Tag | Content |
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CPLM ID | CPLM-009382 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glucose-1-phosphate thymidylyltransferase 2 |
Protein Synonyms/Alias | G1P-TT 2; dTDP-glucose pyrophosphorylase 2; dTDP-glucose synthase 2 |
Gene Name | rmlA2 |
Gene Synonyms/Alias | rffH; yifG; b3789; JW3763 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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58 | IITTPEDKGYFQRLL | acetylation | [1] | 160 | RAISLEEKPKQPKSN | acetylation | [1] | 267 | WLDDEGVKRAASSLA | acetylation | [1] | 275 | RAASSLAKTGYGQYL | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. |
Sequence Annotation | METAL 108 108 Magnesium. METAL 223 223 Magnesium. |
Keyword | 3D-structure; Complete proteome; Exopolysaccharide synthesis; Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 293 AA |
Protein Sequence | MKGIILAGGS GTRLHPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIREIL IITTPEDKGY 60 FQRLLGDGSE FGIQLEYAEQ PSPDGLAQAF IIGETFLNGE PSCLVLGDNI FFGQGFSPKL 120 RHVAARTEGA TVFGYQVMDP ERFGVVEFDD NFRAISLEEK PKQPKSNWAV TGLYFYDSKV 180 VEYAKQVKPS ERGELEITSI NQMYLEAGNL TVELLGRGFA WLDTGTHDSL IEASTFVQTV 240 EKRQGFKIAC LEEIAWRNGW LDDEGVKRAA SSLAKTGYGQ YLLELLRARP RQY 293 |
Gene Ontology | GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:UniProtKB. GO:0000287; F:magnesium ion binding; IDA:UniProtKB. GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway. GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB. |
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