| Tag | Content |
|---|
| CPLM ID | CPLM-041897 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2-ketocyclohexanecarboxyl-CoA hydrolase |
Protein Synonyms/Alias | |
Gene Name | badI |
Gene Synonyms/Alias | RPA0653 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 135 | IFGQVGPKMGSVDPG | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | |
Sequence Annotation | |
Keyword | Complete proteome; Hydrolase; Lyase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 260 AA |
Protein Sequence | MQFEDLIYEI RNGVAWIIIN RPDKMNAFRG TTCDELIKAL YKAGYDKDVG AIVLAGAGDR 60
AFCTGGDQST HDGNYDGRGT VGLPMEELHT AIRDVPKPVI ARVQGYAIGG GNVLATICDL 120
TICSEKAIFG QVGPKMGSVD PGYGTAFLAR VVGEKKAREI WYMCKRYSGK EAEAMGLANL 180
CVPHDELDAE VQKWGEELCE RSPTALAIAK RSFNMDTAHQ AGIAGMGMYA LKLYYDTDES 240
REGVKALQEK RKPEFRKYIK 260 |
Gene Ontology | GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:EC. GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |