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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 2011-06-03 12:49:27
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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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. Beta-1,4-galactosyltransferase 2
  2. Alpha-lactalbumin
  3. Beta-1,4-galactosyltransferase 1
  4. Lactosylceramide 4-alpha-galactosyltransferase
  5. UDP-glucose 4-epimerase
  6. Beta-1,4-galactosyltransferase 3
  7. Galactose-1-phosphate uridylyltransferase
  8. Histo-blood group ABO system transferase
  9. 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
  10. 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)
  11. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
  12. UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
  13. cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
  14. cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
  15. cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 1 [top]
Enzyme 1 ID 5607
Enzyme 1 Name Beta-1,4-galactosyltransferase 2
Enzyme 1 Synonyms
  1. Beta-1,4-GalTase 2
  2. Beta4Gal-T2
  3. b4Gal-T2
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2
  6. Lactose synthase A protein
  7. N-acetyllactosamine synthase
  8. Nal synthase
  9. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  10. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Enzyme 1 Gene Name B4GALT2
Enzyme 1 Protein Sequence >Beta-1,4-galactosyltransferase 2
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG
Enzyme 1 Number of Residues 372
Enzyme 1 Molecular Weight 41971.8
Enzyme 1 Theoretical pI 9.66
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 1 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 1 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose
Enzyme 1 Pathways
Enzyme 1 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 16-36
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4520136 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O60909 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name B4GT2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1119 bp
ATGAGCAGACTGCTGGGGGGGACGCTGGAGCGCGTCTGCAAGGCTGTGCTCCTTCTCTGC
CTGCTGCACTTCCTCGTGGCCGTCATCCTCTACTTTGACGTCTACGCCCAGCACCTGGCC
TTCTTCAGCCGCTTCAGTGCCCGAGGCCCTGCCCATGCCCTCCACCCAGCTGCTAGCAGC
AGCAGCAGCAGCAGCAACTGCTCCCGGCCCAACGCCACCGCCTCTAGCTCCGGGCTCCCT
GAGGTCCCCAGTGCCCTGCCCGGTCCCACGGCTCCCACGCTGCCACCCTGTCCTGACTCG
CCACCTGGTCTTGTGGGCAGACTGCTGATCGAGTTCACCTCACCCATGCCCCTGGAGCGG
GTGCAGAGGGAGAACCCAGGCGTGCTCATGGGCGGCCGATACACACCGCCCGACTGCACC
CCAGCCCAGACGGTGGCGGTCATCATCCCCTTTAGACACCGGGAACACCACCTGCGCTAC
TGGCTCCACTATCTACACCCCATCTTGAGGCGGCAGCGGCTGCGCTACGGCGTCTATGTC
ATCAACCAGCATGGTGAGGACACCTTCAACCGGGCCAAGCTGCTTAACGTGGGCTTCCTA
GAGGCGCTGAAGGAGGATGCCGCCTATGACTGCTTCATCTTCAGCGATGTGGACCTGGTC
CCCATGGATGACCGCAACCTATACCGCTGCGGCGACCAACCCCGCCACTTTGCCATTGCC
ATGGACAAGTTTGGCTTCCGGCTTCCCTATGCTGGCTACTTTGGAGGTGTGTCAGGCCTG
AGTAAGGCTCAGTTTCTGAGAATCAATGGCTTCCCCAATGAGTACTGGGGCTGGGGTGGC
GAGGATGATGACATCTTCAACCGGATCTCCCTGACTGGGATGAAGATCTCACGCCCAGAC
ATCCGAATTGGCCGCTACCGCATGATCAAGCACGACCGCGACAAGCATAACGAACCTAAC
CCTCAGAGGTTTACCAAGATTCAAAACACGAAGCTGACCATGAAGCGGGACGGCATTGGG
TCAGTGCGGTACCAGGTCTTGGAGGTGTCTCGGCAACCACTCTTCACCAATATCACAGTG
GACATTGGGCGGCCTCCGTCGTGGCCCCCTCGGGGCTGA
Enzyme 1 GenBank Gene ID AB024434 Link Image
Enzyme 1 GeneCard ID B4GALT2 Link Image
Enzyme 1 GenAtlas ID B4GALT2 Link Image
Enzyme 1 HGNC ID HGNC:925 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p34-p33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5608
Enzyme 2 Name Alpha-lactalbumin
Enzyme 2 Synonyms
  1. Lactose synthase B protein
  2. Lysozyme-like protein 7
Enzyme 2 Gene Name LALBA
Enzyme 2 Protein Sequence >Alpha-lactalbumin
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAI
VENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGI
DYWLAHKALCTEKLEQWLCEKL
Enzyme 2 Number of Residues 142
Enzyme 2 Molecular Weight 16224.7
Enzyme 2 Theoretical pI 4.60
Enzyme 2 GO Classification
Function
  • UDP-galactosyltransferase activity
  • UDP-glycosyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • lactose synthase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • disaccharide metabolic process
  • lactose biosynthetic process
  • lactose metabolic process
  • metabolic process
  • oligosaccharide metabolic process
  • primary metabolic process
Component
Enzyme 2 General Function Involved in lactose synthase activity
Enzyme 2 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 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-19
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 307104 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00709 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN Link Image
Enzyme 2 PDB ID 1HML Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >429 bp
ATGAGGTTCTTTGTCCCTCTGTTCCTGGTGGGCATCCTGTTCCCTGCCATCCTGGCCAAG
CAATTCACAAAATGTGAGCTGTCCCAGCTGCTGAAAGACATAGATGGTTATGGAGGCATC
GCTTTGCCTGAATTGATCTGTACCATGTTTCACACCAGTGGTTATGACACACAAGCCATA
GTTGAAAACAATGAAAGCACGGAATATGGACTCTTCCAGATCAGTAATAAGCTTTGGTGC
AAGAGCAGCCAGGTCCCTCAGTCAAGGAACATCTGTGACATCTCCTGTGACAAGTTCCTG
GATGATGACATTACTGATGACATAATGTGTGCCAAGAAGATCCTGGATATTAAAGGAATT
GACTACTGGTTGGCCCATAAAGCCCTCTGCACTGAGAAGCTGGAACAGTGGCTTTGTGAG
AAGTTGTGA
Enzyme 2 GenBank Gene ID J00270 Link Image
Enzyme 2 GeneCard ID LALBA Link Image
Enzyme 2 GenAtlas ID LALBA Link Image
Enzyme 2 HGNC ID HGNC:6480 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 12q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed Link Image]
  5. Maynard F: Identification of a new molecular form of human alpha-lactalbumin. J Dairy Res. 1992 Aug;59(3):425-9. [PubMed Link Image]
  6. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. Chowanadisai W, Kelleher SL, Nemeth JF, Yachetti S, Kuhlman CF, Jackson JG, Davis AM, Lien EL, Lonnerdal B: Detection of a single nucleotide polymorphism in the human alpha-lactalbumin gene: implications for human milk proteins. J Nutr Biochem. 2005 May;16(5):272-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5614
Enzyme 3 Name Beta-1,4-galactosyltransferase 1
Enzyme 3 Synonyms
  1. Beta-1,4-GalTase 1
  2. Beta4Gal-T1
  3. b4Gal-T1
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
  6. Lactose synthase A protein
  7. N-acetyllactosamine synthase
  8. Nal synthase
  9. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  10. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
  11. Processed beta-1,4-galactosyltransferase 1
Enzyme 3 Gene Name B4GALT1
Enzyme 3 Protein Sequence >Beta-1,4-galactosyltransferase 1
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 3 Number of Residues 398
Enzyme 3 Molecular Weight 43919.9
Enzyme 3 Theoretical pI 8.77
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 3 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 25-44
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 189053491 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P15291 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B4GT1_HUMAN Link Image
Enzyme 3 PDB ID 1FR8 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1197 bp
ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCAGCGCCGCGATGCCAGGCGCGTCCCTACAG
CGGGCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTAC
TACCTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTG
CAGGGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGA
GGGGCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCC
AGCCCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCC
CACACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCC
ATGCTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAAT
GTGAAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAGGTGGCCATC
ATCATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCA
GTCCTGCAGCGCCAGCAGCTGGACTATGGCATCTATGTTATCAACCAGGCGGGAGACACT
ATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGACTATGAC
TACACCTGCTTTGTGTTTAGCGACGTGGACCTCATTCCAATGAATGACCATAATGCGTAC
AGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTCAGCCTA
CCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTAACCATC
AATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTTAACAGA
TTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGTCGCATG
ATCCGCCACTCAAGAGACAAGAAAAATGAACCCAATCCTCAGAGGTTTGACCGAATTGCA
CACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTGCTGGAT
GTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGCTAG
Enzyme 3 GenBank Gene ID AK312797 Link Image
Enzyme 3 GeneCard ID B4GALT1 Link Image
Enzyme 3 GenAtlas ID B4GALT1 Link Image
Enzyme 3 HGNC ID HGNC:924 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6156
Enzyme 4 Name Lactosylceramide 4-alpha-galactosyltransferase
Enzyme 4 Synonyms
  1. Alpha-1,4-N-acetylglucosaminyltransferase
  2. Alpha-1,4-galactosyltransferase
  3. Alpha4Gal-T1
  4. CD77 synthase
  5. Globotriaosylceramide synthase
  6. Gb3 synthase
  7. P1/Pk synthase
  8. UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase
Enzyme 4 Gene Name A4GALT
Enzyme 4 Protein Sequence >Lactosylceramide 4-alpha-galactosyltransferase
MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIP
CPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGG
NASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRI
ALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDH
YNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDIN
PEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL
Enzyme 4 Number of Residues 353
Enzyme 4 Molecular Weight 40498.8
Enzyme 4 Theoretical pI 9.18
Enzyme 4 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi apparatus part
  • Golgi stack
  • cell part
  • cytoplasmic part
  • intracellular part
Enzyme 4 General Function Involved in galactosyltransferase activity
Enzyme 4 Specific Function Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins
Enzyme 4 Pathways
Enzyme 4 Reactions
  • UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosyl-(11)-ceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosyl-(11)- ceramide [RN:R03486 R05960]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 23-43
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPC4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A4GAT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1062 bp
ATGTCCAAGCCCCCCGACCTCCTGCTGCGGCTGCTCCGGGGCGCCCCAAGGCAGCGGGTC
TGCACCCTGTTCATCATCGGCTTCAAGTTCACGTTTTTCGTCTCCATCATGATCTACTGG
CACGTTGTGGGAGAGCCCAAGGAGAAAGGGCAGCTCTATAACCTGCCAGCAGAGATCCCC
TGCCCCACCTTGACACCCCCCACCCCACCCTCCCACGGCCCCACTCCAGGCAACATCTTC
TTCCTGGAGACTTCAGACCGGACCAACCCCAACTTCCTGTTCATGTGCTCGGTGGAGTCG
GCCGCCAGAACTCACCCCGAATCCCACGTGCTGGTCCTGATGAAAGGGCTTCCGGGTGGC
AACGCCTCTCTGCCCCGGCACCTGGGCATCTCACTTCTGAGCTGCTTCCCGAATGTCCAG
ATGCTCCCGCTGGACCTGCGGGAGCTGTTCCGGGACACACCCCTGGCCGACTGGTACGCG
GCCGTGCAGGGGCGCTGGGAGCCCTACCTGCTGCCCGTGCTCTCCGACGCCTCCAGGATC
GCACTCATGTGGAAGTTCGGCGGCATCTACCTGGACACGGACTTCATTGTTCTCAAGAAC
CTGCGGAACCTGACCAACGTGCTGGGCACCCAGTCCCGCTACGTCCTCAACGGCGCGTTC
CTGGCCTTCGAGCGCCGGCACGAGTTCATGGCGCTGTGCATGCGGGACTTCGTGGACCAC
TACAACGGCTGGATCTGGGGTCACCAGGGCCCGCAGCTGCTCACGCGGGTCTTCAAGAAG
TGGTGTTCCATCCGCAGCCTGGCCGAGAGCCGCGCCTGCCGCGGCGTCACCACCCTGCCC
CCTGAGGCCTTCTACCCCATCCCCTGGCAGGACTGGAAGAAGTACTTTGAGGACATCAAC
CCGGAGGAGCTGCCGCGGCTGCTCAGTGCCACCTATGCTGTCCACGTGTGGAACAAGAAG
AGCCAGGGCACGCGGTTCGAGGCCACGTCCAGGGCACTGCTGGCCCAGCTGCATGCCCGC
TACTGCCCCACGACGCACGAGGCCATGAAAATGTACTTGTGA
Enzyme 4 GenBank Gene ID AB037883 Link Image
Enzyme 4 GeneCard ID A4GALT Link Image
Enzyme 4 GenAtlas ID A4GALT Link Image
Enzyme 4 HGNC ID HGNC:18149 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 22q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kojima Y, Fukumoto S, Furukawa K, Okajima T, Wiels J, Yokoyama K, Suzuki Y, Urano T, Ohta M, Furukawa K: Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J Biol Chem. 2000 May 19;275(20):15152-6. [PubMed Link Image]
  2. Steffensen R, Carlier K, Wiels J, Levery SB, Stroud M, Cedergren B, Nilsson Sojka B, Bennett EP, Jersild C, Clausen H: Cloning and expression of the histo-blood group Pk UDP-galactose: Ga1beta-4G1cbeta1-cer alpha1, 4-galactosyltransferase. Molecular genetic basis of the p phenotype. J Biol Chem. 2000 Jun 2;275(22):16723-9. [PubMed Link Image]
  3. Kitano T, Liu YH, Ueda S, Saitou N: Human-specific amino acid changes found in 103 protein-coding genes. Mol Biol Evol. 2004 May;21(5):936-44. Epub 2004 Mar 10. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Furukawa K, Iwamura K, Uchikawa M, Sojka BN, Wiels J, Okajima T, Urano T, Furukawa K: Molecular basis for the p phenotype. Identification of distinct and multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish and Japanese individuals. J Biol Chem. 2000 Dec 1;275(48):37752-6. [PubMed Link Image]
  8. Koda Y, Soejima M, Sato H, Maeda Y, Kimura H: Three-base deletion and one-base insertion of the alpha(1,4)galactosyltransferase gene responsible for the P phenotype. Transfusion. 2002 Jan;42(1):48-51. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6192
Enzyme 5 Name UDP-glucose 4-epimerase
Enzyme 5 Synonyms
  1. Galactowaldenase
  2. UDP-galactose 4-epimerase
Enzyme 5 Gene Name GALE
Enzyme 5 Protein Sequence >UDP-glucose 4-epimerase
MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSV
EFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMK
AHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNA
VLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRD
YIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARR
EGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA
Enzyme 5 Number of Residues 348
Enzyme 5 Molecular Weight 38281.4
Enzyme 5 Theoretical pI 6.71
Enzyme 5 GO Classification
Function
  • 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 metabolic process
  • carbohydrate metabolic process
  • cellular metabolic process
  • galactose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
Enzyme 5 General Function Involved in catalytic activity
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • UDP-glucose = UDP-galactose [RN:R00291]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1119217 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q14376 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GALE_HUMAN Link Image
Enzyme 5 PDB ID 1EK6 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1047 bp
ATGGCAGAGAAGGTGCTGGTAACAGGTGGGGCTGGCTACATTGGCAGCCACACGGTGCTG
GAGCTGCTGGAGGCTGGCTACTTGCCTGTGGTCATCGATAACTTCCATAATGCCTTCCGT
GGAGGGGGCTCCCTGCCTGAGAGCCTGCGGCGGGTCCAGGAGCTGACAGGCCGCTCTGTG
GAGTTTGAGGAGATGGACATTTTGGACCAGGGAGCCCTACAGCGTCTCTTCAAAAAGTAC
AGCTTTATGGCGGTCATCCACTTTGCGGGGCTCAAGGCCGTGGGCGAGTCGGTGCAGAAG
CCTCTGGATTATTACAGAGTTAACCTGACCGGGACCATCCAGCTTCTGGAGATCATGAAG
GCCCACGGGGTGAAGAACCTGGTGTTCAGCAGCTCAGCCACTGTGTACGGGAACCCCCAG
TACCTGCCCCTTGATGAGGCCCACCCCACGGGTGGTTGTACCAACCCTTACGGCAAGTCC
AAGTTCTTCATCGAGGAAATGATCCGGGACCTGTGCCAGGCAGACAAGACTTGGAACGTA
GTGCTGCTGCGCTATTTCAACCCCACAGGTGCCCATGCCTCTGGCTGCATTGGTGAGGAT
CCCCAGGGCATACCCAACAACCTCATGCCTTATGTCTCCCAGGTGGCGATCGGGCGACGG
GAGGCCCTGAATGTCTTTGGCAATGACTATGACACAGAGGATGGCACAGGTGTCCGGGAT
TACATCCATGTCGTGGATCTGGCCAAGGGCCACATTGCAGCCTTAAGGAAGCTGAAAGAA
CAGTGTGGCTGCCGGATCTACAACCTGGGCACGGGCACAGGCTATTCAGTGCTGCAGATG
GTCCAGGCTATGGAGAAGGCCTCTGGGAAGAAGATCCCGTACAAGGTGGTGGCACGGCGG
GAAGGTGATGTGGCAGCCTGTTACGCCAACCCCAGCCTGGCCCAAGAGGAGCTGGGGTGG
ACAGCAGCCTTAGGGCTGGACAGGATGTGTGAGGATCTCTGGCGCTGGCAGAAGCAGAAT
CCTTCAGGCTTTGGCACGCAAGCCTGA
Enzyme 5 GenBank Gene ID L41668 Link Image
Enzyme 5 GeneCard ID GALE Link Image
Enzyme 5 GenAtlas ID GALE Link Image
Enzyme 5 HGNC ID HGNC:4116 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p36-p35
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Schulz JM, Watson AL, Sanders R, Ross KL, Thoden JB, Holden HM, Fridovich-Keil JL: Determinants of function and substrate specificity in human UDP-galactose 4'-epimerase. J Biol Chem. 2004 Jul 30;279(31):32796-803. Epub 2004 Jun 2. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. Wohlers TM, Fridovich-Keil JL: Studies of the V94M-substituted human UDPgalactose-4-epimerase enzyme associated with generalized epimerase-deficiency galactosaemia. J Inherit Metab Dis. 2000 Nov;23(7):713-29. [PubMed Link Image]
  11. Henderson JM, Huguenin SM, Cowan TM, Fridovich-Keil JL: A PCR-based method for detecting known mutations in the human UDP galactose-4'-epimerase gene associated with epimerase-deficiency galactosemia. Clin Genet. 2001 Nov;60(5):350-5. [PubMed Link Image]
  12. Timson DJ: Functional analysis of disease-causing mutations in human UDP-galactose 4-epimerase. FEBS J. 2005 Dec;272(23):6170-7. [PubMed Link Image]
  13. Park HD, Park KU, Kim JQ, Shin CH, Yang SW, Lee DH, Song YH, Song J: The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients. Genet Med. 2005 Nov-Dec;7(9):646-9. [PubMed Link Image]
  14. Wasilenko J, Lucas ME, Thoden JB, Holden HM, Fridovich-Keil JL: Functional characterization of the K257R and G319E-hGALE alleles found in patients with ostensibly peripheral epimerase deficiency galactosemia. Mol Genet Metab. 2005 Jan;84(1):32-8. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6320
Enzyme 6 Name Beta-1,4-galactosyltransferase 3
Enzyme 6 Synonyms
  1. Beta-1,4-GalTase 3
  2. Beta4Gal-T3
  3. b4Gal-T3
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3
  6. N-acetyllactosamine synthase
  7. Nal synthase
  8. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  9. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Enzyme 6 Gene Name B4GALT3
Enzyme 6 Protein Sequence >Beta-1,4-galactosyltransferase 3
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSH
LPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCE
PRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVR
EALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSAL
TPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEEN
PHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPG
SSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
Enzyme 6 Number of Residues 393
Enzyme 6 Molecular Weight 43927.6
Enzyme 6 Theoretical pI 9.45
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 6 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 6 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids
Enzyme 6 Pathways
Enzyme 6 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 11-31
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2982510 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O60512 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B4GT3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID Y12509 Link Image
Enzyme 6 GeneCard ID B4GALT3 Link Image
Enzyme 6 GenAtlas ID B4GALT3 Link Image
Enzyme 6 HGNC ID HGNC:926 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1q21-q23
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6381
Enzyme 7 Name Galactose-1-phosphate uridylyltransferase
Enzyme 7 Synonyms
  1. Gal-1-P uridylyltransferase
  2. UDP-glucose--hexose-1-phosphate uridylyltransferase
Enzyme 7 Gene Name GALT
Enzyme 7 Protein Sequence >Galactose-1-phosphate uridylyltransferase
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQ
LLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAK
SARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC
SNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWL
VLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGW
HGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA
LPEVHYHLGQKDRETATIA
Enzyme 7 Number of Residues 379
Enzyme 7 Molecular Weight 43362.8
Enzyme 7 Theoretical pI 6.99
Enzyme 7 GO Classification
Function
  • UDP-glucose:hexose-1-phosphate uridylyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • uridylyltransferase activity
  • zinc ion binding
Process
  • alcohol metabolic process
  • galactose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 7 General Function Involved in UDP-glucose:hexose-1-phosphate uridylyltransferase activity
Enzyme 7 Specific Function UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose
Enzyme 7 Pathways
Enzyme 7 Reactions
  • UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose [RN:R00955]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 55663283 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P07902 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GALT_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1140 bp
ATGTCGCGCAGTGGAACCGATCCTCAGCAACGCCAGCAGGCGTCAGAGGCGGACGCCGCA
GCAGCAACCTTCCGGGCAAACGACCATCAGCATATCCGCTACAACCCGCTGCAGGATGAG
TGGGTGCTGGTGTCAGCTCACCGCATGAAGCGGCCCTGGCAGGGTCAAGTGGAGCCCCAG
CTTCTGAAGACAGTGCCCCGCCATGACCCTCTCAACCCTCTGTGTCCTGGGGCCATCCGA
GCCAACGGAGAGGTGAATCCCCAGTACGATAGCACCTTCCTGTTTGACAACGACTTCCCA
GCTCTGCAGCCTGATGCCCCCAGTCCAGGACCCAGTGATCATCCCCTTTTCCAAGCAAAG
TCTGCTCGAGGAGTCTGTAAGGTCATGTGCTTCCACCCCTGGTCGGATGTAACGCTGCCA
CTCATGTCGGTCCCTGAGATCCGGGCTGTTGTTGATGCATGGGCCTCAGTCACAGAGGAG
CTGGGTGCCCAGTACCCTTGGGTGCAGATCTTTGAAAACAAAGGTGCCATGATGGGCTGT
TCTAACCCCCACCCCCACTGCCAGGTATGGGCCAGCAGTTTCCTGCCAGATATTGCCCAG
CGTGAGGAGCGATCTCAGCAGGCCTATAAGAGTCAGCATGGAGAGCCCCTGCTAATGGAG
TACAGCCGCCAGGAGCTACTCAGGAAGGAACGTCTGGTCCTAACCAGTGAGCACTGGTTA
GTACTGGTCCCCTTCTGGGCAACATGGCCCTACCAGACACTGCTGCTGCCCCGTCGGCAT
GTGCGGCGGCTACCTGAGCTGACCCCTGCTGAGCGTGATGATCTAGCCTCCATCATGAAG
AAGCTCTTGACCAAGTATGACAACCTCTTTGAGACGTCCTTTCCCTACTCCATGGGCTGG
CATGGGGCTCCCACAGGATCAGAGGCTGGGGCCAACTGGAACCATTGGCAGCTGCACGCT
CATTACTACCCTCCGCTCCTGCGCTCTGCCACTGTCCGGAAATTCATGGTTGGCTACGAA
ATGCTTGCTCAGGCTCAGAGGGACCTCACCCCTGAGCAGGCTGCAGAGAGACTAAGGGCA
CTTCCTGAGGTTCATTACCACCTGGGGCAGAAGGACAGGGAGACAGCAACCATCGCCTGA
Enzyme 7 GenBank Gene ID AL162231 Link Image
Enzyme 7 GeneCard ID GALT Link Image
Enzyme 7 GenAtlas ID GALT Link Image
Enzyme 7 HGNC ID HGNC:4135 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Reichardt JK: Genetic basis of galactosemia. Hum Mutat. 1992;1(3):190-6. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. Bosch AM, Ijlst L, Oostheim W, Mulders J, Bakker HD, Wijburg FA, Wanders RJ, Waterham HR: Identification of novel mutations in classical galactosemia. Hum Mutat. 2005 May;25(5):502. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6389
Enzyme 8 Name Histo-blood group ABO system transferase
Enzyme 8 Synonyms
  1. Fucosylglycoprotein 3-alpha-galactosyltransferase
  2. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
  3. Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
  4. Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
  5. Histo-blood group A transferase
  6. A transferase
  7. Histo-blood group B transferase
  8. B transferase
  9. NAGAT
  10. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Enzyme 8 Gene Name ABO
Enzyme 8 Protein Sequence >Histo-blood group ABO system transferase
MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH
LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV
FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR
WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS
REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW
HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
Enzyme 8 Number of Residues 354
Enzyme 8 Molecular Weight 40933.6
Enzyme 8 Theoretical pI 9.24
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • membrane
Enzyme 8 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 8 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 8 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 8 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 [RN:R04423]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 33-53
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 58331216 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P16442 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name BGAT_HUMAN Link Image
Enzyme 8 PDB ID 1LZI Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1065 bp
ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG
ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA
AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT
CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGT
AGGAAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTC
AACATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTG
TTTGCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCAC
TTCATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCCGGCCGCGGTGCCC
CGCGTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGC
TGGCAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTC
CTCAGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTG
GGCGTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGC
CGGGAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAG
GGCGATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTC
ACCAGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGG
CACGACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCC
CCCGAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGG
TTCACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA
Enzyme 8 GenBank Gene ID NM_020469.2 Link Image
Enzyme 8 GeneCard ID ABO Link Image
Enzyme 8 GenAtlas ID ABO Link Image
Enzyme 8 HGNC ID HGNC:79 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9q34.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. Seltsam A, Das Gupta C, Bade-Doeding C, Blasczyk R: A weak blood group A phenotype caused by a translation-initiator mutation in the ABO gene. Transfusion. 2006 Mar;46(3):434-40. [PubMed Link Image]
  6. Seltsam A, Wagner FF, Gruger D, Gupta CD, Bade-Doeding C, Blasczyk R: Weak blood group B phenotypes may be caused by variations in the CCAAT-binding factor/NF-Y enhancer region of the ABO gene. Transfusion. 2007 Dec;47(12):2330-5. Epub 2007 Aug 30. [PubMed Link Image]
  7. Seltsam A, Gruger D, Just B, Figueiredo C, Gupta CD, Deluca DS, Blasczyk R: Aberrant intracellular trafficking of a variant B glycosyltransferase. Transfusion. 2008 Sep;48(9):1898-905. Epub 2008 May 29. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Seltsam A, Hallensleben M, Kollmann A, Blasczyk R: The nature of diversity and diversification at the ABO locus. Blood. 2003 Oct 15;102(8):3035-42. Epub 2003 Jun 26. [PubMed Link Image]
  10. Ogasawara K, Yabe R, Uchikawa M, Saitou N, Bannai M, Nakata K, Takenaka M, Fujisawa K, Ishikawa Y, Juji T, Tokunaga K: Molecular genetic analysis of variant phenotypes of the ABO blood group system. Blood. 1996 Oct 1;88(7):2732-7. [PubMed Link Image]
  11. 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]
  12. Roubinet F, Despiau S, Calafell F, Jin F, Bertranpetit J, Saitou N, Blancher A: Evolution of the O alleles of the human ABO blood group gene. Transfusion. 2004 May;44(5):707-15. [PubMed Link Image]
  13. 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]
  14. 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]
  15. 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]
  16. Marcus SL, Polakowski R, Seto NO, Leinala E, Borisova S, Blancher A, Roubinet F, Evans SV, Palcic MM: A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase. J Biol Chem. 2003 Apr 4;278(14):12403-5. Epub 2003 Jan 15. [PubMed Link Image]
  17. Nguyen HP, Seto NO, Cai Y, Leinala EK, Borisova SN, Palcic MM, Evans SV: The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases. J Biol Chem. 2003 Dec 5;278(49):49191-5. Epub 2003 Sep 11. [PubMed Link Image]
  18. Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM: Structural basis for the inactivity of human blood group O2 glycosyltransferase. J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. [PubMed Link Image]
  19. Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV: Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases. J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. [PubMed Link Image]
  20. Persson M, Letts JA, Hosseini-Maaf B, Borisova SN, Palcic MM, Evans SV, Olsson ML: Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif. J Biol Chem. 2007 Mar 30;282(13):9564-70. Epub 2007 Jan 26. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6390
Enzyme 9 Name 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
Enzyme 9 Synonyms
  1. Ceramide UDP-galactosyltransferase
  2. Cerebroside synthase
  3. UDP-galactose-ceramide galactosyltransferase
Enzyme 9 Gene Name UGT8
Enzyme 9 Protein Sequence >2-hydroxyacylsphingosine 1-beta-galactosyltransferase
MKSYTPYFILLWSAVGIAKAAKIIIVPPIMFESHMYIFKTLASALHERGHHTVFLLSEGR
DIAPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAIELFDILDHYTKNCDLMVGN
HALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEF
NSLLTDRMNLLQRMKNTGVYLISRLGVSFLVLPKYERIMQKYNLLPEKSMYDLVHGSSLW
MLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVNGANEHGFVLVSFGAGVKYL
SEDIANKLAGALGRLPQKVIWRFSGPKPKNLGNNTKLIEWLPQNDLLGHSKIKAFLSHGG
LNSIFETIYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWKTVTEKELYEALVKVINNP
SYRQRAQKLSEIHKDQPGHPVNRTIYWIDYIIRHNGAHHLRAAVHQISFCQYFLLDIAFV
LLLGAALLYFLLSWVTKFIYRKIKSLWSRNKHSTVNGHYHNGILNGKYKRNGHIKHEKKV
K
Enzyme 9 Number of Residues 541
Enzyme 9 Molecular Weight 61437.3
Enzyme 9 Theoretical pI 9.97
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 9 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 9 Specific Function Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-20
Enzyme 9 Transmembrane Regions
  • 472-492
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 189491660 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q16880 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name CGT_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1626 bp
ATGAAGTCTTACACTCCATATTTCATTCTCCTGTGGAGTGCTGTTGGGATAGCGAAGGCT
GCCAAAATCATCATCGTGCCGCCAATTATGTTTGAAAGCCATATGTACATTTTCAAGACG
CTAGCCTCAGCCTTGCACGAGAGAGGCCACCATACAGTGTTCCTCCTCTCTGAAGGCAGA
GACATCGCCCCATCTAATCATTACAGCCTCCAGCGCTACCCAGGGATCTTTAACAGTACC
ACCTCAGATGCTTTCCTACAGTCCAAGATGCGGAATATTTTCTCTGGGAGATTGACAGCA
ATCGAACTGTTTGACATACTGGATCACTATACTAAGAACTGTGACCTGATGGTTGGCAAC
CATGCCCTGATCCAGGGTCTGAAGAAAGAAAAATTTGACCTGCTGCTGGTGGACCCTAAT
GATATGTGTGGATTTGTGATAGCTCATCTTTTAGGGGTTAAATATGCTGTATTTTCAACT
GGCCTTTGGTATCCTGCTGAAGTGGGTGCTCCTGCTCCATTAGCATACGTCCCAGAGTTT
AACTCACTCCTCACAGACCGCATGAACTTGCTGCAAAGGATGAAAAATACCGGTGTTTAC
CTCATTTCCAGATTAGGGGTCAGCTTTCTGGTTCTTCCCAAATATGAAAGGATAATGCAG
AAGTACAACCTGCTGCCGGAGAAGTCCATGTATGATTTGGTTCATGGGTCCAGCCTGTGG
ATGCTGTGTACTGACGTAGCACTGGAATTCCCAAGACCCACTCTGCCTAATGTTGTTTAT
GTAGGAGGAATCCTAACCAAACCAGCCAGCCCACTACCAGAAGATCTCCAAAGATGGGTA
AATGGTGCTAATGAACATGGCTTTGTCTTGGTGTCTTTTGGAGCTGGTGTCAAGTATCTG
TCAGAAGACATTGCTAACAAACTGGCAGGAGCTCTGGGGAGATTGCCTCAAAAAGTGATT
TGGAGGTTTTCTGGACCCAAACCAAAGAATCTAGGAAACAACACTAAACTCATAGAATGG
TTACCACAAAATGACCTGCTTGGGCATTCAAAGATTAAAGCCTTCCTGAGCCATGGTGGT
TTGAACAGTATTTTTGAAACTATGTATCATGGTGTGCCTGTAGTGGGAATTCCACTCTTT
GGAGACCATTATGATACTATGACCAGAGTACAGGCAAAAGGCATGGGGATATTGCTAGAA
TGGAAGACAGTTACTGAAAAAGAGCTCTATGAAGCACTAGTGAAGGTTATCAATAATCCC
AGCTACCGTCAGAGGGCTCAGAAGCTTTCGGAAATTCACAAGGATCAACCTGGTCACCCT
GTCAATCGAACTATCTATTGGATAGATTATATTATTCGTCACAATGGAGCCCATCACCTA
CGTGCCGCTGTCCATCAGATCTCCTTTTGTCAGTATTTTTTACTGGATATTGCCTTTGTG
CTTTTGCTTGGTGCTGCCTTGTTATACTTTCTCTTGTCTTGGGTGACAAAATTTATCTAC
AGAAAAATCAAAAGTCTGTGGTCTAGAAATAAGCATAGCACAGTTAATGGACATTACCAC
AATGGAATCCTCAATGGCAAGTACAAAAGAAATGGCCATATTAAACATGAAAAGAAAGTG
AAATGA
Enzyme 9 GenBank Gene ID NM_001128174.1 Link Image
Enzyme 9 GeneCard ID UGT8 Link Image
Enzyme 9 GenAtlas ID UGT8 Link Image
Enzyme 9 HGNC ID HGNC:12555 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4q26
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Bosio A, Binczek E, Le Beau MM, Fernald AA, Stoffel W: The human gene CGT encoding the UDP-galactose ceramide galactosyl transferase (cerebroside synthase): cloning, characterization, and assignment to human chromosome 4, band q26. Genomics. 1996 May 15;34(1):69-75. [PubMed Link Image]
  2. Kapitonov D, Yu RK: Cloning, characterization, and expression of human ceramide galactosyltransferase cDNA. Biochem Biophys Res Commun. 1997 Mar 17;232(2):449-53. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16488
Enzyme 10 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 10 Synonyms Not Available
Enzyme 10 Gene Name B4GALT1
Enzyme 10 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 10 Number of Residues 398
Enzyme 10 Molecular Weight 43921
Enzyme 10 Theoretical pI 8.77
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
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 B2R710 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B2R710_HUMAN Link Image
Enzyme 10 PDB ID 1FR8 Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK312797 Link Image
Enzyme 10 GeneCard ID B2R710 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 16489
Enzyme 11 Name cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
Enzyme 11 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 2, isoform CRA_a
Enzyme 11 Gene Name B4GALT2
Enzyme 11 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 11 Number of Residues 372
Enzyme 11 Molecular Weight 41973
Enzyme 11 Theoretical pI 9.66
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
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 B3KTP0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B3KTP0_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 AK095873 Link Image
Enzyme 11 GeneCard ID B3KTP0 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 SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16517
Enzyme 12 Name UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
Enzyme 12 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a
  2. SubName: cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA
Enzyme 12 Gene Name B4GALT4
Enzyme 12 Protein Sequence >UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKG
KTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKA
LQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLE
ALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSR
EQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAE
RMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA
Enzyme 12 Number of Residues 344
Enzyme 12 Molecular Weight 40040.9
Enzyme 12 Theoretical pI 9.42
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 12 General Function Involved in transferase activity, transferring glycosyl groups
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 189069376 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID B2RAZ5 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B2RAZ5_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1035 bp
ATGGGCTTCAACCTGACTTTCCACCTTTCCTACAAATTCCGATTACTGTTGCTGTTGACT
TTGTGCCTGACAGTGGTTGGGTGGGCCACCAGTAACTACTTCGTGGGTGCCATTCAAGAG
ATTCCTAAAGCAAAGGAGTTCATGGCTAATTTCCATAAGACCCTCATTTTGGGGAAGGGA
AAAACTCTGACTAATGAAGCATCCACGAAGAAGGTAGAACTTGACAACTGCCCTTCTGTG
TCTCCTTACCTCAGAGGCCAGAGCAAGCTCATTTTCAAACCAGATCTCACTTTGGAAGAG
GTACAGGCAGAAAATCCCAAAGTGTCCAGAGGCCGGTATCGCCCTCAGGAATGTAAAGCT
TTACAGAGGGTCGCCATCCTCGTTCCCCACCGGAACAGAGAGAAACACCTGATGTACCTG
CTGGAACATCTGCATCCCTTCCTGCAGAGGCAGCAGCTGGATTATGGCATCTACGTCATC
CACCAGGCTGAAGGTAAAAAGTTTAATCGAGCCAAACTCTTGAATGTGGGCTATCTAGAA
GCCCTCAAGGAAGAAAATTGGGACTGCTTTATATTCCACGATGTGGACCTGGTACCCGAG
AATGACTTTAACCTTTACAAGTGTGAGGAGCATCCCAAGCATCTGGTGGTTGGCAGGAAC
AGCACTGGGTACAGGTTACGTTACAGTGGATATTTTGGGGGTGTTACTGCCCTAAGCAGA
GAGCAGTTTTTCAAGGTGAATGGATTCTCTAACAACTACTGGGGATGGGGAGGCGAAGAC
GATGACCTCAGACTCAGGGTTGAGCTCCAAAGAATGAAAATTTCCCGGCCCCTGCCTGAA
GTGGGTAAATATACAATGGTCTTCCACACTAGAGACAAAGGCAATGAGGTGAACGCAGAA
CGGATGAAGCTCTTACACCAAGTGTCACGAGTCTGGAGAACAGATGGGTTGAGTAGTTGT
TCTTATAAATTAGTATCTGTGGAACACAATCCTTTATATATCAACATCACAGTGGATTTC
TGGTTTGGTGCATGA
Enzyme 12 GenBank Gene ID AK314425 Link Image
Enzyme 12 GeneCard ID B4GALT4 Link Image
Enzyme 12 GenAtlas ID B4GALT4 Link Image
Enzyme 12 HGNC ID HGNC:927 Link Image
Enzyme 12 Chromosome Location 3
Enzyme 12 Locus 3q13.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16552
Enzyme 13 Name cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
Enzyme 13 Synonyms
  1. SubName: UDP glycosyltransferase 8 (UDP-galactose ceramide galactosyltransferase)
Enzyme 13 Gene Name UGT8
Enzyme 13 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 13 Number of Residues 541
Enzyme 13 Molecular Weight 61457
Enzyme 13 Theoretical pI 9.97
Enzyme 13 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322] ALL_REAC R04322
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B3KXU7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B3KXU7_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK127970 Link Image
Enzyme 13 GeneCard ID B3KXU7 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16553
Enzyme 14 Name cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 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 14 Number of Residues 378
Enzyme 14 Molecular Weight 41437.3
Enzyme 14 Theoretical pI 8.22
Enzyme 14 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 14 General Function Involved in galactosyltransferase activity
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 193786784 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID B3KQP5 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B3KQP5_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1137 bp
ATGCAGCTCAGGCTCTTCCGGCGCCTCCTTCTCGCCGCTTTGCTGCTGGTGATCGTCTGG
ACCCTCTTCGGGCCTTCGGGGTTGGGGGAGGAGCTGCTGAGCCTCTCACTAGCCTCCCTG
CTCCCAGCCCCCGCCTCACCGGGGCCGCCCCTGGCCCTGCCCCGCCTCTTGATCCCCAAC
CAGGAAGCTTGCAGTGGTCCCGGGGCCCCTCCCTTCCTGCTCATCCTGGTGTGCACGGCT
CCGGAGAACCTGAACCAGAGAAACGCCATTCGGGCTTCGTGGGGCGGGCTGCGCGAGGCC
CGGGGGCTCAGGGTACAGACGCTATTCTTGCTGGGAGAGCCGAACGCACAGCACCCCGTG
TGGGGTTCCCAGGGGAGTGACCTGGCCTCGGAGTCAGCAGCCCAGGGGGATATCTTGCAG
GCCGCCTTCCAGGACTCCTACCGCAACCTCACCCTAAAGACCCTCAGCGGGCTGAACTGG
GCTGAGAAACACTGCCCCATGGCCCGATACGTCCTCAAGACGGACGATGATGTGTATGTC
AACGTCCCTGAACTGGTATCAGAGCTGGTCTTGCGAGGGGGCCGTTGGGGGCAATGGGAG
GGAAGCACGGAACCCCAGAGAGAGGCTGAGCAGGAAGGAGGCCAGGTTTTGCACAGCGAG
GAAGTGCCTCTTCTGTACTTGGGCCGGGTGCACTGGCGCGTGAACCCCTCTCGGACACCG
GGGGGCAGGCACCGCGTATCAGAGGAGCAGTGGCCTCACACCTGGGGCCCCTTTCCACCC
TATGCCTCAGGCACGGGGTATGTGCTGTCAGCGTCTGCTGTGCAGCTCATTCTCAAGGTG
GCCAGCCGGGCACCCCTTCTCCCATTAGAGGATGTCTTTGTGGGGGTAAGTGCCCGACGA
GGAGGCCTCGCCCCAACACAGTGTGTCAAGCTGGCTGGTGCCACCCACTACCCGCTAGAC
CGGTGCTGCTATGGGAAATTCCTGCTGACGTCCCACAGGCTGGACCCCTGGAAGATGCAG
GAAGCCTGGAAGCTGGTGGGTGGCTCTGACGGGGAAAGGACTGCGCCCTTTTGCTCCTGG
TTCCAGGGAGTCCTGGGCATCCTGCGGTGTCGAGCAATAGCCTGGCTTCAGAGCTGA
Enzyme 14 GenBank Gene ID AK075312 Link Image
Enzyme 14 GeneCard ID Not Available
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID HGNC:919 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs Not Available
Enzyme 14 General References
  1. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16555
Enzyme 15 Name cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name A4GALT
Enzyme 15 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 15 Number of Residues 353
Enzyme 15 Molecular Weight 40500
Enzyme 15 Theoretical pI 9.18
Enzyme 15 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 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID B2R7C4 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B2R7C4_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AK312927 Link Image
Enzyme 15 GeneCard ID B2R7C4 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location 22
Enzyme 15 Locus 22q11.2-q13.2
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available