| Tag | Content |
|---|
| CPLM ID | CPLM-006713 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | GDP-mannose pyrophosphatase NudK |
Protein Synonyms/Alias | |
Gene Name | nudK |
Gene Synonyms/Alias | yffH; b2467; JW2451 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 11 | QITLIKDKILSDNYF | acetylation | [1] | | 56 | TILLYNTKKKTVVLI | acetylation | [1] |
|
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 GDP-mannose. Can also use other substrates, catalyzing the hydrolysis of the pyrophosphate bond, releasing a nucleoside monophosphate and a phosphorylated moiety, depending on the substrate. |
Sequence Annotation | DOMAIN 43 180 Nudix hydrolase.
MOTIF 86 106 Nudix box. |
Keyword | 3D-structure; Complete proteome; Hydrolase; Magnesium; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 191 AA |
Protein Sequence | MTQQITLIKD KILSDNYFTL HNITYDLTRK DGEVIRHKRE VYDRGNGATI LLYNTKKKTV 60
VLIRQFRVAT WVNGNESGQL IESCAGLLDN DEPEVCIRKE AIEETGYEVG EVRKLFELYM 120
SPGGVTELIH FFIAEYSDNQ RANAGGGVED EDIEVLELPF SQALEMIKTG EIRDGKTVLL 180
LNYLQTSHLM D 191 |
Gene Ontology | GO:0052751; F:GDP-mannose hydrolase activity; IDA:EcoCyc. GO:0000287; F:magnesium ion binding; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |