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
- Functionsferrous iron binding / galactokinase activity / UDP-glucose / zinc ion bindingProcessescarbohydrate phosphorylation / galactose catabolic process via UDP-galactoseComponentscytosol
- 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
Resource Link UniProtKB ID P09148 UniProtKB Entry Name GAL7_ECOLI GenBank Protein ID 41524 GenBank Gene ID X06226 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]