Tag | Content |
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CPLM ID | CPLM-003472 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphatase NudJ |
Protein Synonyms/Alias | |
Gene Name | nudJ |
Gene Synonyms/Alias | ymfB; b1134; JW1120 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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76 | HQWIAPDKTPFLRFL | 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 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2- methyl-5-hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate. |
Sequence Annotation | DOMAIN 3 131 Nudix hydrolase. MOTIF 36 57 Nudix box. |
Keyword | Complete proteome; Hydrolase; Magnesium; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 153 AA |
Protein Sequence | MFKPHVTVAC VVHAEGKFLV VEETINGKAL WNQPAGHLEA DETLVEAAAR ELWEETGISA 60 QPQHFIRMHQ WIAPDKTPFL RFLFAIELEQ ICPTQPHDSD IDCCRWVSAE EILQASNLRS 120 PLVAESIRCY QSGQRYPLEM IGDFNWPFTK GVI 153 |
Gene Ontology | GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |