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Human Metabolome Database Version 2.5

 

Showing metabocard for GDP-L-fucose (HMDB01095)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:33
Accession Number HMDB01095
Secondary Accession Numbers Not Available
Common Name GDP-L-fucose
Description GDP-L-fucose is a sugar nucleotide and a readily available source of fucose. Fucose is a deoxyhexose that is found in nearly all plant and animal species. The monosaccharide plays several important metabolic roles in complex carbohydrates and in glycoproteins. Fucosylated oligosaccharides are involved in cell-cell recognition, selectin-mediated leukocyte-endothelial adhesion, and mouse embryogenesis. They form the basis of the Lewis-type blood group antigens, are involved in the formation of atherosclerosis, and mediate host-bacterial interactions. A decrease in the availability of fucose is associated with leukocyte adhesion deficiency type-II disorder, and fucosylated glycoproteins have been implicated in memory processes. Fucose is made available during the synthesis of fucosylated glycolipids, oligosaccharides, and glycoproteins via a sugar nucleotide intermediate, specifically GDP-L-fucose. GTP-L-fucose pyrophosphorylase (GFPP, E. C. 2.7.7.30) catalyzes the reversible condensation of guanosine triphosphate and beta-L-fucose-1-phosphate to form the nucleotide-sugar GDP-L-fucose. The enzyme functions primarily in the mammalian liver and kidney to salvage free L-fucose during the breakdown of glycolipids and glycoproteins. (PMID: 16086588)
Synonyms
  1. GDP-beta-L-fucose
  2. (6-deoxy-beta-l-galactopyranosyl) ester
  3. Guanosine diphosphate fucose
  4. gdp fucose
  5. guanosine diphosphofucose
Chemical IUPAC Name [5-(2-amino-6-oxo-3,9-dihydropurin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-yl]methoxy-[hydroxy-(3,4,5-trihydroxy-6-methyl-tetrahydropyran-2-yl)oxy-phosp
horyl]oxy-phosphinic acid
Chemical Formula C16H25N5O15P2
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
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Fructose and mannose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 589.342
Monoisotopic Molecular Weight 589.082214
Isomeric SMILES C[C@@H]1OC(OP(O)(=O)OP(O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C2N=C(N)NC3=O)[C@@H](O)[C@H](O)[C@@H]1O
Canonical SMILES CC1OC(OP(O)(=O)OP(O)(=O)OCC2OC(C(O)C2O)N2C=NC3=C2N=C(N)NC3=O)C(O)C(O)C1O
KEGG Compound ID C00325 Link Image
BioCyc ID GUANOSINE_DIPHOSPHATE_FUCOSE Link Image
BiGG ID 34623 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01095 Link Image
Metagene Link HMDB01095 Link Image
METLIN ID 6001 Link Image
PubChem Compound 27505 Link Image
PubChem Substance 170094 Link Image
ChEBI ID 17009 Link Image
CAS Registry Number 15839-70-0
InChI Identifier InChI=1/C16H25N5O15P2/c1-4-7(22)9(24)11(26)15(33-4)35-38(30,31)36-37(28,29)32-2-5-8(23)10(25)14(34-5)21-3-18-6-12(21)19-16(17)20-13(6)27/h3-5,7-11,14-15,22-26H,2H2,1H3,(H,28,29)(H,30,31)(H3,17,19,20,27)/t4-,5+,7+,8+,9+,10+,11-,14+,15?/m0/s1
Synthesis Reference Yamamoto, Kenji; Maruyama, Takashi; Kumagai, Hidehiko; Tochikura, Tatsurokuro; Seno, Taiko; Yamaguchi, Hideo. Preparation of GDP-L-fucose by using microbial enzymes. Agricultural and Biological Chemistry (1984), 48(3), 823-4.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 7.04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.69 [Predicted by ALOGPS]; -5.2 [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)
  • golgi apparatus
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Intestine
Kidney
Neuron
Placenta
Platelet
Prostate
Skin
Spleen
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fructose and Mannose Degradation SMP00064 Link Image map00051 Link Image
General References
  1. Sales ME, Sterin-Borda L, de Bracco MM, Rodriguez M, Narbaitz M, Borda E: IgA from HIV+ haemophilic patients triggers intracellular signals coupled to the cholinergic system of the intestine. Clin Exp Immunol. 1997 Nov;110(2):189-95. [PubMed Link Image]
  2. Palma AS, Morais VA, Coelho AV, Costa J: Effect of the manganese ion on human alpha3/4 fucosyltransferase III activity. Biometals. 2004 Feb;17(1):35-43. [PubMed Link Image]
  3. Yegorov YE, Kazimirchuk EV, Terekhov SM, Karachentsev DN, Shirokova EA, Khandazhinskaya AL, Meshcheryakova JA, Corey DR, Zelenin AV: Telomerase-dependent reactivation of DNA synthesis in macrophages implies alteration of telomeres. Cell Biol Int. 2002;26(12):1019-27. [PubMed Link Image]
  4. Coates SW Jr, Hogenauer C, Santa Ana CA, Rosenblatt RL, Emmett M, Fordtran JS: Inhibition of neutral sodium absorption by a prostaglandin analogue in patients with cystic fibrosis. Gastroenterology. 2004 Jul;127(1):65-72. [PubMed Link Image]
  5. Galiegue S, Mary S, Marchand J, Dussossoy D, Carriere D, Carayon P, Bouaboula M, Shire D, Le Fur G, Casellas P: Expression of central and peripheral cannabinoid receptors in human immune tissues and leukocyte subpopulations. Eur J Biochem. 1995 Aug 15;232(1):54-61. [PubMed Link Image]
  6. Anfossi G, Russo I, Massucco P, Mattiello L, Doronzo G, De Salve A, Trovati M: Impaired synthesis and action of antiaggregating cyclic nucleotides in platelets from obese subjects: possible role in platelet hyperactivation in obesity. Eur J Clin Invest. 2004 Jul;34(7):482-9. [PubMed Link Image]
  7. Rastaldi MP, Armelloni S, Berra S, Li M, Pesaresi M, Poczewski H, Langer B, Kerjaschki D, Henger A, Blattner SM, Kretzler M, Wanke R, D'Amico G: Glomerular podocytes possess the synaptic vesicle molecule Rab3A and its specific effector rabphilin-3a. Am J Pathol. 2003 Sep;163(3):889-99. [PubMed Link Image]
  8. Sibley CP, Hochberg A, Boime I: Bromo-adenosine stimulates choriogonadotropin production in JAr and cytotrophoblast cells: evidence for effects on two stages of differentiation. Mol Endocrinol. 1991 Apr;5(4):582-6. [PubMed Link Image]
  9. Rosenfeldt HM, Hobson JP, Milstien S, Spiegel S: The sphingosine-1-phosphate receptor EDG-1 is essential for platelet-derived growth factor-induced cell motility. Biochem Soc Trans. 2001 Nov;29(Pt 6):836-9. [PubMed Link Image]
  10. Sawamura D, Abe R, Goto M, Akiyama M, Hemmi H, Akira S, Shimizu H: Direct injection of plasmid DNA into the skin induces dermatitis by activation of monocytes through toll-like receptor 9. J Gene Med. 2005 May;7(5):664-71. [PubMed Link Image]
  11. Huopaniemi L, Kolmer M, Niittymaki J, Pelto-Huikko M, Renkonen R: Inflammation-induced transcriptional regulation of Golgi transporters required for the synthesis of sulfo sLex glycan epitopes. Glycobiology. 2004 Dec;14(12):1285-94. Epub 2004 Jul 21. [PubMed Link Image]
  12. Noda K, Miyoshi E, Gu J, Gao CX, Nakahara S, Kitada T, Honke K, Suzuki K, Yoshihara H, Yoshikawa K, Kawano K, Tonetti M, Kasahara A, Hori M, Hayashi N, Taniguchi N: Relationship between elevated FX expression and increased production of GDP-L-fucose, a common donor substrate for fucosylation in human hepatocellular carcinoma and hepatoma cell lines. Cancer Res. 2003 Oct 1;63(19):6282-9. [PubMed Link Image]
  13. Qi H, Fournier A, Grenier J, Fillion C, Labrie Y, Labrie C: Isolation of the novel human guanine nucleotide exchange factor Src homology 3 domain-containing guanine nucleotide exchange factor (SGEF) and of C-terminal SGEF, an N-terminally truncated form of SGEF, the expression of which is regulated by androgen in prostate cancer cells. Endocrinology. 2003 May;144(5):1742-52. [PubMed Link Image]
  14. Jakob G, Mair J, Vorderwinkler KP, Judmaier G, Konig P, Zwierzina H, Pichler M, Puschendorf B: Clinical significance of urinary cyclic guanosine monophosphate in diagnosis of heart failure. Clin Chem. 1994 Jan;40(1):96-100. [PubMed Link Image]
  15. da Silva CD, Brunini TM, Reis PF, Moss MB, Santos SF, Roberts NB, Ellory JC, Mann GE, Mendes-Ribeiro AC: Effects of nutritional status on the L-arginine-nitric oxide pathway in platelets from hemodialysis patients. Kidney Int. 2005 Nov;68(5):2173-9. [PubMed Link Image]
  16. Andre M, Latado H, Felley-Bosco E: Inducible nitric oxide synthase-dependent stimulation of PKGI and phosphorylation of VASP in human embryonic kidney cells. Biochem Pharmacol. 2005 Feb 15;69(4):595-602. Epub 2004 Dec 22. [PubMed Link Image]
  17. Benitah SA, Frye M, Glogauer M, Watt FM: Stem cell depletion through epidermal deletion of Rac1. Science. 2005 Aug 5;309(5736):933-5. [PubMed Link Image]
Metabolic Enzymes
  1. Fucose-1-phosphate guanylyltransferase
  2. Galactoside 2-alpha-L-fucosyltransferase 1
  3. GDP-L-fucose synthetase
  4. Alpha-(1,3)-fucosyltransferase
  5. Alpha-(1,3)-fucosyltransferase
  6. cDNA FLJ78078, highly similar to Human alpha (1,3/1,4) fucosyltransferase (FUT3) (Fucosyltransferase 3) (Galactoside 3(4)-L- fucosyltransferase, Lewis blood group)
  7. Alpha-(1,3)-fucosyltransferase
  8. cDNA FLJ75308, highly similar to Human alpha(1,2)fucosyltransferase (FUT2) gene (HCG1998026, isoform CRA_a)
  9. cDNA, FLJ94122, Homo sapiens tissue specific transplantation antigen P35B (TSTA3),mRNA (Tissue specific transplantation antigen P35B, isoform CRA_b)
  10. Alpha-(1,3)-fucosyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5486
Enzyme 1 Name Fucose-1-phosphate guanylyltransferase
Enzyme 1 Synonyms
  1. GDP-L-fucose pyrophosphorylase
  2. GDP-L-fucose diphosphorylase
Enzyme 1 Gene Name FPGT
Enzyme 1 Protein Sequence >Fucose-1-phosphate guanylyltransferase
MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
Enzyme 1 Number of Residues 594
Enzyme 1 Molecular Weight 66600
Enzyme 1 Theoretical pI 6.44
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids
Enzyme 1 Pathways
Enzyme 1 Reactions
  • GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2582185 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14772 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FPGT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1785 bp
ATGGCAGCTGCTAGGGACCCTCCGGAAGTATCGCTGCGAGAAGCCACCCAGCGAAAATTG
CGGAGGTTTTCCGAGCTAAGAGGCAAACTTGTAGCACGTGGAGAATTCTGGGACATAGTT
GCAATAACAGCGGCTGATGAAAAACAGGAACTTGCTTACAACCAACAGCTGTCAGAAAAG
CTGAAAAGAAAGGAGTTACCCCTTGGAGTTCAATATCACGTTTTTGTGGATCCTGCTGGA
GCCAAAATTGGAAATGGAGGATCAACACTTTGTGCCCTTCAATGTTTGGAAAAGCTATAT
GGAGATAAATGGAATTCTTTTACCATCTTATTAATTCACTCTGGTGGCTACAGTCAACGA
CTTCCAAATGCAAGTGCTCTGGGAAAAATTTTCACTGCTTTACCTCTTGGTAACCCCATT
TATCAGATGCTAGAATTAAAGCTAGCCATGTACATTGATTTCCCCTTAAATATGAATCCT
GGAATTCTGGTTACCTGTGCAGATGATATTGAACTTTATAGTATTGGAGAATTTGAGTTT
ATTAGGTTTGACAAACCTGGCTTTACTGCTTTAGCTCATCCTTCTAGTTTGACGATAGGT
ACCACACATGGAGTATTTGTCTTAGATCCTTTTGATGATTTAAAACATAGAGACCTTGAA
TACAGGTCTTGCCATCGTTTCCTTCATAAGCCCAGCATAGAAAAGATGTATCAGTTTAAT
GCTGTGTGTAGACCTGGAAATTTTTGTCAACAGGACTTTGCTGGGGGTGACATTGCCGAT
CTTAAATTAGACTCTGACTATGTCTACACAGATAGCCTATTTTATATGGATCATAAATCA
GCAAAAATGTTACTTGCTTTTTATGAAAAAATAGGCACACTGAGCTGTGAAATAGATGCC
TATGGTGACTTTCTGCAGGCTTTGGGACCTGGAGCAACTGTGGAGTACACCAGAAACACA
TCACATGTCATTAAAGAAGAGTCAGAGTTGGTAGAAATGAGGCAGAGAATATTTCATCTT
CTTAAAGGAACATCACTAAATGTTGTTGTTCTTAATAACTCCAAATTTTATCACATTGGA
ACAACCGAAGAATATTTGTTTTACTTTACCTCAGATAACAGTTTAAAGTCAGAGCTCGGC
TTACAGTCCATAACTTTTAGTATCTTTCCAGATATACCAGAATGCTCTGGCAAAACATCC
TGTATCATTCAAAGCATACTGGATTCAAGATGTTCTGTGGCACCTGGCTCAGTTGTGGAG
TATTCCAGATTGGGGCCTGATGTTTCAGTTGGGGAAAACTGCATTATTAGTGGTTCTTAC
ATCCTAACAAAAGCTGCCCTCCCCGCACATTCTTTTGTATGTTCCTTAAGCTTAAAGATG
AATAGATGCTTAAAGTATGCAACTATGGCATTTGGAGTGCAAGACAACTTGAAAAAGAGT
GTGAAAACATTGTCAGATATAAAGTTACTTCAATTCTTTGGAGTCTGTTTCCTGTCATGC
TTAGATGTTTGGAATCTTAAAGTTACAGAGGAACTGTTCTCTGGTAACAAGACATGTCTG
AGTTTGTGGACTGCACGCATTTTCCCAGTTTGTTCTTCTTTGAGTGACTCAGTTATAACA
TCCCTAAAGATGTTAAATGCTGTTAAGAACAAGTCAGCATTCAGCCTGAATAGCTATAAG
TTGCTGTCCATTGAAGAAATGCTTATCTACAAAGATGTAGAAGATATGATAACTTACAGG
GAACAAATTTTTCTAGAAATCAGTTTAAAAAGCAGTTTGATGTAG
Enzyme 1 GenBank Gene ID AF017445 Link Image
Enzyme 1 GeneCard ID FPGT Link Image
Enzyme 1 GenAtlas ID FPGT Link Image
Enzyme 1 HGNC ID HGNC:3825 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p31.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD: GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. J Biol Chem. 1998 Nov 13;273(46):30165-74. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5707
Enzyme 2 Name Galactoside 2-alpha-L-fucosyltransferase 1
Enzyme 2 Synonyms
  1. GDP-L- fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1
  2. Alpha(1,2FT 1
  3. Fucosyltransferase 1
  4. Blood group H alpha 2- fucosyltransferase
Enzyme 2 Gene Name FUT1
Enzyme 2 Protein Sequence >Galactoside 2-alpha-L-fucosyltransferase 1
MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGT
AMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAAL
APVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQ
IRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSA
YLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQC
NHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLW
TLAKP
Enzyme 2 Number of Residues 365
Enzyme 2 Molecular Weight 41252
Enzyme 2 Theoretical pI 7.38
Enzyme 2 GO Classification
Function
  • alpha(1,2)-fucosyltransferase activity
  • catalytic activity
  • fucosyltransferase activity
  • galactoside 2-alpha-L-fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • Golgi apparatus
  • cell
  • intracellular membrane-bound organelle
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. H and Se enzymes fucosylate the same acceptor substrates but exhibit different Km values
Enzyme 2 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Globoside metabolism (map00603 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 2 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 306830 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P19526 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name FUT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1098 bp
ATGTGGCTCCGGAGCCATCGTCAGCTCTGCCTGGCCTTCCTGCTAGTCTGTGTCCTCTCT
GTAATCTTCTTCCTCCATATCCATCAAGACAGCTTTCCACATGGCCTAGGCCTGTCGATC
CTGTGTCCAGACCGCCGCCTGGTGACACCCCCAGTGGCCATCTTCTGCCTGCCGGGTACT
GCGATGGGCCCCAACGCCTCCTCTTCCTGTCCCCAGCACCCTGCTTCCCTCTCCGGCACC
TGGACTGTCTACCCCAATGGCCGGTTTGGTAATCAGATGGGACAGTATGCCACGCTGCTG
GCTCTGGCCCAGCTCAACGGCCGCCGGGCCTTTATCCTGCCTGCCATGCATGCCGCCCTG
GCCCCGGTATTCCGCATCACCCTGCCCGTGCTGGCCCCAGAAGTGGACAGCCGCACGCCG
TGGCGGGAGCTGCAGCTTCACGACTGGATGTCGGAGGAGTACGCGGACTTGAGAGATCCT
TTCCTGAAGCTCTCTGGCTTCCCCTGCTCTTGGACTTTCTTCCACCATCTCCGGGAACAG
ATCCGCAGAGAGTTCACCCTGCACGACCACCTTCGGGAAGAGGCGCAGAGTGTGCTGGGT
CAGCTCCGCCTGGGCCGCACAGGGGACCGCCCGCGCACCTTTGTCGGCGTCCACGTGCGC
CGTGGGGACTATCTGCAGGTTATGCCTCAGCGCTGGAAGGGTGTGGTGGGCGACAGCGCC
TACCTCCGGCAGGCCATGGACTGGTTCCGGGCACGGCACGAAGCCCCCGTTTTCGTGGTC
ACCAGCAACGGCATGGAGTGGTGTAAAGAAAACATCGACACCTCCCAGGGCGATGTGACG
TTTGCTGGCGATGGACAGGAGGCTACACCGTGGAAAGACTTTGCCCTGCTCACACAGTGC
AACCACACCATTATGACCATTGGCACCTTCGGCTTCTGGGCTGCCTACCTGGCTGGCGGA
GACACTGTCTACCTGGCCAACTTCACCCTGCCAGACTCTGAGTTCCTGAAGATCTTTAAG
CCGGAGGCGGCCTTCCTGCCCGAGTGGGTGGGCATTAATGCAGACTTGTCTCCACTCTGG
ACATTGGCTAAGCCTTGA
Enzyme 2 GenBank Gene ID M35531 Link Image
Enzyme 2 GeneCard ID FUT1 Link Image
Enzyme 2 GenAtlas ID FUT1 Link Image
Enzyme 2 HGNC ID HGNC:4012 Link Image
Enzyme 2 Chromosome Location 19
Enzyme 2 Locus 19q13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Larsen RD, Ernst LK, Nair RP, Lowe JB: Molecular cloning, sequence, and expression of a human GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6674-8. [PubMed Link Image]
  2. Wagner FF, Flegel WA: Polymorphism of the h allele and the population frequency of sporadic nonfunctional alleles. Transfusion. 1997 Mar;37(3):284-90. [PubMed Link Image]
  3. Kaneko M, Nishihara S, Shinya N, Kudo T, Iwasaki H, Seno T, Okubo Y, Narimatsu H: Wide variety of point mutations in the H gene of Bombay and para-Bombay individuals that inactivate H enzyme. Blood. 1997 Jul 15;90(2):839-49. [PubMed Link Image]
  4. Kelly RJ, Ernst LK, Larsen RD, Bryant JG, Robinson JS, Lowe JB: Molecular basis for H blood group deficiency in Bombay (Oh) and para-Bombay individuals. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):5843-7. [PubMed Link Image]
  5. Koda Y, Soejima M, Johnson PH, Smart E, Kimura H: Missense mutation of FUT1 and deletion of FUT2 are responsible for Indian Bombay phenotype of ABO blood group system. Biochem Biophys Res Commun. 1997 Sep 8;238(1):21-5. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6213
Enzyme 3 Name GDP-L-fucose synthetase
Enzyme 3 Synonyms
  1. Protein FX
  2. Red cell NADP(H- binding protein
  3. GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4- reductase
Enzyme 3 Gene Name TSTA3
Enzyme 3 Protein Sequence >GDP-L-fucose synthetase
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEK
VQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPD
KTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNF
NIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPI
ILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTP
FKQAVKETCAWFTDNYEQARK
Enzyme 3 Number of Residues 321
Enzyme 3 Molecular Weight 35893
Enzyme 3 Theoretical pI 6.59
Enzyme 3 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Two step NADP-dependent conversion of GDP-4-dehydro-6- deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction
Enzyme 3 Pathways
Enzyme 3 Reactions
  • GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1381179 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q13630 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name FCL_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >966 bp
ATGGGTGAACCCCAGGGATCCATGCGGATTCTAGTGACAGGGGGCTCTGGGCTGGTAGGC
AAAGCCATCCAGAAGGTGGTAGCAGATGGAGCTGGACTTCCTGGAGAGGACTGGGTGTTT
GTCTCCTCTAAAGACGCCGATCTCACGGATACAGCACAGACCCGCGCCCTGTTTGAGAAG
GTCCAACCCACACACGTCATCCATCTTGCTGCAATGGTGGGGGGCCTGTTCCGGAATATC
AAATACAATTTGGACTTCTGGAGGAAAAACGTGCACATGAACGACAACGTCCTGCACTCG
GCCTTTGAGGTGGGGGCCCGCAAGGTGGTGTCCTGCCTGTCCACCTGTATCTTCCCTGAC
AAGACGACCTACCCGATAGATGAGACCATGATCCACAATGGGCCTCCCCACAACAGCAAT
TTTGGGTACTCGTATGCCAAGAGGATGATCGACGTGCAGAACAGGGCCTACTTCCAGCAG
TACGGCTGCACCTTCACCGCTGTCATCCCCACCAACGTTTTCGGGCCCCACGACAACTTC
AACATCGAGGATGGCCACGTGCTGCCTGGCCTCATCCACAAGGTGCACCTGGCCAAGAGC
AGCGGCTCGGCCCTGACGGTGTGGGGTACAGGGAATCCGCGGAGGCAGTTCATATACTCG
CTGGACCTGGCCCAGCTCTTTATCTGGGTCCTGCGGGAGTACAATGAAGTGGAGCCCATC
ATCCTCTCCGTGGGCGAGGAAGATGAGGTCTCCATCAAGGAGGCAGCCGAGGCGGTGGTG
GAGGCCATGGACTTCCATGGGGAAGTCACCTTTGATACAACCAAGTCGGATGGGCAGTTT
AAGAAGACAGCCAGTAACAGCAAGCTGAGGACCTACCTGCCCGACTTCCGGTTCACACCC
TTCAAGCAGGCGGTGAAGGAGACCTGTGCTTGGTTCACTGACAACTACGAGCAGGCCCGG
AAGTGA
Enzyme 3 GenBank Gene ID U58766 Link Image
Enzyme 3 GeneCard ID TSTA3 Link Image
Enzyme 3 GenAtlas ID TSTA3 Link Image
Enzyme 3 HGNC ID HGNC:12390 Link Image
Enzyme 3 Chromosome Location 8
Enzyme 3 Locus 8q24.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Tonetti M, Sturla L, Bisso A, Benatti U, De Flora A: Synthesis of GDP-L-fucose by the human FX protein. J Biol Chem. 1996 Nov 1;271(44):27274-9. [PubMed Link Image]
  2. Camardella L, Carratore V, Ciardiello MA, Damonte G, Benatti U, De Flora A: Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B. Blood. 1995 Jan 1;85(1):264-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6308
Enzyme 4 Name Alpha-(1,3)-fucosyltransferase
Enzyme 4 Synonyms
  1. Galactoside 3-L- fucosyltransferase
  2. Fucosyltransferase 5
  3. FucT-V
  4. Fuc-TV
Enzyme 4 Gene Name FUT5
Enzyme 4 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPN
GSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVI
VHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFT
PYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHK
PLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPP
DAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQQE
SRYQTVRSIAAWFT
Enzyme 4 Number of Residues 374
Enzyme 4 Molecular Weight 43008
Enzyme 4 Theoretical pI 8.37
Enzyme 4 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function May catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens
Enzyme 4 Pathways
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 4 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl-R
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-27
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1280209 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q11128 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name FUT5_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1125 bp
ATGGATCCCCTGGGCCCAGCCAAGCCACAGTGGCTGTGGCGCCGCTGTCTGGCCGGGCTG
CTGTTTCAGCTGCTGGTGGCTGTGTGTTTCTTCTCCTACCTGCGTGTGTCCCGAGACGAT
GCCACTGGATCCCCTAGGCCAGGGCTTATGGCAGTGGAACCTGTCACCGGGGCTCCCAAT
GGGTCCCGCTGCCAGGACAGCATGGCGACCCCTGCCCACCCCACCCTACTGATCCTGCTG
TGGACGTGGCCTTTTAACACACCCGTGGCTCTGCCCCGCTGCTCAGAGATGGTGCCCGGC
GCGGCCGACTGCAACATCACTGCCGACTCCAGTGTGTACCCACAGGCAGACGCGGTCATC
GTGCACCACTGGGATATCATGTACAACCCCAGTGCCAACCTCCCGCCCCCCACCAGGCCG
CAGGGGCAGCGCTGGATCTGGTTCAGCATGGAGTCCCCCAGCAACTGCCGGCACCTGGAA
GCCCTGGACGGATACTTCAATCTCACCATGTCCTACCGCAGCGACTCCGACATCTTCACG
CCCTACGGCTGGCTGGAGCCGTGGTCCGGCCAGCCTGCCCACCCACCGCTCAACCTCTCG
GCCAAGACCGAGCTGGTGGCCTGGGCGGTGTCCAACTGGAAGCCGGACTCGGCCAGGGTG
CGCTACTACCAGAGCCTGCAGGCTCATCTCAAGGTGGACGTGTACGGACGCTCCCACAAG
CCCCTGCCCAAGGGGACCATGATGGAGACGCTGTCCCGGTACAAGTTCTATCTGGCCTTC
GAGAACTCCTTGCACCCCGACTACATCACCGAGAAGCTGTGGAGGAACGCCCTGGAGGCC
TGGGCCGTGCCCGTGGTGCTGGGCCCCAGCAGAAGCAACTACGAGAGGTTCCTGCCGCCC
GACGCCTTCATCCACGTGGATGACTTCCAGAGCCCCAAGGACCTGGCCCGGTACCTGCAG
GAGCTGGACAAGGACCACGCCCGCTACCTGAGCTACTTTCGCTGGCGGGAGACGCTGCGG
CCTCGCTCCTTCAGCTGGGCACTGGCTTTCTGCAAGGCCTGCTGGAAGCTGCAGCAGGAA
TCCAGGTACCAGACGGTGCGCAGCATAGCGGCTTGGTTCACCTGA
Enzyme 4 GenBank Gene ID M81485 Link Image
Enzyme 4 GeneCard ID FUT5 Link Image
Enzyme 4 GenAtlas ID FUT5 Link Image
Enzyme 4 HGNC ID HGNC:4016 Link Image
Enzyme 4 Chromosome Location 19
Enzyme 4 Locus 19p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Weston BW, Nair RP, Larsen RD, Lowe JB: Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J Biol Chem. 1992 Feb 25;267(6):4152-60. [PubMed Link Image]
  2. Cameron HS, Szczepaniak D, Weston BW: Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. J Biol Chem. 1995 Aug 25;270(34):20112-22. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 11509
Enzyme 5 Name Alpha-(1,3)-fucosyltransferase
Enzyme 5 Synonyms
  1. Galactoside 3-L- fucosyltransferase
  2. Fucosyltransferase 9
  3. FucT-IX
Enzyme 5 Gene Name FUT9
Enzyme 5 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWIFSPMESASSVLKMKNFFSTKTDY
FNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNL
PQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVF
EVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISACKF
YLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDYNSPSELAK
YLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
Enzyme 5 Number of Residues 359
Enzyme 5 Molecular Weight 42041
Enzyme 5 Theoretical pI Not Available
Enzyme 5 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • (Gal)4 (Glc)1 (GlcNAc)3 (LFuc)2 (Cer)1 + GDP-L-fucose --> (Gal)4 (Glc)1 (GlcNAc)3 (LFuc)3 (Cer)1 + GDP + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 12-32
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 5139693 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y231 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name FUT9_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 AB023021 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID FUT9 Link Image
Enzyme 5 HGNC ID HGNC:4020 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Cailleau-Thomas A, Coullin P, Candelier JJ, Balanzino L, Mennesson B, Oriol R, Mollicone R: FUT4 and FUT9 genes are expressed early in human embryogenesis. Glycobiology. 2000 Aug;10(8):789-802. [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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15893
Enzyme 6 Name cDNA FLJ78078, highly similar to Human alpha (1,3/1,4) fucosyltransferase (FUT3) (Fucosyltransferase 3) (Galactoside 3(4)-L- fucosyltransferase, Lewis blood group)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name FUT3
Enzyme 6 Protein Sequence >cDNA FLJ78078, highly similar to Human alpha (1,3/1,4) fucosyltransferase (FUT3) (Fucosyltransferase 3) (Galactoside 3(4)-L- fucosyltransferase, Lewis blood group)
MDPLGAAKPQWPWRRCLAALLFQLLVAVCFFSYLRVSRDDATGSPRAPSGSSRQDTTPTR
PTLLILLWTWPFHIPVALSRCSEMVPGTADCHITADRKVYPQADTVIVHHWDIMSNPKSR
LPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPA
HPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSR
YKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPK
DLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTVRSIAAWF
T
Enzyme 6 Number of Residues 361
Enzyme 6 Molecular Weight 42117
Enzyme 6 Theoretical pI 9.23
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID A8K737 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8K737_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 AK291852 Link Image
Enzyme 6 GeneCard ID A8K737 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15894
Enzyme 7 Name Alpha-(1,3)-fucosyltransferase
Enzyme 7 Synonyms
  1. Galactoside 3-L-fucosyltransferase
  2. Fucosyltransferase 6
  3. FucT-VI
Enzyme 7 Gene Name FUT6
Enzyme 7 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MDPLGPAKPQWSWRCCLTTLLFQLLMAVCFFSYLRVSQDDPTVYPNGSRFPDSTGTPAHS
IPLILLWTWPFNKPIALPRCSEMVPGTADCNITADRKVYPQADAVIVHHREVMYNPSAQL
PRSPRRQGQRWIWFSMESPSHCWQLKAMDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAH
PPLNLSAKTELVAWAVSNWGPNSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRY
KFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKD
LARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQEESRYQTRGIAAWFT
Enzyme 7 Number of Residues 359
Enzyme 7 Molecular Weight 41860
Enzyme 7 Theoretical pI 8.82
Enzyme 7 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Enzyme involved in the biosynthesis of the E-Selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP- beta-fucose to alpha-2,3 sialylated substrates
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 15-34
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID P51993 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name FUT6_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 M98825 Link Image
Enzyme 7 GeneCard ID P51993 Link Image
Enzyme 7 GenAtlas ID FUT6 Link Image
Enzyme 7 HGNC ID HGNC:4017 Link Image
Enzyme 7 Chromosome Location 19
Enzyme 7 Locus 19p13.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Koszdin KL, Bowen BR: The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand. Biochem Biophys Res Commun. 1992 Aug 31;187(1):152-7. [PubMed Link Image]
  2. Weston BW, Smith PL, Kelly RJ, Lowe JB: Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes. J Biol Chem. 1992 Dec 5;267(34):24575-84. [PubMed Link Image]
  3. Cameron HS, Szczepaniak D, Weston BW: Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. J Biol Chem. 1995 Aug 25;270(34):20112-22. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15895
Enzyme 8 Name cDNA FLJ75308, highly similar to Human alpha(1,2)fucosyltransferase (FUT2) gene (HCG1998026, isoform CRA_a)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name Not Available
Enzyme 8 Protein Sequence >cDNA FLJ75308, highly similar to Human alpha(1,2)fucosyltransferase (FUT2) gene (HCG1998026, isoform CRA_a)
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQL
RGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATAS
RIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQK
FLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSLIFV
VTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTG
GDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
Enzyme 8 Number of Residues 343
Enzyme 8 Molecular Weight 39018
Enzyme 8 Theoretical pI 8.73
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
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 A8K2L2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K2L2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK290277 Link Image
Enzyme 8 GeneCard ID A8K2L2 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 Not Available
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16520
Enzyme 9 Name cDNA, FLJ94122, Homo sapiens tissue specific transplantation antigen P35B (TSTA3),mRNA (Tissue specific transplantation antigen P35B, isoform CRA_b)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name TSTA3
Enzyme 9 Protein Sequence >cDNA, FLJ94122, Homo sapiens tissue specific transplantation antigen P35B (TSTA3),mRNA (Tissue specific transplantation antigen P35B, isoform CRA_b)
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEK
VQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPD
KTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNF
NIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPI
ILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTP
FKQAVKETCAWFTDNYEQARK
Enzyme 9 Number of Residues 321
Enzyme 9 Molecular Weight 35893
Enzyme 9 Theoretical pI 6.59
Enzyme 9 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 9 General Function Cell wall/membrane/envelope biogenesis
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B2R8Y7 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2R8Y7_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK313560 Link Image
Enzyme 9 GeneCard ID B2R8Y7 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16962
Enzyme 10 Name Alpha-(1,3)-fucosyltransferase
Enzyme 10 Synonyms
  1. Galactoside 3-L-fucosyltransferase
  2. Fucosyltransferase 7
  3. FucT-VII
  4. Selectin-ligand synthase
Enzyme 10 Gene Name FUT7
Enzyme 10 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MNNAGHGPTRRLRGLGVLAGVALLAALWLLWLLGSAPRGTPAPQPTITILVWHWPFTDQP
PELPSDTCTRYGIARCHLSANRSLLASADAVVFHHRELQTRRSHLPLAQRPRGQPWVWAS
MESPSHTHGLSHLRGIFNWVLSYRRDSDIFVPYGRLEPHWGPSPPLPAKSRVAAWVVSNF
QERQLRARLYRQLAPHLRVDVFGRANGRPLCASCLVPTVAQYRFYLSFENSQHRDYITEK
FWRNALVAGTVPVVLGPPRATYEAFVPADAFVHVDDFGSARELAAFLTGMNESRYQRFFA
WRDRLRVRLFTDWRERFCAICDRYPHLPRSQVYEDLEGWFQA
Enzyme 10 Number of Residues 342
Enzyme 10 Molecular Weight 39239
Enzyme 10 Theoretical pI 10.25
Enzyme 10 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function May catalyze alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 15-36
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q11130 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name FUT7_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID X78031 Link Image
Enzyme 10 GeneCard ID Q11130 Link Image
Enzyme 10 GenAtlas ID FUT7 Link Image
Enzyme 10 HGNC ID HGNC:4018 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Natsuka S, Gersten KM, Zenita K, Kannagi R, Lowe JB: Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant. J Biol Chem. 1994 Jun 17;269(24):16789-94. [PubMed Link Image]
  2. Natsuka S, Gersten KM, Zenita K, Kannagi R, Lowe JB: Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant. J Biol Chem. 1994 Aug 12;269(32):20806. [PubMed Link Image]
  3. Sasaki K, Kurata K, Funayama K, Nagata M, Watanabe E, Ohta S, Hanai N, Nishi T: Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes. J Biol Chem. 1994 May 20;269(20):14730-7. [PubMed Link Image]
  4. de Vries T, Yen TY, Joshi RK, Storm J, van Den Eijnden DH, Knegtel RM, Bunschoten H, Joziasse DH, Macher BA: Neighboring cysteine residues in human fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures. Glycobiology. 2001 May;11(5):423-32. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available