Tag | Content |
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CPLM ID | CPLM-004495 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoribosyl 1,2-cyclic phosphodiesterase |
Protein Synonyms/Alias | Phosphoribosyl cyclic phosphodiesterase |
Gene Name | phnP |
Gene Synonyms/Alias | b4092; JW4053 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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171 | DTAGLPEKTLKFLRN | 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 hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate. |
Sequence Annotation | METAL 21 21 Zinc. METAL 23 23 Zinc. METAL 26 26 Zinc. METAL 76 76 Manganese 1; via tele nitrogen. METAL 78 78 Manganese 1; via pros nitrogen. METAL 80 80 Manganese 2. METAL 81 81 Manganese 2; via tele nitrogen. METAL 143 143 Manganese 1; via tele nitrogen. METAL 164 164 Manganese 1. METAL 164 164 Manganese 2. METAL 222 222 Manganese 2; via tele nitrogen. METAL 225 225 Zinc; via pros nitrogen. |
Keyword | 3D-structure; Complete proteome; Hydrolase; Manganese; Metal-binding; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 252 AA |
Protein Sequence | MSLTLTLTGT GGAQGVPAWG CECAACARAR RSPQYRRQPC SGVVKFNDAI TLIDAGLHDL 60 ADRWSPGSFQ QFLLTHYHMD HVQGLFPLRW GVGDPIPVYG PPDEQGCDDL FKHPGLLDFS 120 HTVEPFVVFD LQGLQVTPLP LNHSKLTFGY LLETAHSRVA WLSDTAGLPE KTLKFLRNNQ 180 PQVMVMDCSH PPRADAPRNH CDLNTVLALN QVIRSPRVIL THISHQFDAW LMENALPSGF 240 EVGFDGMEIG VA 252 |
Gene Ontology | GO:0030145; F:manganese ion binding; IDA:EcoCyc. GO:0008081; F:phosphoric diester hydrolase activity; IDA:EcoCyc. GO:0019700; P:organic phosphonate catabolic process; IMP:EcoCyc. |
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PRINTS | |