Tag | Content |
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CPLM ID | CPLM-006785 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glucose-1-phosphate thymidylyltransferase 1 |
Protein Synonyms/Alias | G1P-TT 1; dTDP-glucose pyrophosphorylase 1; dTDP-glucose synthase 1 |
Gene Name | rmlA1 |
Gene Synonyms/Alias | rfbA; rmlA; b2039; JW2024 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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153 | YGVVEFDKNGTAISL | acetylation | [1] | 163 | TAISLEEKPLEPKSN | acetylation | [1] | 191 | VQMAKNLKPSARGEL | acetylation | [1] | 271 | IDVEQVRKLAVPLIK | acetylation | [1] | 278 | KLAVPLIKNNYGQYL | acetylation | [1] | 287 | NYGQYLYKMTKDSN* | 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 111 111 Magnesium (By similarity). METAL 226 226 Magnesium (By similarity). |
Keyword | 3D-structure; Complete proteome; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 293 AA |
Protein Sequence | MKMRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD 60 TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GGDDCALVLG DNIFYGHDLP 120 KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDKNGTAISL EEKPLEPKSN YAVTGLYFYD 180 NDVVQMAKNL KPSARGELEI TDINRIYLEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI 240 ATIEERQGLK VSCPEEIAFR KGFIDVEQVR KLAVPLIKNN YGQYLYKMTK DSN 293 |
Gene Ontology | GO:0005829; C:cytosol; IDA:UniProtKB. GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway. GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro. GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway. |
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PRINTS | |