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Human Metabolome Database Version 2.5

 

Showing metabocard for Uridine diphosphategalactose (HMDB00302)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:50
Accession Number HMDB00302
Secondary Accession Numbers Not Available
Common Name Uridine diphosphategalactose
Description Uridine diphosphategalactose (UDPgal) is a nucleoside diphosphate sugar which can be epimerized into UDPglucose for entry into the mainstream of carbohydrate metabolism. UDPgal is a pivotal compound in the metabolism of galactose. UDPgal is a product of the galactose-l-phosphate uridyl transferase (EC 2.7.7.10) reaction but may also be made from Glucose-l-P, involving uridine diphosphate galactose-4-epimerase (EC 5.1.3.2). UDPgal is the necessary galactosyl donor of galactose in the metabolism to incorporate it into complex oligosaccharides, glycoproteins and glycolipids (galactosides). Defective galactosylation of complex glycoconjugates exists in tissues from galactosemic patients. There is a tendency for galactosemic red cell UDPgal to be in the low normal range with a high uridine diphosphate glucose to UDP-gal ratio. This may reflect an inability of red cell UDPgal-4'-epimerase to maintain a normal ratio and consequently higher levels of UDPgal. In the more complex white blood cells and cultured fibroblasts, the UDPgal content and the uridine diphosphate glucose to UDPgal ratio of galactosemics are normal. Therefore, defective galactosylation observed in galactosemic fibroblasts must result from a defect in the transfer of galactose from UDPgal to these moieties. (PMID: 2122114, 7671968)
Synonyms
  1. GDU
  2. UDP-D-galactose
  3. UDP-Gal
  4. UDP-a-D-Galactose
  5. UDP-galactopyranose
  6. UDP-galactose
  7. UDPgalactose
  8. UPG
  9. Udp galactose
  10. Udp-alpha-d-galactose
  11. Udp-d-galactopyranose
  12. Udpgal
  13. Uridine 5'-(alpha-D-galactopyranosyl pyrophosphate)
  14. Uridine 5'-diphosphate galactose
  15. Uridine 5'-diphosphogalactose
  16. Uridine 5'-pyrophosphate D-galactosyl ester
  17. Uridine 5'-pyrophosphate a-D-galactopyranosyl ester
  18. Uridine 5'-pyrophosphate a-D-galactosyl ester
  19. Uridine 5'-pyrophosphate alpha-D-galactosyl ester
  20. Uridine diphosphate galactose
  21. Uridine diphosphate-D-galactose
  22. Uridine diphosphate-galactose
  23. Uridine diphosphogalactose
  24. Uridine pyrophosphate a-D-galactopyranosyl ester
  25. Uridine pyrophosphate alpha-d-galactopyranosyl ester
  26. Uridine pyrophosphogalactose
  27. Uridinediphosphate galactose
  28. Uridinediphosphogalactose
  29. UDP-delta-galactose
  30. UDP-alpha-delta-Galactose
  31. Udp-delta-galactopyranose
  32. Uridine 5'-(alpha-delta-galactopyranosyl pyrophosphate)
  33. Uridine 5'-pyrophosphate a-delta-galactopyranosyl ester
  34. Uridine 5'-pyrophosphate a-delta-galactosyl ester
  35. Uridine 5'-pyrophosphate alpha-delta-galactosyl ester
  36. Uridine diphosphate-delta-galactose
  37. Uridine pyrophosphate a-delta-galactopyranosyl ester
  38. Uridine pyrophosphate alpha-delta-galactopyranosyl ester
  39. uridine 5'-[3-(D-galactopyranosyl) dihydrogen diphosphate]
Chemical IUPAC Name [[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] hydrogen phosphate
Chemical Formula C15H24N2O17P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Galactose metabolism
  • Component of Ganglioside biosynthesis
  • Component of Globoside metabolism
  • Component of Keratan sulfate biosynthesis
  • Component of N-Glycan biosynthesis
  • Component of Nucleotide sugars metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 566.302
Monoisotopic Molecular Weight 566.054993
Isomeric SMILES OC[C@H]1O[C@H](O[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=CC(=O)NC2=O)[C@H](O)[C@@H](O)[C@H]1O
Canonical SMILES OCC1OC(OP(O)(=O)OP(O)(=O)OCC2OC(C(O)C2O)N2C=CC(=O)NC2=O)C(O)C(O)C1O
KEGG Compound ID C00052 Link Image
BioCyc ID UDP-GLACTOSE Link Image
BiGG ID 33675 Link Image
Wikipedia Link UDP-galactose Link Image
NuGOwiki Link HMDB00302 Link Image
Metagene Link HMDB00302 Link Image
METLIN ID 5291 Link Image
PubChem Compound 18068 Link Image
PubChem Substance 855022 Link Image
ChEBI ID 18307 Link Image
CAS Registry Number 2956-16-3
InChI Identifier InChI=1/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8+,9-,10+,11-,12-,13-,14-/m1/s1
Synthesis Reference Takeda, Satoshi; Noguchi, Toshitada. Enzymic manufacture of 5'-uridine diphosphate galactose (UDP-Gal) from UMP. Jpn. Kokai Tokkyo Koho (2001), 9 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 15.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -6.5 [Predicted by PubChem via XLOGP]; -1.43 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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
  • golgi apparatus
Biofluid Location Not Available
Tissue Location
Tissue References
Liver —
Most Tissues —
Platelet —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Galactose Metabolism SMP00043 Link Image map00052 Link Image
Lactose Synthesis SMP00444 Link Image
Nucleotide Sugars Metabolism SMP00010 Link Image map00520 Link Image
General References
  1. Matsukura Y: Alpha-galactosyltransferase activity in the serum of frogs (Rana catesbeiana). Z Immunitatsforsch Immunobiol. 1976 Nov;152(3):260-5. [PubMed Link Image]
  2. Ng WG, Xu YK, Kaufman FR, Donnell GN: Deficit of uridine diphosphate galactose in galactosaemia. J Inherit Metab Dis. 1989;12(3):257-66. [PubMed Link Image]
  3. Keevill NJ, Holton JB, Allen JT: UDP-glucose and UDP-galactose concentrations in cultured skin fibroblasts of patients with classical galactosaemia. J Inherit Metab Dis. 1994;17(1):23-6. [PubMed Link Image]
  4. Matsukura Y: On the blood group B gene-specified alpha-galactosyltransferase in the serum of the Japanese tortoise (Clemmys japonica). Immunology. 1976 Oct;31(4):571-5. [PubMed Link Image]
  5. Hoffmeister KM, Josefsson EC, Isaac NA, Clausen H, Hartwig JH, Stossel TP: Glycosylation restores survival of chilled blood platelets. Science. 2003 Sep 12;301(5639):1531-4. [PubMed Link Image]
  6. Holton JB: Galactose disorders: an overview. J Inherit Metab Dis. 1990;13(4):476-86. [PubMed Link Image]
  7. Segal S: Defective galactosylation in galactosemia: is low cell UDPgalactose an explanation? Eur J Pediatr. 1995;154(7 Suppl 2):S65-71. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Alpha-lactalbumin precursor
  2. Beta-1,4-galactosyltransferase 1
  3. UDP-glucose 4-epimerase
  4. Beta-1,4-galactosyltransferase 3
  5. Galactose-1-phosphate uridylyltransferase
  6. Histo-blood group ABO system transferase
  7. cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
  8. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
  9. cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a)
  10. cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
  11. cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
  12. cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 1 [top]
Enzyme 1 ID 5608
Enzyme 1 Name Alpha-lactalbumin precursor
Enzyme 1 Synonyms
  1. Lactose synthase B protein
  2. Lysozyme- like protein 7
Enzyme 1 Gene Name LALBA
Enzyme 1 Protein Sequence >Alpha-lactalbumin precursor 
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAI
VENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGI
DYWLAHKALCTEKLEQWLCEKL
Enzyme 1 Number of Residues 142
Enzyme 1 Molecular Weight 16225
Enzyme 1 Theoretical pI 4.60
Enzyme 1 GO Classification
Function
  • UDP-galactosyltransferase activity
  • UDP-glycosyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • lactose synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • disaccharide metabolism
  • lactose biosynthesis
  • lactose metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • extracellular region
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-19
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 307104 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P00709 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN Link Image
Enzyme 1 PDB ID 1HML Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >429 bp 
ATGAGGTTCTTTGTCCCTCTGTTCCTGGTGGGCATCCTGTTCCCTGCCATCCTGGCCAAG
CAATTCACAAAATGTGAGCTGTCCCAGCTGCTGAAAGACATAGATGGTTATGGAGGCATC
GCTTTGCCTGAATTGATCTGTACCATGTTTCACACCAGTGGTTATGACACACAAGCCATA
GTTGAAAACAATGAAAGCACGGAATATGGACTCTTCCAGATCAGTAATAAGCTTTGGTGC
AAGAGCAGCCAGGTCCCTCAGTCAAGGAACATCTGTGACATCTCCTGTGACAAGTTCCTG
GATGATGACATTACTGATGACATAATGTGTGCCAAGAAGATCCTGGATATTAAAGGAATT
GACTACTGGTTGGCCCATAAAGCCCTCTGCACTGAGAAGCTGGAACAGTGGCTTTGTGAG
AAGTTGTGA
Enzyme 1 GenBank Gene ID J00270 Link Image
Enzyme 1 GeneCard ID LALBA Link Image
Enzyme 1 GenAtlas ID LALBA Link Image
Enzyme 1 HGNC ID HGNC:6480 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12q13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hall L, Craig RK, Edbrooke MR, Campbell PN: Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 1982 Jun 11;10(11):3503-15. [PubMed Link Image]
  2. Hall L, Emery DC, Davies MS, Parker D, Craig RK: Organization and sequence of the human alpha-lactalbumin gene. Biochem J. 1987 Mar 15;242(3):735-42. [PubMed Link Image]
  3. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed Link Image]
  4. Acharya KR, Ren JS, Stuart DI, Phillips DC, Fenna RE: Crystal structure of human alpha-lactalbumin at 1.7 A resolution. J Mol Biol. 1991 Sep 20;221(2):571-81. [PubMed Link Image]
  5. Ren J, Stuart DI, Acharya KR: Alpha-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993 Sep 15;268(26):19292-8. [PubMed Link Image]
  6. Chandra N, Brew K, Acharya KR: Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. [PubMed Link Image]
  7. Harata K, Abe Y, Muraki M: Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method. J Mol Biol. 1999 Mar 26;287(2):347-58. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5614
Enzyme 2 Name Beta-1,4-galactosyltransferase 1
Enzyme 2 Synonyms
  1. Beta-1,4-GalTase 1
  2. Beta4Gal-T1
  3. b4Gal-T1
  4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 1
  5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 1[Includes: Lactose synthase A protein
  6. Nal synthetase
  7. Beta-N-acetylglucosaminylglycopeptide beta-1,4- galactosyltransferase
Enzyme 2 Gene Name B4GALT1
Enzyme 2 Protein Sequence >Beta-1,4-galactosyltransferase 1 
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 2 Number of Residues 398
Enzyme 2 Molecular Weight 43921
Enzyme 2 Theoretical pI 8.77
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix
Enzyme 2 Pathways
Enzyme 2 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-37
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 29424 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P15291 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name B4GT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1203 bp 
ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCGCCGCGATGCCAGGCGCGTCCCTACAGCGG
GCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTACTAC
CTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTGCAG
GGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGAGGG
GCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCCAGC
CCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCCCAC
ACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCCATG
CTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAATGTG
AAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAAGTGGCCATCATC
ATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCAGTC
CTGCAGCGCCAGCAGCTGGACTATGGCATCTATGGCATCTATGTTATCAACCAGGCGGGA
GACACTATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGAC
TATGACTACACCTGCTTTGTGTTTAGTGACGTGGACCTCATCCCAATGAATGACCATAAT
GCGTACAGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTC
AGCCTACCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTA
ACCATCAATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTT
AACAGATTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGT
CGCATGATCCGCCACTCAAGAGACAAAAAAAATGAACCCAATCCTCAGAGGTTTGACCGA
ATTGCACACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTG
CTGGATGTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGC
TAG
Enzyme 2 GenBank Gene ID X14085 Link Image
Enzyme 2 GeneCard ID B4GALT1 Link Image
Enzyme 2 GenAtlas ID B4GALT1 Link Image
Enzyme 2 HGNC ID HGNC:924 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Masri KA, Appert HE, Fukuda MN: Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). Biochem Biophys Res Commun. 1988 Dec 15;157(2):657-63. [PubMed Link Image]
  2. Watzele G, Berger EG: Near identity of HeLa cell galactosyltransferase with the human placental enzyme. Nucleic Acids Res. 1990 Dec 11;18(23):7174. [PubMed Link Image]
  3. Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC: Genomic structure and expression of human beta-1,4-galactosyltransferase. Biochem Biophys Res Commun. 1991 May 15;176(3):1269-76. [PubMed Link Image]
  4. Uejima T, Uemura M, Nozawa S, Narimatsu H: Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. Cancer Res. 1992 Nov 15;52(22):6158-63. [PubMed Link Image]
  5. Kudo T, Narimatsu H: The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. Glycobiology. 1995 Jun;5(4):397-403. [PubMed Link Image]
  6. Chatterjee SK, Mukerjee S, Tripathi PK: Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. Int J Biochem Cell Biol. 1995 Mar;27(3):329-36. [PubMed Link Image]
  7. Appert HE, Rutherford TJ, Tarr GE, Wiest JS, Thomford NR, McCorquodale DJ: Isolation of a cDNA coding for human galactosyltransferase. Biochem Biophys Res Commun. 1986 Aug 29;139(1):163-8. [PubMed Link Image]
  8. Appert HE, Rutherford TJ, Tarr GE, Thomford NR, McCorquodale DJ: Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. Biochem Biophys Res Commun. 1986 Jul 16;138(1):224-9. [PubMed Link Image]
  9. Aoki D, Appert HE, Johnson D, Wong SS, Fukuda MN: Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. EMBO J. 1990 Oct;9(10):3171-8. [PubMed Link Image]
  10. Lopez LC, Youakim A, Evans SC, Shur BD: Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. J Biol Chem. 1991 Aug 25;266(24):15984-91. [PubMed Link Image]
  11. Yamaguchi N, Fukuda MN: Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. J Biol Chem. 1995 May 19;270(20):12170-6. [PubMed Link Image]
  12. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6192
Enzyme 3 Name UDP-glucose 4-epimerase
Enzyme 3 Synonyms
  1. Galactowaldenase
  2. UDP-galactose 4-epimerase
Enzyme 3 Gene Name GALE
Enzyme 3 Protein Sequence >UDP-glucose 4-epimerase 
MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSV
EFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMK
AHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNA
VLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRD
YIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARR
EGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA
Enzyme 3 Number of Residues 348
Enzyme 3 Molecular Weight 38282
Enzyme 3 Theoretical pI 6.71
Enzyme 3 GO Classification
Function
  • NAD binding
  • UDP-glucose 4-epimerase activity
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • isomerase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
Process
  • alcohol metabolism
  • carbohydrate metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • macromolecule metabolism
  • metabolism
  • monosaccharide 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 Catalyzes two distinct but analogous reactions:the epimerization of UDP-glucose to UDP-galactose and the epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • UDP-glucose = UDP-galactose
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1119217 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q14376 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GALE_HUMAN Link Image
Enzyme 3 PDB ID 1EK6 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1047 bp 
ATGGCAGAGAAGGTGCTGGTAACAGGTGGGGCTGGCTACATTGGCAGCCACACGGTGCTG
GAGCTGCTGGAGGCTGGCTACTTGCCTGTGGTCATCGATAACTTCCATAATGCCTTCCGT
GGAGGGGGCTCCCTGCCTGAGAGCCTGCGGCGGGTCCAGGAGCTGACAGGCCGCTCTGTG
GAGTTTGAGGAGATGGACATTTTGGACCAGGGAGCCCTACAGCGTCTCTTCAAAAAGTAC
AGCTTTATGGCGGTCATCCACTTTGCGGGGCTCAAGGCCGTGGGCGAGTCGGTGCAGAAG
CCTCTGGATTATTACAGAGTTAACCTGACCGGGACCATCCAGCTTCTGGAGATCATGAAG
GCCCACGGGGTGAAGAACCTGGTGTTCAGCAGCTCAGCCACTGTGTACGGGAACCCCCAG
TACCTGCCCCTTGATGAGGCCCACCCCACGGGTGGTTGTACCAACCCTTACGGCAAGTCC
AAGTTCTTCATCGAGGAAATGATCCGGGACCTGTGCCAGGCAGACAAGACTTGGAACGTA
GTGCTGCTGCGCTATTTCAACCCCACAGGTGCCCATGCCTCTGGCTGCATTGGTGAGGAT
CCCCAGGGCATACCCAACAACCTCATGCCTTATGTCTCCCAGGTGGCGATCGGGCGACGG
GAGGCCCTGAATGTCTTTGGCAATGACTATGACACAGAGGATGGCACAGGTGTCCGGGAT
TACATCCATGTCGTGGATCTGGCCAAGGGCCACATTGCAGCCTTAAGGAAGCTGAAAGAA
CAGTGTGGCTGCCGGATCTACAACCTGGGCACGGGCACAGGCTATTCAGTGCTGCAGATG
GTCCAGGCTATGGAGAAGGCCTCTGGGAAGAAGATCCCGTACAAGGTGGTGGCACGGCGG
GAAGGTGATGTGGCAGCCTGTTACGCCAACCCCAGCCTGGCCCAAGAGGAGCTGGGGTGG
ACAGCAGCCTTAGGGCTGGACAGGATGTGTGAGGATCTCTGGCGCTGGCAGAAGCAGAAT
CCTTCAGGCTTTGGCACGCAAGCCTGA
Enzyme 3 GenBank Gene ID L41668 Link Image
Enzyme 3 GeneCard ID GALE Link Image
Enzyme 3 GenAtlas ID GALE Link Image
Enzyme 3 HGNC ID HGNC:4116 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p36-p35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Daude N, Gallaher TK, Zeschnigk M, Starzinski-Powitz A, Petry KG, Haworth IS, Reichardt JK: Molecular cloning, characterization, and mapping of a full-length cDNA encoding human UDP-galactose 4'-epimerase. Biochem Mol Med. 1995 Oct;56(1):1-7. [PubMed Link Image]
  2. Maceratesi P, Daude N, Dallapiccola B, Novelli G, Allen R, Okano Y, Reichardt J: Human UDP-galactose 4' epimerase (GALE) gene and identification of five missense mutations in patients with epimerase-deficiency galactosemia. Mol Genet Metab. 1998 Jan;63(1):26-30. [PubMed Link Image]
  3. Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM: Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry. 2000 May 16;39(19):5691-701. [PubMed Link Image]
  4. Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM: Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase. J Biol Chem. 2001 Jun 8;276(23):20617-23. Epub 2001 Mar 7. [PubMed Link Image]
  5. Quimby BB, Alano A, Almashanu S, DeSandro AM, Cowan TM, Fridovich-Keil JL: Characterization of two mutations associated with epimerase-deficiency galactosemia, by use of a yeast expression system for human UDP-galactose-4-epimerase. Am J Hum Genet. 1997 Sep;61(3):590-8. [PubMed Link Image]
  6. Wohlers TM, Christacos NC, Harreman MT, Fridovich-Keil JL: Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia. Am J Hum Genet. 1999 Feb;64(2):462-70. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6320
Enzyme 4 Name Beta-1,4-galactosyltransferase 3
Enzyme 4 Synonyms
  1. Beta-1,4-GalTase 3
  2. Beta4Gal-T3
  3. b4Gal-T3
  4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 3
  5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 3[Includes: N-acetyllactosamine synthase
  6. Nal synthetase
  7. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
Enzyme 4 Gene Name B4GALT3
Enzyme 4 Protein Sequence >Beta-1,4-galactosyltransferase 3 
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSH
LPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCE
PRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVR
EALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSAL
TPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEEN
PHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPG
SSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
Enzyme 4 Number of Residues 393
Enzyme 4 Molecular Weight 43929
Enzyme 4 Theoretical pI 9.45
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids
Enzyme 4 Pathways
Enzyme 4 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-36
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2982510 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O60512 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B4GT3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1182 bp 
ATGTTGCGGAGGCTGCTGGAGCGGCCTTGCACGCTGGCCCTGCTTGTGGGCTCCCAGCTG
GCTGTCATGATGTACCTGTCACTGGGGGGCTTCCGAAGTCTCAGTGCCCTATTTGGCCGA
GATCAGGGACCGACATTTGACTATTCTCACCCTCGTGATGTCTACAGTAACCTCAGTCAC
CTGCCTGGGGCCCCAGGGGGTCCTCCAGCTCCTCAAGGTCTGCCCTACTGTCCAGAACGA
TCTCCTCTCTTAGTGGGTCCTGTGTCGGTGTCCTTTAGCCCAGTGCCATCACTGGCAGAG
ATTGTGGAGCGGAATCCCCGGGTAGAACCAGGGGGCCGGTACCGCCCTGCAGGTTGTGAG
CCCCGCTCCCGAACAGCCATCATTGTGCCTCATCGTGCCCGGGAGCACCACCTGCGCCTG
CTGCTCTACCACCTGCACCCCTTCTTGCAGCGCCAGCAGCTTGCTTATGGCATCTATGTC
ATCCACCAGGCTGGAAATGGAACATTTAACAGGGCAAAACTGTTGAACGTTGGGGTGCGA
GAGGCCCTGCGTGATGAAGAGTGGGACTGCCTGTTCTTGCACGATGTGGACCTCTTGCCA
GAAAATGACCACAATCTGTATGTGTGTGACCCCCGGGGACCCCGCCATGTTGCCGTTGCT
ATGAACAAGTTTGGATACAGCCTCCCGTACCCCCAGTACTTCGGAGGAGTCTCAGCACTT
ACTCCTGACCAGTACCTGAAGATGAATGGCTTCCCCAATGAATACTGGGGCTGGGGTGGT
GAGGATGACGACATTGCTACCAGGGTGCGCCTGGCTGGGATGAAGATCTCTCGGCCCCCC
ACATCTGTAGGACACTATAAGATGGTGAAGCACCGAGGAGATAAGGGCAATGAGGAAAAT
CCCCACAGATTTGACCTCCTGGTCCGTACCCAGAATTCCTGGACGCAAGATGGGATGAAC
TCACTGACATACCAGTTGCTGGCTCGAGAGCTGGGGCCTCTTTATACCAACATCACAGCA
GACATTGGGACTGACCCTCGGGGTCCTCGGGCTCCTTCTGGGCCACGTTACCCACCTGGT
TCCTCCCAAGCCTTCCGTCAAGAGATGCTGCAACGCCGGCCCCCAGCCAGGCCTGGGCCT
CTATCTACTGCCAACCACACAGCCCTCCGAGGTTCACACTGA
Enzyme 4 GenBank Gene ID Y12509 Link Image
Enzyme 4 GeneCard ID B4GALT3 Link Image
Enzyme 4 GenAtlas ID B4GALT3 Link Image
Enzyme 4 HGNC ID HGNC:926 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q21-q23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H: A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3. J Biol Chem. 1997 Dec 19;272(51):31979-91. [PubMed Link Image]
  2. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed Link Image]
  3. Guo S, Sato T, Shirane K, Furukawa K: Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells. Glycobiology. 2001 Oct;11(10):813-20. [PubMed Link Image]
  4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6381
Enzyme 5 Name Galactose-1-phosphate uridylyltransferase
Enzyme 5 Synonyms
  1. Gal-1-P uridylyltransferase
  2. UDP-glucose--hexose-1-phosphate uridylyltransferase
Enzyme 5 Gene Name GALT
Enzyme 5 Protein Sequence >Galactose-1-phosphate uridylyltransferase 
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQ
LLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAK
SARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC
SNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWL
VLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGW
HGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA
LPEVHYHLGQKDRETATIA
Enzyme 5 Number of Residues 379
Enzyme 5 Molecular Weight 43364
Enzyme 5 Theoretical pI 6.99
Enzyme 5 GO Classification
Function
  • UDP-glucose:hexose-1-phosphate uridylyltransferase activity
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose
Enzyme 5 Pathways
Enzyme 5 Reactions
  • UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDPgalactose
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 182951 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P07902 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GALT_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1140 bp 
ATGTCGCGCAGTGGAACCGATCCTCAGCAACGCCAGCAGGCGTCAGAGGCGGACGCCGCA
GCAGCAACCTTCCGGGCAAACGACCATCAGCATATCCGCTACAACCCGCTGCAGGATGAG
TGGGTGCTGGTGTCAGCTCACCGCATGAAGCGGCCCTGGCAGGGTCAAGTGGAGCCCCAG
CTTCTGAAGACAGTGCCCCGCCATGACCCTCTCAACCCTCTGTGTCCTGGGGCCATCCGA
GCCAACGGAGAGGTGAATCCCCAGTACGATAGCACCTTCCTGTTTGACAACGACTTCCCA
GCTCTGCAGCCTGATGCCCCCAGTCCAGGACCCAGTGATCATCCCCTTTTCCAAGCAAAG
TCTGCTCGAGGAGTCTGTAAGGTCATGTGCTTCCACCCCTGGTCGGATGTAACGCTGCCA
CTCATGTCGGTCCCTGAGATCCGGGCTGTTGTTGATGCATGGGCCTCAGTCACAGAGGAG
CTGGGTGCCCAGTACCCTTGGGTGCAGATCTTTGAAAACAAAGGTGCCATGATGGGCTGT
TCTAACCCCCACCCCCACTGCCAGGTATGGGCCAGCAGTTTCCTGCCAGATATTGCCCAG
CGTGAGGAGCGATCTCAGCAGGCCTATAAGAGTCAGCATGGAGAGCCCCTGCTAATGGAG
TACAGCCGCCAGGAGCTACTCAGGAAGGAACGTCTGGTCCTAACCAGTGAGCACTGGTTA
GTACTGGTCCCCTTCTGGGCAACATGGCCCTACCAGACACTGCTGCTGCCCGTCGGCCAT
GTGCGGCGGCTACCTGAGCTGACCCCTGCTGAGCGTGATGATCTAGCCTCCATCATGAAG
AAGCTCTTGACCAAGTATGACAACCTCTTTGAGACGTCCTTTCCCTACTCCATGGGCTGG
CATGGGGCTCCCACAGGATCAGAGGCTGGGGCCAACTGGAACCATTGGCAGCTGCACGCT
CATTACTACCCTCCGCTCCTGCGCTCTGCCACTGTCCGGAAATTCATGGTTGGCTACGAA
ATGCTTGCTCAGGCTCAGAGGGACCTCACCCCTGAGCAGGCTGCAGAGAGACTAAGGGCA
CTTCCTGAGGTTCATTACCACCTGGGGCAGAAGGACAGGGAGACAGCAACCATCGCCTGA
Enzyme 5 GenBank Gene ID M60091 Link Image
Enzyme 5 GeneCard ID GALT Link Image
Enzyme 5 GenAtlas ID GALT Link Image
Enzyme 5 HGNC ID HGNC:4135 Link Image
Enzyme 5 Chromosome Location 9
Enzyme 5 Locus 9p13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Reichardt JK, Berg P: Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol Biol Med. 1988 Apr;5(2):107-22. [PubMed Link Image]
  2. Flach JE, Reichardt JK, Elsas LJ 2nd: Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol Biol Med. 1990 Aug;7(4):365-9. [PubMed Link Image]
  3. Leslie ND, Immerman EB, Flach JE, Florez M, Fridovich-Keil JL, Elsas LJ: The human galactose-1-phosphate uridyltransferase gene. Genomics. 1992 Oct;14(2):474-80. [PubMed Link Image]
  4. Reichardt JK: Genetic basis of galactosemia. Hum Mutat. 1992;1(3):190-6. [PubMed Link Image]
  5. Tyfield L, Reichardt J, Fridovich-Keil J, Croke DT, Elsas LJ 2nd, Strobl W, Kozak L, Coskun T, Novelli G, Okano Y, Zekanowski C, Shin Y, Boleda MD: Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene. Hum Mutat. 1999;13(6):417-30. [PubMed Link Image]
  6. Reichardt JK, Packman S, Woo SL: Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase. Am J Hum Genet. 1991 Oct;49(4):860-7. [PubMed Link Image]
  7. Reichardt JK, Woo SL: Molecular basis of galactosemia: mutations and polymorphisms in the gene encoding human galactose-1-phosphate uridylyltransferase. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2633-7. [PubMed Link Image]
  8. Reichardt JK, Levy HL, Woo SL: Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. Biochemistry. 1992 Jun 23;31(24):5430-3. [PubMed Link Image]
  9. Reichardt JK, Belmont JW, Levy HL, Woo SL: Characterization of two missense mutations in human galactose-1-phosphate uridyltransferase: different molecular mechanisms for galactosemia. Genomics. 1992 Mar;12(3):596-600. [PubMed Link Image]
  10. Reichardt JK, Novelli G, Dallapiccola B: Molecular characterization of the H319Q galactosemia mutation. Hum Mol Genet. 1993 Mar;2(3):325-6. [PubMed Link Image]
  11. Lin HC, Kirby LT, Ng WG, Reichardt JK: On the molecular nature of the Duarte variant of galactose-1-phosphate uridyl transferase (GALT). Hum Genet. 1994 Feb;93(2):167-9. [PubMed Link Image]
  12. Elsas LJ, Langley S, Steele E, Evinger J, Fridovich-Keil JL, Brown A, Singh R, Fernhoff P, Hjelm LN, Dembure PP: Galactosemia: a strategy to identify new biochemical phenotypes and molecular genotypes. Am J Hum Genet. 1995 Mar;56(3):630-9. [PubMed Link Image]
  13. Fridovich-Keil JL, Langley SD, Mazur LA, Lennon JC, Dembure PP, Elsas JL 2nd: Identification and functional analysis of three distinct mutations in the human galactose-1-phosphate uridyltransferase gene associated with galactosemia in a single family. Am J Hum Genet. 1995 Mar;56(3):640-6. [PubMed Link Image]
  14. Sommer M, Gathof BS, Podskarbi T, Giugliani R, Kleinlein B, Shin YS: Mutations in the galactose-1-phosphate uridyltransferase gene of two families with mild galactosaemia variants. J Inherit Metab Dis. 1995;18(5):567-76. [PubMed Link Image]
  15. Ashino J, Okano Y, Suyama I, Yamazaki T, Yoshino M, Furuyama J, Lin HC, Reichardt JK, Isshiki G: Molecular characterization of galactosemia (type 1) mutations in Japanese. Hum Mutat. 1995;6(1):36-43. [PubMed Link Image]
  16. Shin YS, Gathof BS, Podskarbi T, Sommer M, Giugliani R, Gresser U: Three missense mutations in the galactose-1-phosphate uridyltransferase gene of three families with mild galactosaemia. Eur J Pediatr. 1996 May;155(5):393-7. [PubMed Link Image]
  17. Maceratesi P, Sangiuolo F, Novelli G, Ninfali P, Magnani M, Reichardt JK, Dallapiccola B: Three new mutations (P183T, V150L, 528insG) and eleven sequence polymorphisms in Italian patients with galactose-1-phosphate uridyltransferase (GALT) deficiency. Hum Mutat. 1996;8(4):369-72. [PubMed Link Image]
  18. Ninfali P, Bresolin N, Dallapiccola B, Novelli G: Molecular basis of galactose-1-phosphate uridyltransferase deficiency involving skeletal muscle. J Neurol. 1996 Jan;243(1):102-3. [PubMed Link Image]
  19. Greber-Platzer S, Guldberg P, Scheibenreiter S, Item C, Schuller E, Patel N, Strobl W: Molecular heterogeneity of classical and Duarte galactosemia: mutation analysis by denaturing gradient gel electrophoresis. Hum Mutat. 1997;10(1):49-57. [PubMed Link Image]
  20. Seyrantepe V, Ozguc M, Coskun T, Ozalp I, Reichardt JK: Identification of mutations in the galactose-1-phosphate uridyltransferase (GALT) gene in 16 Turkish patients with galactosemia, including a novel mutation of F294Y. Mutation in brief no. 235. Online. Hum Mutat. 1999;13(4):339. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6389
Enzyme 6 Name Histo-blood group ABO system transferase
Enzyme 6 Synonyms
  1. NAGAT[Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase
  2. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
  3. Histo-blood group A transferase
  4. A transferase
  5. Glycoprotein-fucosylgalactoside alpha- galactosyltransferase
  6. Fucosylglycoprotein 3-alpha- galactosyltransferase
  7. Histo-blood group B transferase
  8. B transferase] [Contains: Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase
  9. Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase soluble form]
Enzyme 6 Gene Name ABO
Enzyme 6 Protein Sequence >Histo-blood group ABO system transferase 
MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH
LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV
FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR
WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS
REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW
HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
Enzyme 6 Number of Residues 354
Enzyme 6 Molecular Weight 40934
Enzyme 6 Theoretical pI 9.24
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens:A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity
Enzyme 6 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 6 Reactions
  • UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-35
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 340078 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P16442 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name BGAT_HUMAN Link Image
Enzyme 6 PDB ID 1LZI Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1062 bp 
ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG
ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA
AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT
CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGG
AAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTCAAC
ATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTGTTT
GCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCACTTC
ATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCTGGCCGCGGTGCCCCGC
GTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGCTGG
CAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTCCTC
AGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTGGGC
GTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGCCGG
GAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAGGGC
GATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTCACC
AGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGGCAC
GACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCCCCC
GAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGGTTC
ACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA
Enzyme 6 GenBank Gene ID J05175 Link Image
Enzyme 6 GeneCard ID ABO Link Image
Enzyme 6 GenAtlas ID ABO Link Image
Enzyme 6 HGNC ID HGNC:79 Link Image
Enzyme 6 Chromosome Location 9
Enzyme 6 Locus 9q34.1-q34.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Yamamoto F, Marken J, Tsuji T, White T, Clausen H, Hakomori S: Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1----2Gal alpha 1----3GalNAc transferase (histo-blood group A transferase) mRNA. J Biol Chem. 1990 Jan 15;265(2):1146-51. [PubMed Link Image]
  2. Yamamoto F, Clausen H, White T, Marken J, Hakomori S: Molecular genetic basis of the histo-blood group ABO system. Nature. 1990 May 17;345(6272):229-33. [PubMed Link Image]
  3. Bennett EP, Steffensen R, Clausen H, Weghuis DO, van Kessel AG: Genomic cloning of the human histo-blood group ABO locus. Biochem Biophys Res Commun. 1995 Jan 5;206(1):318-25. [PubMed Link Image]
  4. Bennett EP, Steffensen R, Clausen H, Weghuis DO, Geurts van Kessel A: Genomic cloning of the human histo-blood group ABO locus. Biochem Biophys Res Commun. 1995 Jun 6;211(1):347. [PubMed Link Image]
  5. Olsson ML, Chester MA: Heterogeneity of the blood group Ax allele: genetic recombination of common alleles can result in the Ax phenotype. Transfus Med. 1998 Sep;8(3):231-8. [PubMed Link Image]
  6. Kominato Y, McNeill PD, Yamamoto M, Russell M, Hakomori S, Yamamoto F: Animal histo-blood group ABO genes. Biochem Biophys Res Commun. 1992 Nov 30;189(1):154-64. [PubMed Link Image]
  7. Yamamoto F, Hakomori S: Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions. J Biol Chem. 1990 Nov 5;265(31):19257-62. [PubMed Link Image]
  8. Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV: The structural basis for specificity in human ABO(H) blood group biosynthesis. Nat Struct Biol. 2002 Sep;9(9):685-90. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16488
Enzyme 7 Name cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name B4GALT1
Enzyme 7 Protein Sequence >cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a) 
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 7 Number of Residues 398
Enzyme 7 Molecular Weight 43921
Enzyme 7 Theoretical pI 8.77
Enzyme 7 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
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 B2R710 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2R710_HUMAN Link Image
Enzyme 7 PDB ID 1FR8 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK312797 Link Image
Enzyme 7 GeneCard ID B2R710 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 16489
Enzyme 8 Name cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
Enzyme 8 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 2, isoform CRA_a
Enzyme 8 Gene Name B4GALT2
Enzyme 8 Protein Sequence >cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-) 
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG
Enzyme 8 Number of Residues 372
Enzyme 8 Molecular Weight 41973
Enzyme 8 Theoretical pI 9.66
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
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
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 B3KTP0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B3KTP0_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 AK095873 Link Image
Enzyme 8 GeneCard ID B3KTP0 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
Enzyme 9 [top]
Enzyme 9 ID 16517
Enzyme 9 Name cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name B4GALT4
Enzyme 9 Protein Sequence >cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a) 
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKG
KTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKA
LQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLE
ALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSR
EQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAE
RMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA
Enzyme 9 Number of Residues 344
Enzyme 9 Molecular Weight 40042
Enzyme 9 Theoretical pI 9.42
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Not Available
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 B2RAZ5 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2RAZ5_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 AK314425 Link Image
Enzyme 9 GeneCard ID B2RAZ5 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 16552
Enzyme 10 Name cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
Enzyme 10 Synonyms
  1. SubName: UDP glycosyltransferase 8 (UDP-galactose ceramide galactosyltransferase)
Enzyme 10 Gene Name UGT8
Enzyme 10 Protein Sequence >cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45) 
MKSYTPYFILLWSAVGIAKAAKIIIVPPIMFESHMYIFKTLASALHERGHHTVFLLSEGR
DIAPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAIELFDILDHYTKNCDLMVGN
HALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEF
NSLLTDRMNLLQRMKNTGVYLISRLGVSFLVLPKYERIMQKYNLLPEKSMYDLVHGSSLW
MLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVNGANEHGFVLVSFGAGVKYL
SEDIANKLAGALGRLPQKVIWRFSGPKPKNLGNNTKLIEWLPQNDLLGHSKIKAFLSHGG
LNSIFETMYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWKTVTEKELYEALVKVINNP
SYRQRAQKLSEIHKDQPGHPVNRTIYWIDYIIRHNGAHHLRAAVHQISFCQYFLLDIAFV
LLLGAALLYFLLSWVTKFIYRKIKSLWSRNKHSTVNGHYHNGILNGKYKRNGHIKHEKKV
K
Enzyme 10 Number of Residues 541
Enzyme 10 Molecular Weight 61457
Enzyme 10 Theoretical pI 9.97
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322] ALL_REAC R04322
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID B3KXU7 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B3KXU7_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 AK127970 Link Image
Enzyme 10 GeneCard ID B3KXU7 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16553
Enzyme 11 Name cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name Not Available
Enzyme 11 Protein Sequence >cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62) 
MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPN
QEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPV
WGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYV
NVPELVSELVLRGGRWGQWEGSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTP
GGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARR
GGLAPTQCVKLAGATHYPLDRCCYGKFLLTSHRLDPWKMQEAWKLVGGSDGERTAPFCSW
FQGVLGILRCRAIAWLQS
Enzyme 11 Number of Residues 378
Enzyme 11 Molecular Weight 41438
Enzyme 11 Theoretical pI 8.22
Enzyme 11 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • hormone activity
  • receptor binding
  • signal transducer 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
  • extracellular region
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • UDP-galactose + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-1,4- beta-D-glucosyl-N-acylsphingosine = UDP + D-galactosyl-1,3-beta-N-acetyl-D-galactosaminyl-(N- acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine [RN:R04631 R05941] ALL_REAC R04631 R05941(G)
  • (other) R05110 R05111 R05948(G) R05953(G) R05956(G)
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B3KQP5 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B3KQP5_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK075312 Link Image
Enzyme 11 GeneCard ID B3KQP5 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs Not Available
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16555
Enzyme 12 Name cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name A4GALT
Enzyme 12 Protein Sequence >cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase) 
MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIP
CPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGG
NASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRI
ALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDH
YNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDIN
PEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL
Enzyme 12 Number of Residues 353
Enzyme 12 Molecular Weight 40500
Enzyme 12 Theoretical pI 9.18
Enzyme 12 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
—
Component
  • Golgi apparatus
  • Golgi stack
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID B2R7C4 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B2R7C4_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK312927 Link Image
Enzyme 12 GeneCard ID B2R7C4 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location 22
Enzyme 12 Locus 22q11.2-q13.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available