Tag | Content |
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CPLM ID | CPLM-003133 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Sugar phosphatase YidA |
Protein Synonyms/Alias | |
Gene Name | yidA |
Gene Synonyms/Alias | b3697; JW3674 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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98 | DDYRFLEKLSREVGS | acetylation | [1] | 193 | YFLEILDKRVNKGTG | 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 dephosphorylation of different sugar phosphates including erythrose-4-phosphate (Ery4P), ribose-5- phosphate (Ribu5P), fructose-1-phosphate (Fru1P), fructose-6- phosphate (Fru6P), glucose-6-P (Glu6P), and also imidodiphosphate (Imido-di-P) and acetyl phosphate (Acetyl-P). Selectively hydrolyzes alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form. |
Sequence Annotation | REGION 9 11 Substrate (By similarity). ACT_SITE 9 9 Nucleophile (Probable). METAL 9 9 Magnesium. METAL 11 11 Magnesium. METAL 220 220 Magnesium. |
Keyword | 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 270 AA |
Protein Sequence | MAIKLIAIDM DGTLLLPDHT ISPAVKNAIA AARARGVNVV LTTGRPYAGV HNYLKELHME 60 QPGDYCITYN GALVQKAADG STVAQTALSY DDYRFLEKLS REVGSHFHAL DRTTLYTANR 120 DISYYTVHES FVATIPLVFC EAEKMDPNTQ FLKVMMIDEP AILDQAIARI PQEVKEKYTV 180 LKSAPYFLEI LDKRVNKGTG VKSLADVLGI KPEEIMAIGD QENDIAMIEY AGVGVAMDNA 240 IPSVKEVANF VTKSNLEDGV AFAIEKYVLN 270 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IDA:EcoliWiki. GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki. |
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