Tag | Content |
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CPLM ID | CPLM-026787 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Beta-ketothiolase, acetoacetyl-CoA thiolase |
Protein Synonyms/Alias | |
Gene Name | RPA0531 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
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145 | ELVDTMLKDGLWDAF | acetylation | [1] | 208 | PVTIKTRKGDIVVDT | acetylation | [1] | 286 | GQAGVDPKIMGSGPI | acetylation | [1] |
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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 | Acyltransferase; Complete proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 392 AA |
Protein Sequence | MSDDVVIVSA ARTAVGSFNG AFANTPAHEL GAVAIKAALE RGGIDPAQVS EVIMGQILTA 60 GQGQNPARQA SIAAGIPVDS PAWGINQLCG SGLRSVALGY QALMNGDSDI VIAGGQESMS 120 MAPHAQYLRG GVKMGAVELV DTMLKDGLWD AFNGYHMGNT AENVARQWQI TRDQQDEFAV 180 ASQQKAEAAQ KAGKFKDEIV PVTIKTRKGD IVVDTDEYPR HGATLEAMAK LKPAFEKDGT 240 VTAGSASGIN DGAAAVVLMT AKQAEKLGKK PLARIVSWGQ AGVDPKIMGS GPIPASRAAL 300 KKAGWSVGDL DLIEANEAFA AQACAVNKDL GWDTSKVNVN GGAIAIGHPI GASGARVLVT 360 LLHEMQKRDS KKGLATLCIG GGMGIAMCLA RD 392 |
Gene Ontology | GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |