Tag | Content |
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CPLM ID | CPLM-009806 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphodiesterase YfcE |
Protein Synonyms/Alias | |
Gene Name | yfcE |
Gene Synonyms/Alias | b2300; JW5377 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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55 | PEGYAPAKVAERLNE | acetylation | [1] | 66 | RLNEVAHKVIAVRGN | 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 | Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p- nitrophenylphosphorylcholine (pNPPC). The physiological substrate is unknown. |
Sequence Annotation | METAL 9 9 Manganese 1. METAL 11 11 Manganese 1. METAL 37 37 Manganese 1. METAL 37 37 Manganese 2. METAL 73 73 Manganese 2. METAL 105 105 Manganese 2. METAL 127 127 Manganese 2. METAL 129 129 Manganese 1. |
Keyword | 3D-structure; Complete proteome; Hydrolase; Manganese; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 184 AA |
Protein Sequence | MMKLMFASDI HGSLPATERV LELFAQSGAQ WLVILGDVLN HGPRNALPEG YAPAKVAERL 60 NEVAHKVIAV RGNCDSEVDQ MLLHFPITAP WQQVLLEKQR LFLTHGHLFG PENLPALNQN 120 DVLVYGHTHL PVAEQRGEIF HFNPGSVSIP KGGNPASYGM LDNDVLSVIA LNDQSIIAQV 180 AINP 184 |
Gene Ontology | GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. GO:0008270; F:zinc ion binding; IDA:EcoCyc. |
Interpro | |
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SMART | |
PROSITE | |
PRINTS | |