Tag | Content |
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CPLM ID | CPLM-007748 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ADP compounds hydrolase NudE |
Protein Synonyms/Alias | |
Gene Name | nudE |
Gene Synonyms/Alias | yrfE; b3397; JW3360 |
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 | *MSKSLQKPTILNVE | acetylation | [1] | 111 | ANDLTFLKKLSMAPS | acetylation | [1] | 181 | FLVREWLKGQGRV** | 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 | Active on adenosine(5')triphospho(5')adenosine (Ap3A), ADP-ribose, NADH, adenosine(5')diphospho(5')adenosine (Ap2A). |
Sequence Annotation | DOMAIN 45 172 Nudix hydrolase. MOTIF 80 101 Nudix box. METAL 95 95 Divalent metal cation (By similarity). METAL 99 99 Divalent metal cation (By similarity). BINDING 40 40 Substrate; via amide nitrogen and BINDING 118 118 Substrate; via carbonyl oxygen. |
Keyword | 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 186 AA |
Protein Sequence | MSKSLQKPTI LNVETVARSR LFTVESVDLE FSNGVRRVYE RMRPTNREAV MIVPIVDDHL 60 ILIREYAVGT ESYELGFSKG LIDPGESVYE AANRELKEEV GFGANDLTFL KKLSMAPSYF 120 SSKMNIVVAQ DLYPESLEGD EPEPLPQVRW PLAHMMDLLE DPDFNEARNV SALFLVREWL 180 KGQGRV 186 |
Gene Ontology | GO:0019144; F:ADP-sugar diphosphatase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. |
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