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Human Metabolome Database Version 2.5

 

Showing metabocard for Reduced Vitamin K (phylloquinone) (HMDB04198)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 15:02:40
Update Date 2010-07-22 17:55:35
Accession Number HMDB04198
Secondary Accession Numbers Not Available
Common Name Reduced Vitamin K (phylloquinone)
Description Vitamin K is a family of fat-soluble compounds with a common chemical structure, 2, methyl-1,4-napthoquinone. Phylloquinone is present in food of plant origin, such as green, leafy vegetables and certain plant oils, and is the predominant form in the diet. Bacterial and other forms of vitamin K, referred to as the menaquinones, differ in structure from phylloquinone in their 3-substituted lipophilic side chain. Menaquinone-4 (MK-4), which is alkylated from menadione, is present in animal feeds or is the product of tissue-specific conversion directly from dietary phylloquinone. Vitamin K is a cofactor specific to the formation of gamma-carboxyglutamyl (Gla) residues in certain proteins, including prothrombin necessary for normal hemostatic function. The naturally occurring forms of vitamin K are quinones (i.e. phylloquinone and menaquinones) so vitamin K is reduced to the vitamin K hydroquinone prior to catalyzing the gamma-carboxylation reaction. The active site for the carboxylation reaction is on the napthoquinone ring, which is identical for all forms of vitamin K, including phylloquinone and MK-4. (PMID 16857056)
Synonyms
  1. vitamin K hydroquinone (phylloquinone)
Chemical IUPAC Name 1a-methyl-7a-[(E)-3,7,11,15-tetramethylhexadec-2-enyl]-2,7-dihydronaphtho[2,3-b]oxirene-2,7-diol
Chemical Formula C31H50O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Naphthoquinones
Sub Class
  • Diols
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • dialkyl ether
  • alkene
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 470.727
Monoisotopic Molecular Weight 470.376007
Isomeric SMILES CC(C)CCCC(C)CCCC(C)CCCC(C)=CCC12OC1(C)C(O)C1=CC=CC=C1C2O
Canonical SMILES CC(C)CCCC(C)CCCC(C)CCCC(C)=CCC12OC1(C)C(O)C1=CC=CC=C1C2O
KEGG Compound ID C05850 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB04198 Link Image
Metagene Link HMDB04198 Link Image
METLIN ID 7027 Link Image
PubChem Compound 5280846 Link Image
PubChem Substance 700875 Link Image
ChEBI ID Not Available
CAS Registry Number 81382-12-9
InChI Identifier InChI=1/C31H50O3/c1-22(2)12-9-13-23(3)14-10-15-24(4)16-11-17-25(5)20-21-31-29(33)27-19-8-7-18-26(27)28(32)30(31,6)34-31/h7-8,18-20,22-24,28-29,32-33H,9-17,21H2,1-6H3/b25-20+
Synthesis Reference Masaki, Yukio; Hashimoto, Kinji; Kaji, Kenji. Synthetic studies on isoprenoidquinones. II. Syntheses of ubiquinone-10, phylloquinone, and menaquinone-4 by a chain-extending method utilizing terminally functionalized isoprenoidhydroquinones. Chemical & Pharmaceutical Bulletin (1984), 32(10), 3959-67.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.26e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 8.29 [Predicted by ALOGPS]; 8.4 [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
  • Membrane (Predicted from LogP)
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
Vitamin K Metabolism SMP00464 Link Image
General References Not Available
Metabolic Enzymes
  1. NAD(P)H dehydrogenase [quinone] 1
  2. Vitamin K-dependent gamma-carboxylase
  3. cDNA, FLJ92690, Homo sapiens NAD(P)H dehydrogenase, quinone 1 (NQO1), mRNA (NAD(P)H dehydrogenase, quinone 1, isoform CRA_c)
Enzyme 1 [top]
Enzyme 1 ID 7026
Enzyme 1 Name NAD(P)H dehydrogenase [quinone] 1
Enzyme 1 Synonyms
  1. Quinone reductase 1
  2. NAD(PH:quinone oxidoreductase 1
  3. QR1
  4. DT-diaphorase
  5. DTD
  6. Azoreductase
  7. Phylloquinone reductase
  8. Menadione reductase
Enzyme 1 Gene Name NQO1
Enzyme 1 Protein Sequence >NAD(P)H dehydrogenase [quinone] 1 
MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKL
KDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERV
FIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFC
GFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMK
KEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
Enzyme 1 Number of Residues 274
Enzyme 1 Molecular Weight 30868
Enzyme 1 Theoretical pI 9.34
Enzyme 1 GO Classification
Function
  • NAD(P)H dehydrogenase (quinone) activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189246 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15559 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NQO1_HUMAN Link Image
Enzyme 1 PDB ID 1KBQ Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >825 bp 
ATGGTCGGCAGAAGAGCACTGATCGTACTGGCTCACTCAGAGAGGACCTCCTTCAACTAT
GCCATGAAGGAGGCTGCTGCAGCGGCTTTGAAGAAGAAAGGATGGGAGGTGGTGGAGTCG
GACCTCTATGCCATGAACTTCAATCCCATCATTTCCAGAAAGGACATCACAGGTAAACTG
AAGGACCCTGCGAACTTTCAGTATCCTGCCGAGTCTGTTCTGGCTTATAAAGAAGGCCAT
CTGAGCCCAGATATTGTGGCTGAACAAAAGAAGCTGGAAGCCGCAGACCTTGTGATATTC
CAGTTCCCCCTGCAGTGGTTTGGAGTCCCTGCCATTCTGAAAGGCTGGTTTGAGCGAGTG
TTCATAGGAGAGTTTGCTTACACTTACGCTGCCATGTATGACAAAGGACCCTTCCGGAGT
AAGAAGGCAGTGCTTTCCATCACCACTGGTGGCAGTGGCTCCATGTACTCTCTGCAAGGG
ATCCACGGGGACATGAATGTCATTCTCTGGCCAATTCAGAGTGGCATTCTGCATTTCTGT
GGCTTCCAAGTCTTAGAACCTCAACTGACATATAGCATTGGGCACACTCCAGCAGACGCC
CGAATTCAAATCCTGGAAGGATGGAAGAAACGCCTGGAGAATATTTGGGATGAGACACCA
CTGTATTTTGCTCCAAGCAGCCTCTTTGACCTAAACTTCCAGGCAGGATTCTTAATGAAA
AAAGAGGTACAGGATGAGGAGAAAAACAAGAAATTTGGCCTTTCTGTGGGCCATCACTTG
GGCAAGTCCATCCCAACTGACAACCAGATCAAAGCTAGAAAATGA
Enzyme 1 GenBank Gene ID J03934 Link Image
Enzyme 1 GeneCard ID NQO1 Link Image
Enzyme 1 GenAtlas ID NQO1 Link Image
Enzyme 1 HGNC ID HGNC:2874 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16q22.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Jaiswal AK, McBride OW, Adesnik M, Nebert DW: Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16. J Biol Chem. 1988 Sep 25;263(27):13572-8. [PubMed Link Image]
  2. Jaiswal AK: Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin. Biochemistry. 1991 Nov 5;30(44):10647-53. [PubMed Link Image]
  3. Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM: Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3177-82. [PubMed Link Image]
  4. Traver RD, Horikoshi T, Danenberg KD, Stadlbauer TH, Danenberg PV, Ross D, Gibson NW: NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity. Cancer Res. 1992 Feb 15;52(4):797-802. [PubMed Link Image]
  5. Kristiansen OP, Larsen ZM, Johannesen J, Nerup J, Mandrup-Poulsen T, Pociot F: No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population. DIEGG and DSGD. Danish IDDM Epidemiology and Genetics Group and The Danish Study Group of Diabetes in Childhood. Hum Mutat. 1999;14(1):67-70. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 7028
Enzyme 2 Name Vitamin K-dependent gamma-carboxylase
Enzyme 2 Synonyms
  1. Gamma-glutamyl carboxylase
  2. Vitamin K gamma glutamyl carboxylase
Enzyme 2 Gene Name GGCX
Enzyme 2 Protein Sequence >Vitamin K-dependent gamma-carboxylase 
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTD
PASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYT
IMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYW
SVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSP
FKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFS
YVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRH
QLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRT
GELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQR
IFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHL
ENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYM
YVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFL
RRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEV
TYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
Enzyme 2 Number of Residues 758
Enzyme 2 Molecular Weight 87562
Enzyme 2 Theoretical pI 8.10
Enzyme 2 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • gamma-glutamyl carboxylase activity
  • lyase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptidyl-amino acid modification
  • peptidyl-glutamic acid carboxylation
  • peptidyl-glutamic acid modification
  • physiological process
  • protein modification
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium binding gamma-carboxyglutamate (Gla) residues with the concomitant convertion of the reduced hydroquinone form of vitamin K to vitamin K epoxide
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 61-81 114-134 137-157 293-313 362-382
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 184028 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P38435 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name VKGC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2277 bp 
ATGGCGGTGTCTGCCGGGTCCGCGCGGACCTCGCCCAGCTCAGATAAAGTACAGAAAGAC
AAGGCTGAACTGATCTCAGGGCCCAGGCAGGACAGCCGAATAGGGAAACTCTTGGGTTTT
GAGTGGACAGATTTGTCCAGTTGGCGGAGGCTGGTGACCCTGCTGAATCGACCAACGGAC
CCTGCAAGCTTAGCTGTCTTTCGTTTTCTTTTTGGGTTCTTGATGGTGCTAGACATTCCC
CAGGAGCGGGGGCTCAGCTCTCTGGACCGGAAATACCTTGATGGGCTGGATGTGTGCCGC
TTCCCCTTGCTGGATGCCCTACGCCCACTGCCACTTGACTGGATGTATCTTGTCTACACC
ATCATGTTTCTGGGGGCACTGGGCATGATGCTGGGCCTGTGCTACCGGATAAGCTGTGTG
TTATTCCTGCTGCCATACTGGTATGTGTTTCTCCTGGACAAGACATCATGGAACAACCAC
TCCTATCTGTATGGGTTGTTGGCCTTTCAGCTAACATTCATGGATGCAAACCACTACTGG
TCTGTGGACGGTCTGCTGAATGCCCATAGGAGGAATGCCCACGTGCCCCTTTGGAACTAT
GCAGTGCTCCGTGGCCAGATCTTCATTGTGTACTTCATTGCGGGTGTGAAAAAGCTGGAT
GCAGACTGGGTTGAAGGCTATTCCATGGAATATTTGTCCCGGCACTGGCTCTTCAGTCCC
TTCAAACTGCTGTTGTCTGAGGAGCTGACTAGCCTGCTGGTCGTGCACTGGGGTGGGCTG
CTGCTTGACCTCTCAGCTGGTTTCCTGCTCTTTTTTGATGTCTCAAGATCCATTGGCCTG
TTCTTTGTGTCCTACTTCCACTGCATGAATTCCCAGCTTTTCAGCATTGGTATGTTCTCC
TACGTCATGCTGGCCAGCAGCCCTCTCTTCTGCTCCCCTGAGTGGCCTCGGAAGCTGGTG
TCCTACTGCCCCCAAAGGTTGCAACAACTGTTGCCCCTCAAGGCAGCCCCTCAGCCCAGT
GTTTCCTGTGTGTATAAGAGGAGCCGGGGCAAAAGTGGCCAGAAGCCAGGGCTGCGCCAT
CAGCTGGGAGCTGCCTTCACCCTGCTCTACCTCCTGGAGCAGCTATTCCTGCCCTATTCT
CATTTTCTCACCCAGGGCTATAACAACTGGACAAATGGGCTGTATGGCTATTCCTGGGAC
ATGATGGTGCACTCCCGTTCCCACCAGCACGTGAAGATCACCTACCGTGATGGCCGCACT
GGCGAACTGGGCTACCTTAACCCTGGGGTATTTACACAGAGTCGGCGATGGAAGGATCAT
GCAGACATGCTGAAGCAATATGCCACTTGCCTGAGCCGCCTGCTTCCCAAGTATAATGTC
ACTGAGCCCCAGATCTACTTTGATATTTGGGTCTCCATCAATGACCGCTTCCAGCAGAGG
ATTTTTGACCCTCGTGTGGACATCGTGCAGGCCGCTTGGTCACCCTTTCAGCGCACATCC
TGGGTGCAACCACTCTTGATGGACCTGTCTCCCTGGAGGGCCAAGTTACAGGAAATCAAG
AGCAGCCTAGACAACCACACTGAGGTGGTCTTCATTGCAGATTTCCCTGGACTGCACTTG
GAGAATTTTGTGAGTGAAGACCTGGGCAACACTAGCATCCAGCTGCTGCAGGGGGAAGTG
ACTGTGGAGCTTGTGGCAGAACAGAAGAACCAGACTCTTCGAGAGGGAGAAAAAATGCAG
TTGCCTGCTGGTGAGTACCATAAGGTGTATACGACATCACCTAGCCCTTCTTGCTACATG
TACGTCTATGTCAACACTACAGAGCTTGCACTGGAGCAAGACCTGGCATATCTGCAAGAA
TTAAAGGAAAAGGTGGAGAATGGAAGTGAAACAGGGCCTCTACCCCCAGAGCTGCAGCCT
CTGTTGGAAGGGGAAGTAAAAGGGGGCCCTGAGCCAACACCTCTGGTTCAGACCTTTCTT
AGACGCCAACAAAGGCTCCAGGAGATTGAACGCCGGCGAAATACTCCTTTCCATGAGCGA
TTCTTCCGCTTCTTGTTGCGAAAGCTCTATGTCTTTCGCCGCAGCTTCCTGATGACTTGT
ATCTCACTTCGAAATCTGATATTAGGCCGTCCTTCCCTGGAGCAGCTGGCCCAGGAGGTG
ACTTATGCAAACTTGAGACCCTTTGAGGCAGTTGGAGAACTGAATCCCTCAAACACGGAT
TCTTCACATTCTAATCCTCCTGAGTCAAATCCTGATCCTGTCCACTCAGAGTTCTGA
Enzyme 2 GenBank Gene ID M81592 Link Image
Enzyme 2 GeneCard ID GGCX Link Image
Enzyme 2 GenAtlas ID GGCX Link Image
Enzyme 2 HGNC ID HGNC:4247 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Wu SM, Cheung WF, Frazier D, Stafford DW: Cloning and expression of the cDNA for human gamma-glutamyl carboxylase. Science. 1991 Dec 13;254(5038):1634-6. [PubMed Link Image]
  2. Wu SM, Stafford DW, Frazier LD, Fu YY, High KA, Chu K, Sanchez-Vega B, Solera J: Genomic sequence and transcription start site for the human gamma-glutamyl carboxylase. Blood. 1997 Jun 1;89(11):4058-62. [PubMed Link Image]
  3. Brenner B, Sanchez-Vega B, Wu SM, Lanir N, Stafford DW, Solera J: A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors. Blood. 1998 Dec 15;92(12):4554-9. [PubMed Link Image]
  4. Spronk HM, Farah RA, Buchanan GR, Vermeer C, Soute BA: Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors. Blood. 2000 Nov 15;96(10):3650-2. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 16521
Enzyme 3 Name cDNA, FLJ92690, Homo sapiens NAD(P)H dehydrogenase, quinone 1 (NQO1), mRNA (NAD(P)H dehydrogenase, quinone 1, isoform CRA_c)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name NQO1
Enzyme 3 Protein Sequence >cDNA, FLJ92690, Homo sapiens NAD(P)H dehydrogenase, quinone 1 (NQO1), mRNA (NAD(P)H dehydrogenase, quinone 1, isoform CRA_c) 
MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKL
KDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERV
FIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFC
GFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMK
KEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
Enzyme 3 Number of Residues 274
Enzyme 3 Molecular Weight 30868
Enzyme 3 Theoretical pI 9.34
Enzyme 3 GO Classification
Function
  • NAD(P)H dehydrogenase (quinone) activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B2R5Y9 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B2R5Y9_HUMAN Link Image
Enzyme 3 PDB ID 1KBQ Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK312368 Link Image
Enzyme 3 GeneCard ID B2R5Y9 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16q22.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available