| Tag | Content |
|---|
| CPLM ID | CPLM-007843 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Quercetin 2,3-dioxygenase |
Protein Synonyms/Alias | Quercetinase; Pirin-like protein YhhW |
Gene Name | yhhW |
Gene Synonyms/Alias | b3439; JW3402 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 141 | RFDAVQGKQLVLSPD | acetylation | [1] | | 155 | DARDGSLKVHQDMEL | acetylation | [1] | | 169 | LYRWALLKDEQSVHQ | 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 | Has quercetin 2,3-dioxygenase activity in vitro. Its physiological role is unknown; however, may provide a mechanism that would avoid inhibition of key cellular proteins, such as DNA gyrase, by quercetin. |
Sequence Annotation | METAL 57 57 Divalent metal cation.
METAL 59 59 Divalent metal cation.
METAL 101 101 Divalent metal cation.
METAL 103 103 Divalent metal cation (By similarity). |
Keyword | 3D-structure; Complete proteome; Copper; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 231 AA |
Protein Sequence | MIYLRKANER GHANHGWLDS WHTFSFANYY DPNFMGFSAL RVINDDVIEA GQGFGTHPHK 60
DMEILTYVLE GTVEHQDSMG NKEQVPAGEF QIMSAGTGIR HSEYNPSSTE RLHLYQIWIM 120
PEENGITPRY EQRRFDAVQG KQLVLSPDAR DGSLKVHQDM ELYRWALLKD EQSVHQIAAE 180
RRVWIQVVKG NVTINGVKAS TSDGLAIWDE QAISIHADSD SEVLLFDLPP V 231 |
Gene Ontology | GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008127; F:quercetin 2,3-dioxygenase activity; IDA:EcoCyc. |
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