyme 4 GenAtlas ID RRM2 Link Image
Enzyme 4 HGNC ID HGNC:10452 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2p25-p24
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5344
Enzyme 5 Name Nucleoside diphosphate kinase B
Enzyme 5 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 5 Gene Name NME2
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17298
Enzyme 5 Theoretical pI 8.69
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 Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4467843 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 5 PDB ID 1NSK Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 5 GenBank Gene ID X58965 Link Image
Enzyme 5 GeneCard ID NME2 Link Image
Enzyme 5 GenAtlas ID NME2 Link Image
Enzyme 5 HGNC ID HGNC:7850 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5346
Enzyme 6 Name Nucleoside diphosphate kinase 6
Enzyme 6 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 6 Gene Name NME6
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 6 Number of Residues 186
Enzyme 6 Molecular Weight 21142
Enzyme 6 Theoretical pI 8.49
Enzyme 6 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 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. Inhibitor of p53-induced apoptosis
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3228530 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 6 GenBank Gene ID AF051941 Link Image
Enzyme 6 GeneCard ID NME6 Link Image
Enzyme 6 GenAtlas ID NME6 Link Image
Enzyme 6 HGNC ID HGNC:20567 Link Image
Enzyme 6 Chromosome Location 3
Enzyme 6 Locus 3p21
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5442
Enzyme 7 Name Glucokinase
Enzyme 7 Synonyms
  1. Hexokinase-4
  2. Hexokinase type IV
  3. HK IV
  4. HK4
  5. Hexokinase-D
Enzyme 7 Gene Name GCK
Enzyme 7 Protein Sequence >Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Enzyme 7 Number of Residues 465
Enzyme 7 Molecular Weight 52192
Enzyme 7 Theoretical pI 4.85
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • 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 7 General Function Not Available
Enzyme 7 Specific Function Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + D-glucose = ADP + D-glucose 6-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 179427 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P35557 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name HXK4_HUMAN Link Image
Enzyme 7 PDB ID 1V4T Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
Enzyme 7 GenBank Gene ID M88011 Link Image
Enzyme 7 GeneCard ID GCK Link Image
Enzyme 7 GenAtlas ID GCK Link Image
Enzyme 7 HGNC ID HGNC:4195 Link Image
Enzyme 7 Chromosome Location 7
Enzyme 7 Locus 7p15.3-p15.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed Link Image]
  2. Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed Link Image]
  3. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed Link Image]
  4. Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed Link Image]
  5. Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed Link Image]
  6. Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed Link Image]
  7. St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed Link Image]
  8. Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed Link Image]
  9. Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed Link Image]
  10. Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed Link Image]
  11. Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed Link Image]
  12. Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed Link Image]
  13. Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed Link Image]
  14. Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed Link Image]
  15. Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed Link Image]
  16. Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed Link Image]
  17. Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed Link Image]
  18. Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed Link Image]
  19. Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5444
Enzyme 8 Name Hexokinase-3
Enzyme 8 Synonyms
  1. Hexokinase type III
  2. HK III
Enzyme 8 Gene Name HK3
Enzyme 8 Protein Sequence >Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
Enzyme 8 Number of Residues 923
Enzyme 8 Molecular Weight 98921
Enzyme 8 Theoretical pI 5.11
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • 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 8 General Function Not Available
Enzyme 8 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1255788 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P52790 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name HXK3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
Enzyme 8 GenBank Gene ID U51333 Link Image
Enzyme 8 GeneCard ID HK3 Link Image
Enzyme 8 GenAtlas ID HK3 Link Image
Enzyme 8 HGNC ID HGNC:4925 Link Image
Enzyme 8 Chromosome Location 5
Enzyme 8 Locus 5q35.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed Link Image]
  2. Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5445
Enzyme 9 Name Hexokinase-2
Enzyme 9 Synonyms
  1. Hexokinase type II
  2. HK II
  3. Muscle form hexokinase
Enzyme 9 Gene Name HK2
Enzyme 9 Protein Sequence >Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
Enzyme 9 Number of Residues 917
Enzyme 9 Molecular Weight 102381
Enzyme 9 Theoretical pI 5.93
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • 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 9 General Function Not Available
Enzyme 9 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 587202 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P52789 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name HXK2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
Enzyme 9 GenBank Gene ID Z46376 Link Image
Enzyme 9 GeneCard ID HK2 Link Image
Enzyme 9 GenAtlas ID HK2 Link Image
Enzyme 9 HGNC ID HGNC:4923 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 2p13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed Link Image]
  2. Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed Link Image]
  3. Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed Link Image]
  4. Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed Link Image]
  5. Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed Link Image]
  6. Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5834
Enzyme 10 Name Adenylate kinase isoenzyme 1
Enzyme 10 Synonyms
  1. ATP-AMP transphosphorylase
  2. AK1
  3. Myokinase
Enzyme 10 Gene Name AK1
Enzyme 10 Protein Sequence >Adenylate kinase isoenzyme 1
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEI
MEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDA
GPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVD
SVFSQVCTHLDALK
Enzyme 10 Number of Residues 194
Enzyme 10 Molecular Weight 21635
Enzyme 10 Theoretical pI 8.99
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • ATP metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate metabolism
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function This small ubiquitous enzyme is essential for maintenance and cell growth
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + AMP = 2 ADP
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 178322 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P00568 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name KAD1_HUMAN Link Image
Enzyme 10 PDB ID 1Z83 Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >585 bp
ATGGAAGAGAAGCTGAAGAAAACCAAGATCATCTTTGTGGTGGGTGGGCCTGGCTCAGGG
AAGGGCACCCAGTGTGAGAAGATCGTGCAGAAGTATGGCTACACCCACCTCTCCACCGGG
GACCTCCTGCGGTCCGAGGTCAGCTCAGGCTCGGCCAGGGGCAAGAAGCTGTCGGAAATC
ATGGAGAAGGGGCAGCTGGTTCCACTGGAGACAGTGTTGGACATGCTCCGGGATGCCATG
GTGGCCAAAGTCAATACTTCCAAAGGCTTCCTGATTGATGGCTACCCGCGGGAGGTGCAG
CAAGGAGAAGAGTTTGAGCGACGGATTGGACAGCCCACACTGCTGCTGTATGTGGACGCA
GGCCCTGAGACCATGACCCAGCGGCTCTTGAAACGTGGAGAGACCAGCGGGCGTGTGGAC
GACAATGAGGAGACCATCAAAAAGCGGCTGGAGACCTATTACAAGGCCACAGAACCCGTC
ATCGCCTTCTATGAGAAACGTGGCATTGTGCGCAAGGTCAACGCTGAGGGCTCCGTGGAC
AGTGTCTTCTCCCAGGTCTGCACCCACCTGGACGCCCTAAAGTAG
Enzyme 10 GenBank Gene ID J04809 Link Image
Enzyme 10 GeneCard ID AK1 Link Image
Enzyme 10 GenAtlas ID AK1 Link Image
Enzyme 10 HGNC ID HGNC:361 Link Image
Enzyme 10 Chromosome Location 9
Enzyme 10 Locus 9q34.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed Link Image]
  2. Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5875
Enzyme 11 Name Putative adenylate kinase 7
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name AK7
Enzyme 11 Protein Sequence >Putative adenylate kinase 7
MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENK
SAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNIT
ESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRR
RKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPAL
PVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGK
IQKIPRENAYLTKDLTQDCLDHLLVNLRMEALFVKENFNIRWAAQTGFVENINTILKEYK
QSRGLMPIKICILGPPAVGKSSIAKELAKYYKLHHIQLKDVISEAIAKLEAIVAPNDVGE
GEEEVEEEEEEENVEDAQELLDGIKESMEQNAGQLDDQYIIRFMKEKLKSMPCRNQGYIL
DGFPKTYDQAKDLFNQEDEEEEDDVRGRMFPFDKLIIPEFVCALDASDEFLKERVINLPE
SIVAGTHYSQDRFLRALSNYRDINIDDETVFNYFDELEIHPIHIDVGKLEDAQNRLAIKQ
LIKEIGEPRNYGLTDEEKAEEERKAAEERLAREAAEEAEREHQEAVEMAEKIARWEEWNK
RLEEVKREERELLEAQSIPLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP
EAQ
Enzyme 11 Number of Residues 723
Enzyme 11 Molecular Weight 82673
Enzyme 11 Theoretical pI 4.40
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function ATP + AMP = 2 ADP
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + AMP = 2 ADP
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 16553126 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96M32 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name KAD7_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2172 bp
ATGGCTGAAGAAGAGGAAACTGCTGCTCTCACGGAGAAGGTTATCCGGACCCAGAGGGTG
TTTATAAACCTGTTGGATTCCTACAGCAGCGGAAACATCGGGAAGTTTCTATCTAACTGT
GTAGTTGGGGCTTCGCTTGAAGAAATTACAGAGGAAGAGGAAGAGGAAGATGAAAATAAG
TCAGCTATGCTGGAAGCTTCCTCAACCAAAGTGAAGGAAGGCACATTCCAGATTGTGGGC
ACGCTGTCCAAGCCTGACAGCCCGCGGCCTGACTTTGCGGTGGAGACGTACTCTGCCATC
TCTCAAGAAGACCTTCTCATGCGCCTGCTGGAGTGTGATGTTATTATTTATAACATCACT
GAGAGCTCACAGCAAATGGAGGAAGCCATCTGGGCAGTCTCTGCACTCAGTGAAGAAGTC
AGCCACTTTGAAAAGCGAAAGCTATTTATTTTACTGTCGACGGTGATGACTTGGGCGCGC
TCCAAAGCCCTGGACCCCGAGGATTCTGAGGTTCCATTCACTGAAGAAGATTATCGAAGA
AGAAAGTCTCATCCTAATTTTCTGGACCACATAAATGCTGAAAAAATGGTTCTCAAATTT
GGAAAAAAGGCCAGAAAATTTGCAGCATACGTAGTTGCTGCTGGACTCCAGTATGGAGCG
GAAGGAGGCATGTTACACACATTTTTTAAGATGGCTTGGTTGGGCGAGATTCCTGCATTA
CCAGTTTTTGGCGATGGAACAAATGTAATTCCAACAATCCATGTTCTTGATCTAGCAGGA
GTGATACAAAACGTCATAGATCACGTGCCAAAGCTTCACTACCTGGTTGCTGTGGATGAG
TCTGTTCATACCCTGGAAGACATAGTCAAGTGTATCAGTAAAAATACTGGCCCTGGGAAA
ATCCAGAAAATACCCAGAGAAAATGCATACCTAACCAAGGACTTAACGCAAGATTGTCTT
GACCATTTACTGGTCAACTTAAGAATGGAAGCGCTCTTTGTGAAGGAGAATTTTAATATT
CGATGGGCTGCCCAAACAGGATTTGTGGAAAATATCAACACTATCCTCAAGGAGTACAAG
CAAAGCAGAGGATTGATGCCAATCAAGATCTGCATTCTTGGTCCCCCTGCTGTGGGAAAA
TCCAGTATTGCTAAAGAATTGGCCAAGTACTACAAACTGCATCACATCCAACTGAAGGAT
GTCATTTCTGAAGCCATAGCAAAACTGGGGGCGATTGTTGCCCCTAACGATGTAGGGGAA
GGAGAAGAAGAAGTCGAAGAGGAAGAGGAGGAGGAGAATGTGGAAGATGCACAGGAGCTC
CTAGATGGCATCAAGGAGAGCATGGAGCAGAATGCAGGTCAACTAGACGATCAATATATA
ATTAGATTTATGAAAGAAAAGCTAAAATCAATGCCTTGCAGGAATCAAGGTTATATTTTG
GATGGATTCCCAAAGACCTATGATCAAGCAAAAGACCTGTTCAATCAGGAAGATGAGGAG
GAGGAAGATGATGTCAGAGGCAGAATGTTTCCCTTTGATAAATTAATTATACCTGAATTC
GTTTGTGCACTGGATGCTTCGGATGAGTTTCTGAAGGAGCGTGTGATAAACCTTCCTGAG
AGCATCGTGGCGGGGACCCACTACAGCCAAGACCGATTCCTCCGGGCTCTGAGCAACTAC
CGGGACATCAATATCGACGATGAGACTGTCTTCAACTATTTTGATGAACTTGAAATTCAC
CCGATACATATTGATGTAGGAAAACTTGAAGATGCTCAGAATAGACTTGCTATCAAACAG
CTCATCAAAGAGATTGGGGAGCCTCGAAATTATGGTTTAACAGACGAAGAAAAGGCAGAA
GAGGAGCGGAAGGCTGCGGAGGAGCGGCTGGCCAGGGAGGCTGCTGAGGAAGCAGAACGC
GAGCACCAGGAGGCCGTGGAGATGGCAGAGAAGATAGCTCGCTGGGAGGAGTGGAATAAA
CGACTGGAGGAAGTGAAAAGAGAAGAAAGAGAATTACTGGAGGCTCAGTCAATTCCCCTG
AGAAACTATTTAATGACCTATGTGATGCCAACTCTTATTCAGGGCCTGAATGAATGTTGC
AACGTCCGACCCGAAGACCCTGTTGATTTTCTGGCAGAATATCTCTTCAAGAACAATCCT
GAAGCACAGTGA
Enzyme 11 GenBank Gene ID AK057426 Link Image
Enzyme 11 GeneCard ID AK7 Link Image
Enzyme 11 GenAtlas ID AK7 Link Image
Enzyme 11 HGNC ID HGNC:20091 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5924
Enzyme 12 Name Adenylate kinase isoenzyme 5
Enzyme 12 Synonyms
  1. ATP-AMP transphosphorylase
Enzyme 12 Gene Name AK5
Enzyme 12 Protein Sequence >Adenylate kinase isoenzyme 5
MGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLI
RDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDPQLVIC
MDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEG
TPEDVFLQLCTAIDSIIF
Enzyme 12 Number of Residues 198
Enzyme 12 Molecular Weight 22088
Enzyme 12 Theoretical pI 5.16
Enzyme 12 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • ATP metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate metabolism
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 12 General Function Nucleotide transport and metabolism
Enzyme 12 Specific Function Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP
Enzyme 12 Pathways
Enzyme 12 Reactions
  • ATP + AMP = 2 ADP
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 4691541 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y6K8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name KAD5_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >597 bp
ATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTCATAATTGGTGGTCCT
GGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATATGGATTTACACATCTC
TCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAAAGAAGCAAATTGATC
AGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTTTTGGAGCTCCTGAAG
GAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATTGACGGCTATCCTCGG
GAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCACAGTTGGTGATCTGT
ATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGGAGCCGGAGCAGCCTG
CCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCCTACTACCGAGCGTCC
ATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAGATAAATGCAGAGGGA
ACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCTATTATTTTCTGA
Enzyme 12 GenBank Gene ID AF062595 Link Image
Enzyme 12 GeneCard ID AK5 Link Image
Enzyme 12 GenAtlas ID AK5 Link Image
Enzyme 12 HGNC ID HGNC:365 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p31
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6041
Enzyme 13 Name Pyruvate kinase isozymes R/L
Enzyme 13 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 13 Gene Name PKLR
Enzyme 13 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 13 Number of Residues 574
Enzyme 13 Molecular Weight 61831
Enzyme 13 Theoretical pI 7.83
Enzyme 13 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 13 General Function Carbohydrate transport and metabolism
Enzyme 13 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 13 Pathways
Enzyme 13 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3327365 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 13 PDB ID 1LIU Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID AB015983 Link Image
Enzyme 13 GeneCard ID PKLR Link Image
Enzyme 13 GenAtlas ID PKLR Link Image
Enzyme 13 HGNC ID HGNC:9020 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1q21
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  6. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
  13. 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 Link Image]
  14. 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 Link Image]
  15. 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 Link Image]
  16. 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 Link Image]
  17. 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 Link Image]
  18. 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 Link Image]
  19. 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 Link Image]
  20. 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 Link Image]
  21. 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 Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8075
Enzyme 14 Name Uridine-cytidine kinase 2
Enzyme 14 Synonyms
  1. UCK 2
  2. Uridine monophosphokinase 2
  3. Cytidine monophosphokinase 2
Enzyme 14 Gene Name UCK2
Enzyme 14 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 14 Number of Residues 261
Enzyme 14 Molecular Weight 29299
Enzyme 14 Theoretical pI 6.68
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Nucleotide transport and metabolism
Enzyme 14 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 1655420 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 14 PDB ID 1XRJ Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
Enzyme 14 GenBank Gene ID D78335 Link Image
Enzyme 14 GeneCard ID UCK2 Link Image
Enzyme 14 GenAtlas ID UCK2 Link Image
Enzyme 14 HGNC ID HGNC:12562 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q23
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed Link Image]
  2. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  3. Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 13094
Enzyme 15 Name Ribonucleoside-diphosphate reductase subunit M2 B
Enzyme 15 Synonyms
  1. TP53- inducible ribonucleotide reductase M2 B
  2. p53-inducible ribonucleotide reductase small subunit 2-like protein
  3. p53R2
Enzyme 15 Gene Name RRM2B
Enzyme 15 Protein Sequence >Ribonucleoside-diphosphate reductase subunit M2 B
MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQ
ASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA
RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRK
STFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQ
YLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFS
KVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Enzyme 15 Number of Residues 351
Enzyme 15 Molecular Weight 40737
Enzyme 15 Theoretical pI 4.61
Enzyme 15 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 15 General Function Nucleotide transport and metabolism
Enzyme 15 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 15 Pathways
Enzyme 15 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294] ALL_REAC R04294 > R02017 R02018 R02019 R02024
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 7229086 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q7LG56 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name RIR2B_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AB036063 Link Image
Enzyme 15 GeneCard ID Q7LG56 Link Image
Enzyme 15 GenAtlas ID RRM2B Link Image
Enzyme 15 HGNC ID HGNC:17296 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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 Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 13098
Enzyme 16 Name Uridine/cytidine kinase-like 1
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name UCKL1
Enzyme 16 Protein Sequence >Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 16 Number of Residues 548
Enzyme 16 Molecular Weight 61142
Enzyme 16 Theoretical pI 7.40
Enzyme 16 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Nucleotide transport and metabolism
Enzyme 16 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 16 Pathways
Enzyme 16 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964] ALL_REAC R00964
  • (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548 R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 38228699 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AJ605558 Link Image
Enzyme 16 GeneCard ID Q9NWZ5 Link Image
Enzyme 16 GenAtlas ID UCKL1 Link Image
Enzyme 16 HGNC ID HGNC:15938 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [PubMed Link Image]
  2. 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 Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15070
Enzyme 17 Name cDNA FLJ78347, highly similar to Homo sapiens adenylate kinase 2 (AK2), transcript variant AK2A, mRNA (Adenylate kinase 2, isoform CRA_d)
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name AK2
Enzyme 17 Protein Sequence >cDNA FLJ78347, highly similar to Homo sapiens adenylate kinase 2 (AK2), transcript variant AK2A, mRNA (Adenylate kinase 2, isoform CRA_d)
MAPSVPAAEPEYPKGIRAVLLGPPGAGKGTQAPRLAENFCVCHLATGDMLRAMVASGSEL
GKKLKATMDAGKLVSDEMVVELIEKNLETPLCKNGFLLDGFPRTVRQAEMLDDLMEKRKE
KLDSVIEFSIPDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNE
KALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI
Enzyme 17 Number of Residues 239
Enzyme 17 Molecular Weight 26478
Enzyme 17 Theoretical pI 7.97
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Nucleotide transport and metabolism
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function Not Available
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 158256784 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID A8K6L1 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name A8K6L1_HUMAN Link Image
Enzyme 17 PDB ID 2AK2 Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >720 bp
ATGGCTCCCAGCGTGCCAGCGGCAGAACCCGAGTATCCTAAAGGCATCCGGGCCGTGCTG
CTGGGGCCTCCCGGGGCCGGTAAAGGGACCCAGGCACCCAGATTGGCTGAAAACTTCTGT
GTCTGCCATTTAGCTACTGGGGACATGCTGAGGGCCATGGTGGCTTCTGGCTCAGAGCTA
GGAAAAAAGCTGAAGGCAACTATGGATGCTGGGAAACTGGTGAGTGATGAAATGGTAGTG
GAGCTCATTGAGAAGAATTTGGAGACCCCCTTGTGCAAAAATGGTTTTCTTCTGGATGGC
TTCCCTCGGACTGTGAGGCAGGCAGAAATGCTCGATGACCTCATGGAGAAGAGGAAAGAG
AAGCTTGATTCTGTGATTGAATTCAGCATCCCAGACTCTCTGCTGATCCGAAGAATCACA
GGAAGGCTGATTCACCCCAAGAGTGGCCGTTCCTACCACGAGGAGTTCAACCCTCCAAAA
GAGCCCATGAAAGATGACATCACCGGGGAACCCTTGATCCGTCGATCAGATGATAATGAA
AAGGCCTTGAAAATCCGCCTGCAAGCCTACCACACTCAAACCACCCCACTCATAGAGTAC
TACAGGAAACGGGGGATCCACTCCGCCATCGATGCATCCCAGACCCCCGATGTCGTGTTC
GCAAGCATCCTAGCAGCCTTCTCCAAAGCCACATGTAAAGACTTGGTTATGTTTATCTAA
Enzyme 17 GenBank Gene ID AK291676 Link Image
Enzyme 17 GeneCard ID A8K6L1 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15191
Enzyme 18 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 18 Synonyms Not Available
Enzyme 18 Gene Name NME7
Enzyme 18 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 18 Number of Residues 376
Enzyme 18 Molecular Weight 42492
Enzyme 18 Theoretical pI 6.44
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158254838 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 18 GenBank Gene ID AK290701 Link Image
Enzyme 18 GeneCard ID A8K3T6 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 15200
Enzyme 19 Name Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name UCK1
Enzyme 19 Protein Sequence >Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 19 Number of Residues 201
Enzyme 19 Molecular Weight 22761
Enzyme 19 Theoretical pI 6.23
Enzyme 19 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 19 General Function Nucleotide transport and metabolism
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 57162360 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 19 GenBank Gene ID AL358781 Link Image
Enzyme 19 GeneCard ID Q5JT13 Link Image
Enzyme 19 GenAtlas ID UCK1 Link Image
Enzyme 19 HGNC ID HGNC:14859 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 15209
Enzyme 20 Name cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name Not Available
Enzyme 20 Protein Sequence >cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
Enzyme 20 Number of Residues 917
Enzyme 20 Molecular Weight 102388
Enzyme 20 Theoretical pI 6.70
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function Not Available
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 158257456 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID A8K7J7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name A8K7J7_HUMAN Link Image
Enzyme 20 PDB ID 1HKB Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
Enzyme 20 GenBank Gene ID AK292012 Link Image
Enzyme 20 GeneCard ID A8K7J7 Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs Not Available
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 16434
Enzyme 21 Name cDNA, FLJ94180, Homo sapiens adenylate kinase 3 (AK3), mRNA (AK3L2 protein)
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name AK3L2
Enzyme 21 Protein Sequence >cDNA, FLJ94180, Homo sapiens adenylate kinase 3 (AK3), mRNA (AK3L2 protein)
MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEK
SLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLK
DRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKP
VIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY
Enzyme 21 Number of Residues 223
Enzyme 21 Molecular Weight 25268
Enzyme 21 Theoretical pI 8.66
Enzyme 21 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 21 General Function Nucleotide transport and metabolism
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID B2R927 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name B2R927_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID BC148270 Link Image
Enzyme 21 GeneCard ID B2R927 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 12
Enzyme 21 Locus 12p11.21
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16476
Enzyme 22 Name cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name PKM2
Enzyme 22 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 22 Number of Residues 531
Enzyme 22 Molecular Weight 57938
Enzyme 22 Theoretical pI 7.94
Enzyme 22 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 22 General Function Carbohydrate transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID B2R5N8 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name B2R5N8_HUMAN Link Image
Enzyme 22 PDB ID 1F3X Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AK312253 Link Image
Enzyme 22 GeneCard ID B2R5N8 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 15
Enzyme 22 Locus 15q22
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available