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Human Metabolome Database Version 2.5

 

Showing metabocard for Nicotinic acid adenine dinucleotide (HMDB01179)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:37
Accession Number HMDB01179
Secondary Accession Numbers Not Available
Common Name Nicotinic acid adenine dinucleotide
Description Nicotinamide adenine dinucleotide (NAD) is an important coenzyme found in cells.
Synonyms
  1. NAAD
  2. NAADP
  3. NaADN
  4. Nicotinic acid adenine dinucleotide phosphate
  5. deamido-NAD+
  6. deamidonicotinamide adenine dinucleoetide
  7. deamino-nad+
  8. nicotinate adenine dinucleotide
  9. nicotinic acid adenine dinucleotide
Chemical IUPAC Name 1-[5-[[[[5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxymethyl]-3,4-dihydroxy-oxolan-2-yl]pyridine-5-carboxylate
Chemical Formula C21H27N6O15P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Second messenger
Application
—
Source
  • Endogenous
Average Molecular Weight 665.418
Monoisotopic Molecular Weight 665.100952
Isomeric SMILES NC1=C2N=CN([C@@H]3O[C@H](COP(O)(=O)OP(O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)[N+]4=CC=CC(=C4)C(O)=O)[C@@H](O)[C@H]3O)C2=NC=N1
Canonical SMILES NC1=C2N=CN(C3OC(COP(O)(=O)OP(O)(=O)OCC4OC(C(O)C4O)[N+]4=CC=CC(=C4)C(O)=O)C(O)C3O)C2=NC=N1
KEGG Compound ID C00857 Link Image
BioCyc ID DEAMIDO-NAD Link Image
BiGG ID 36219 Link Image
Wikipedia Link NAADP Link Image
NuGOwiki Link HMDB01179 Link Image
Metagene Link HMDB01179 Link Image
METLIN ID 4234 Link Image
PubChem Compound 165490 Link Image
PubChem Substance 841415 Link Image
ChEBI ID Not Available
CAS Registry Number 6450-77-7
InChI Identifier InChI=1/C21H26N6O15P2/c22-17-12-18(24-7-23-17)27(8-25-12)20-16(31)14(29)11(41-20)6-39-44(36,37)42-43(34,35)38-5-10-13(28)15(30)19(40-10)26-3-1-2-9(4-26)21(32)33/h1-4,7-8,10-11,13-16,19-20,28-31H,5-6H2,(H4-,22,23,24,32,33,34,35,36,37)/p+1/t10-,11-,13-,14-,15-,16-,19-,20-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.88 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.89 [Predicted by ALOGPS] 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
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Nicotinate and Nicotinamide Metabolism SMP00048 Link Image map00760 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  3. Nicotinamide mononucleotide adenylyltransferase 3
  4. Nicotinamide mononucleotide adenylyltransferase 2
  5. Glutamine-dependent NAD(+) synthetase
  6. Peroxisomal NADH pyrophosphatase NUDT12
  7. cDNA FLJ40747 fis, clone TRACH2000502, highly similar to Peroxisomal NADH pyrophosphatase NUDT12 (EC 3.6.1.22)
  8. Nicotinamide nucleotide adenylyltransferase 1 (Nicotinamide nucleotide adenylyltransferase 1, isoform CRA_a) (cDNA, FLJ96727, Homo sapiens nicotinamide nucleotide adenylyltransferase 1(NMNAT1), mRNA)
Enzyme 1 [top]
Enzyme 1 ID 5351
Enzyme 1 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 1 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 1 Gene Name ENPP1
Enzyme 1 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 1 Number of Residues 925
Enzyme 1 Molecular Weight 104925
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 77-97
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189650 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2622 bp 
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 1 GenBank Gene ID M57736 Link Image
Enzyme 1 GeneCard ID ENPP1 Link Image
Enzyme 1 GenAtlas ID ENPP1 Link Image
Enzyme 1 HGNC ID HGNC:3356 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6q22-q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5426
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Enzyme 2 Synonyms
  1. E- NPP 3
  2. Phosphodiesterase I/nucleotide pyrophosphatase 3
  3. Phosphodiesterase I beta
  4. PD-Ibeta
  5. CD203c antigen[Includes: Alkaline phosphodiesterase I
  6. NPPase]
Enzyme 2 Gene Name ENPP3
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 2 Number of Residues 875
Enzyme 2 Molecular Weight 100097
Enzyme 2 Theoretical pI 6.55
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-38
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2465540 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14638 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2628 bp 
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
Enzyme 2 GenBank Gene ID AF005632 Link Image
Enzyme 2 GeneCard ID ENPP3 Link Image
Enzyme 2 GenAtlas ID ENPP3 Link Image
Enzyme 2 HGNC ID HGNC:3358 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5572
Enzyme 3 Name Nicotinamide mononucleotide adenylyltransferase 3
Enzyme 3 Synonyms
  1. NMN adenylyltransferase 3
Enzyme 3 Gene Name NMNAT3
Enzyme 3 Protein Sequence >Nicotinamide mononucleotide adenylyltransferase 3 
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAA
SHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKAL
FSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESP
ILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWK
GKSTQSTEGKTS
Enzyme 3 Number of Residues 252
Enzyme 3 Molecular Weight 28322
Enzyme 3 Theoretical pI 9.69
Enzyme 3 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • NAD biosynthesis
  • biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
—
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function ATP + nicotinamide ribonucleotide = diphosphate + NAD(+)
Enzyme 3 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 3 Reactions
  • ATP + nicotinamide ribonucleotide = diphosphate + NAD+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 14029540 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96T66 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NMNA3_HUMAN Link Image
Enzyme 3 PDB ID 1NUU Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >759 bp 
ATGAAGAGCCGAATACCTGTGGTGCTCCTGGCCTGTGGCTCCTTTAACCCCATCACCAAC
ATGCACCTGCGCATGTTTGAGGTGGCCAGAGATCACCTACACCAAACAGGAATGTACCAG
GTCATCCAGGGTATCATCTCTCCTGTCAACGACACCTATGGGAAGAAAGACCTCGCAGCT
TCTCATCACCGAGTGGCCATGGCCCGGCTGGCCCTGCAGACATCCGACTGGATCCGGGTG
GACCCTTGGGAGAGTGAGCAGGCACAGTGGATGGAGACAGTGAAGGTGCTGAGGCATCAT
CACAGCAAACTGCTCAGATCTCCACCCCAGATGGAAGGCCCAGACCATGGCAAGGCACTC
TTCTCGACCCCTGCAGCTGTGCCTGAGCTGAAGCTTCTCTGTGGGGCAGACGTCTTGAAG
ACCTTCCAGACCCCCAACCTCTGGAAGGATGCGCACATCCAGGAAATAGTGGAGAAGTTT
GGCTTGGTGTGCGTGGGCCGAGTAAGTCACGACCCAAAAGGTTACATCGCAGAATCTCCC
ATCCTACGGATGCACCAGCACAACATTCACCTGGCCAAGGAGCCTGTGCAGAATGAGATC
AGTGCCACATACATCAGGCGAGCCTTGGGCCAAGGGCAGAGCGTAAAGTACCTGATTCCC
GATGCTGTCATCACGTACATCAAGGACCATGGCCTCTACACCAAGGGCAGTACCTGGAAA
GGCAAAAGCACCCAGAGCACTGAGGGCAAGACAAGCTAG
Enzyme 3 GenBank Gene ID AF345564 Link Image
Enzyme 3 GeneCard ID NMNAT3 Link Image
Enzyme 3 GenAtlas ID NMNAT3 Link Image
Enzyme 3 HGNC ID HGNC:20989 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5574
Enzyme 4 Name Nicotinamide mononucleotide adenylyltransferase 2
Enzyme 4 Synonyms
  1. NMN adenylyltransferase 2
Enzyme 4 Gene Name NMNAT2
Enzyme 4 Protein Sequence >Nicotinamide mononucleotide adenylyltransferase 2 
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG
Enzyme 4 Number of Residues 307
Enzyme 4 Molecular Weight 34439
Enzyme 4 Theoretical pI 7.07
Enzyme 4 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • NAD biosynthesis
  • biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function ATP + nicotinamide ribonucleotide = diphosphate + NAD(+)
Enzyme 4 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 4 Reactions
  • ATP + nicotinamide ribonucleotide = diphosphate + NAD+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 12620200 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9BZQ4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NMNA2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >924 bp 
ATGACCGAGACCACCAAGACCCACGTTATCTTGCTCGCCTGCGGCAGCTTCAATCCCATC
ACCAAAGGGCACATTCAGATGTTTGAAAGAGCCAGGGATTATCTGCACAAAACTGGAAGG
TTTATTGTGATTGGCGGGATTGTCTCCCCTGTCCACGACTCCTATGGAAAACAGGGCCTC
GTGTCAAGCCGGCACCGTCTCATCATGTGTCAGCTGGCCGTCCAGAATTCTGATTGGATC
AGGGTGGACCCTTGGGAGTGCTACCAGGACACCTGGCAGACGACCTGCAGCGTGTTGGAA
CACCACCGGGACCTCATGAAGAGGGTGACTGGCTGCATCCTCTCCAATGTCAACACACCT
TCCATGACACCTGTGATCGGACAGCCACAAAACGAGACCCCCCAGCCCATTTACCAGAAC
AGCAACGTGGCCACCAAGCCCACTGCAGCCAAGATCTTGGGGAAGGTGGGAGAAAGCCTC
AGCCGGATCTGCTGTGTCCGCCCGCCGGTGGAGCGTTTCACCTTTGTAGATGAGAATGCC
AATCTGGGCACGGTGATGCGGTATGAAGAGATTGAGCTACGGATCCTGCTGCTGTGTGGT
AGTGACCTGCTGGAGTCCTTCTGCATCCCAGGGCTCTGGAACGAGGCAGATATGGAGGTG
ATTGTTGGTGACTTTGGGATTGTGGTGGTGCCCCGGGATGCAGCCGACACAGACCGAATC
ATGAATCACTCCTCAATACTCCGCAAATACAAAAACAACATCATGGTGGTGAAGGATGAC
ATCAACCATCCCATGTCTGTTGTCAGCTCAACCAAGAGCAGGCTGGCCCTGCAGCATGGG
GACGGCCATGTTGTGGATTACCTGTCCCAGCCGGTCATCGACTACATCCTCAAAAGCCAG
CTGTACATCAATGCCTCCGGCTAG
Enzyme 4 GenBank Gene ID AF288395 Link Image
Enzyme 4 GeneCard ID NMNAT2 Link Image
Enzyme 4 GenAtlas ID NMNAT2 Link Image
Enzyme 4 HGNC ID HGNC:16789 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Sood R, Bonner TI, Makalowska I, Stephan DA, Robbins CM, Connors TD, Morgenbesser SD, Su K, Faruque MU, Pinkett H, Graham C, Baxevanis AD, Klinger KW, Landes GM, Trent JM, Carpten JD: Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus. Genomics. 2001 Apr 15;73(2):211-22. [PubMed Link Image]
  2. Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O: Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. DNA Res. 1997 Oct 31;4(5):345-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8813
Enzyme 5 Name Glutamine-dependent NAD(+) synthetase
Enzyme 5 Synonyms
  1. NAD(+synthase [glutamine-hydrolyzing]
  2. NAD(+synthetase 1
Enzyme 5 Gene Name NADSYN1
Enzyme 5 Protein Sequence >Glutamine-dependent NAD(+) synthetase 
MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYES
DTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANE
GNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWT
PHSPHIDMGLDGVEIITNASGSHHVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRL
YYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR
VKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGV
DSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMAS
KNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLA
LQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIG
GISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSV
YGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAE
NYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD
Enzyme 5 Number of Residues 706
Enzyme 5 Molecular Weight 79295
Enzyme 5 Theoretical pI 6.46
Enzyme 5 GO Classification
Function
  • ATP binding
  • NAD+ synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • NAD biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
—
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals Not Available
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q6IA69 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NADE1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AB091316 Link Image
Enzyme 5 GeneCard ID NADSYN1 Link Image
Enzyme 5 GenAtlas ID NADSYN1 Link Image
Enzyme 5 HGNC ID HGNC:29832 Link Image
Enzyme 5 Chromosome Location 11
Enzyme 5 Locus 11q13.4
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M: Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem. 2003 Mar 28;278(13):10914-21. Epub 2003 Jan 23. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13073
Enzyme 6 Name Peroxisomal NADH pyrophosphatase NUDT12
Enzyme 6 Synonyms
  1. Nucleoside diphosphate-linked moiety X motif 12
  2. Nudix motif 12
Enzyme 6 Gene Name NUDT12
Enzyme 6 Protein Sequence >Peroxisomal NADH pyrophosphatase NUDT12 
MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPE
IVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENY
FSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLN
YTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEF
KQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKR
LCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPG
ETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDAR
WFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
Enzyme 6 Number of Residues 462
Enzyme 6 Molecular Weight 52076
Enzyme 6 Theoretical pI 6.82
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Replication, recombination and repair
Enzyme 6 Specific Function Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle
Enzyme 6 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 6 Reactions
  • NAD+ + H2O = AMP + NMN [RN:R00103] ALL_REAC R00103
  • (other) R03004
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 13276687 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BQG2 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NUD12_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AL136592 Link Image
Enzyme 6 GeneCard ID Q9BQG2 Link Image
Enzyme 6 GenAtlas ID NUDT12 Link Image
Enzyme 6 HGNC ID HGNC:18826 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16438
Enzyme 7 Name cDNA FLJ40747 fis, clone TRACH2000502, highly similar to Peroxisomal NADH pyrophosphatase NUDT12 (EC 3.6.1.22)
Enzyme 7 Synonyms
  1. SubName: Nudix (Nucleoside diphosphate linked moiety X)-type motif 12
Enzyme 7 Gene Name NUDT12
Enzyme 7 Protein Sequence >cDNA FLJ40747 fis, clone TRACH2000502, highly similar to Peroxisomal NADH pyrophosphatase NUDT12 (EC 3.6.1.22) 
MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPE
IVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENY
FSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLN
YTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEF
KQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKR
LCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPG
ETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDAR
WFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
Enzyme 7 Number of Residues 462
Enzyme 7 Molecular Weight 52076
Enzyme 7 Theoretical pI 6.82
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Replication, recombination and repair
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • NAD+ + H2O = AMP + NMN [RN:R00103] ALL_REAC R00103
  • (other) R03004
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B3KUW2 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B3KUW2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK098066 Link Image
Enzyme 7 GeneCard ID B3KUW2 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16529
Enzyme 8 Name Nicotinamide nucleotide adenylyltransferase 1 (Nicotinamide nucleotide adenylyltransferase 1, isoform CRA_a) (cDNA, FLJ96727, Homo sapiens nicotinamide nucleotide adenylyltransferase 1(NMNAT1), mRNA)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name NMNAT1
Enzyme 8 Protein Sequence >Nicotinamide nucleotide adenylyltransferase 1 (Nicotinamide nucleotide adenylyltransferase 1, isoform CRA_a) (cDNA, FLJ96727, Homo sapiens nicotinamide nucleotide adenylyltransferase 1(NMNAT1), mRNA) 
MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGL
IPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTL
ERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVAN
YGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLV
PDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT
Enzyme 8 Number of Residues 279
Enzyme 8 Molecular Weight 31933
Enzyme 8 Theoretical pI 9.24
Enzyme 8 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • NAD biosynthesis
  • biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
—
Enzyme 8 General Function Coenzyme transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B1AN63 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B1AN63_HUMAN Link Image
Enzyme 8 PDB ID 1KQO Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK315640 Link Image
Enzyme 8 GeneCard ID B1AN63 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available