Tag | Content |
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CPLM ID | CPLM-006200 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NADH pyrophosphatase |
Protein Synonyms/Alias | |
Gene Name | nudC |
Gene Synonyms/Alias | yjaD; b3996; JW5548 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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7 | *MDRIIEKLDHGWWV | acetylation | [1] | 20 | WVVSHEQKLWLPKGE | acetylation | [1] | 25 | EQKLWLPKGELPYGE | 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 | |
Sequence Annotation | DOMAIN 125 248 Nudix hydrolase. MOTIF 159 180 Nudix box. METAL 98 98 Zinc. METAL 101 101 Zinc. METAL 116 116 Zinc. METAL 119 119 Zinc. METAL 174 174 Divalent metal cation (By similarity). METAL 178 178 Divalent metal cation (By similarity). |
Keyword | 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 257 AA |
Protein Sequence | MDRIIEKLDH GWWVVSHEQK LWLPKGELPY GEAANFDLVG QRALQIGEWQ GEPVWLVQQQ 60 RRHDMGSVRQ VIDLDVGLFQ LAGRGVQLAE FYRSHKYCGY CGHEMYPSKT EWAMLCSHCR 120 ERYYPQIAPC IIVAIRRDDS ILLAQHTRHR NGVHTVLAGF VEVGETLEQA VAREVMEESG 180 IKVKNLRYVT SQPWPFPQSL MTAFMAEYDS GDIVIDPKEL LEANWYRYDD LPLLPPPGTV 240 ARRLIEDTVA MCRAEYE 257 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0030145; F:manganese ion binding; IDA:EcoCyc. GO:0000210; F:NAD+ diphosphatase activity; IEA:HAMAP. GO:0035529; F:NADH pyrophosphatase activity; IDA:EcoCyc. GO:0008270; F:zinc ion binding; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |