Galactose-1-phosphate uridylyltransferase

Details

Name
Galactose-1-phosphate uridylyltransferase
Synonyms
  • 2.7.7.12
  • Gal-1-P uridylyltransferase
  • galB
  • UDP-glucose--hexose-1-phosphate uridylyltransferase
Gene Name
galT
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010994|Galactose-1-phosphate uridylyltransferase
MTQFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQVLPAHDPDCFLCAGNVR
VTGDKNPDYTGTYVFTNDFAALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLP
ELSVAALTEIVKTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAE
REDRLQKEYFAEQKSPMLVDYVQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAH
VLRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENQHWQLHAHFY
PPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHFRESGV
Number of residues
348
Molecular Weight
39645.395
Theoretical pI
6.45
GO Classification
Functions
ferrous iron binding / galactokinase activity / UDP-glucose / zinc ion binding
Processes
carbohydrate phosphorylation / galactose catabolic process via UDP-galactose
Components
cytosol
General Function
Zinc ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010995|Galactose-1-phosphate uridylyltransferase (galT)
ATGACGCAATTTAATCCCGTTGATCATCCACATCGCCGCTACAACCCGCTCACCGGGCAA
TGGATTCTGGTTTCACCGCACCGCGCTAAGCGCCCCTGGCAGGGGGCGCAGGAAACGCCA
GCCAAACAGGTGTTACCTGCGCACGATCCAGATTGCTTCCTCTGCGCAGGTAATGTGCGG
GTGACAGGCGATAAAAACCCCGATTACACCGGGACTTACGTTTTCACTAATGACTTTGCG
GCTTTGATGTCTGACACGCCAGATGCGCCAGAAAGTCACGATCCGCTGATGCGTTGCCAG
AGCGCGCGCGGCACCAGCCGGGTGATCTGCTTTTCACCGGATCACAGTAAAACGCTGCCA
GAGCTCAGCGTTGCAGCATTGACGGAAATCGTCAAAACCTGGCAGGAGCAAACCGCAGAA
CTGGGGAAAACGTACCCATGGGTGCAGGTTTTTGAAAACAAAGGCGCGGCGATGGGCTGC
TCTAACCCGCATCCGCACGGTCAGATTTGGGCAAATAGCTTCCTGCCTAACGAAGCTGAG
CGCGAAGACCGCCTGCAAAAAGAATATTTTGCCGAACAGAAATCACCAATGCTGGTGGAT
TATGTTCAGCGCGAGCTGGCAGACGGTAGCCGTACCGTTGTCGAAACCGAACACTGGTTA
GCCGTCGTGCCTTACTGGGCTGCCTGGCCGTTCGAAACGCTACTGCTGCCCAAAGCCCAC
GTTTTACGGATCACCGATTTGACCGACGCCCAGCGCAGCGATCTGGCGCTGGCGTTGAAA
AAGCTGACCAGTCGTTATGACAACCTCTTCCAGTGCTCCTTCCCCTACTCTATGGGCTGG
CACGGCGCGCCATTTAATGGCGAAGAGAATCAACACTGGCAGCTGCACGCGCACTTTTAT
CCGCCTCTGCTGCGCTCCGCCACCGTACGTAAATTTATGGTTGGTTATGAAATGCTGGCA
GAGACCCAGCGAGACCTGACCGCAGAACAGGCAGCAGAGCGTTTGCGCGCAGTCAGCGAT
ATCCATTTTCGCGAATCCGGAGTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP09148
UniProtKB Entry NameGAL7_ECOLI
GenBank Protein ID41524
GenBank Gene IDX06226
General References
  1. Lemaire HG, Muller-Hill B: Nucleotide sequences of the gal E gene and the gal T gene of E. coli. Nucleic Acids Res. 1986 Oct 10;14(19):7705-11. [Article]
  2. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Debouck C, Riccio A, Schumperli D, McKenney K, Jeffers J, Hughes C, Rosenberg M, Heusterspreute M, Brunel F, Davison J: Structure of the galactokinase gene of Escherichia coli, the last (?) gene of the gal operon. Nucleic Acids Res. 1985 Mar 25;13(6):1841-53. [Article]
  6. Cornwell TL, Adhya SL, Reznikoff WS, Frey PA: The nucleotide sequence of the gal T gene of Escherichia coli. Nucleic Acids Res. 1987 Oct 12;15(19):8116. [Article]
  7. Wong LJ, Sheu KF, Lee SL, Frey PA: Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate. Biochemistry. 1977 Mar 8;16(5):1010-6. [Article]
  8. Wedekind JE, Frey PA, Rayment I: The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry. 1996 Sep 10;35(36):11560-9. [Article]
  9. Geeganage S, Ling VW, Frey PA: Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine. Biochemistry. 2000 May 9;39(18):5397-404. [Article]
  10. Wedekind JE, Frey PA, Rayment I: Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Biochemistry. 1995 Sep 5;34(35):11049-61. [Article]
  11. Thoden JB, Ruzicka FJ, Frey PA, Rayment I, Holden HM: Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site. Biochemistry. 1997 Feb 11;36(6):1212-22. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01861Uridine diphosphate glucoseexperimentalunknownDetails
DB03435Uridine-5'-DiphosphateexperimentalunknownDetails
DB03685Uridine monophosphateexperimentalunknownDetails