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LOCUS WP_000665977 392 aa linear BCT 02-JAN-2025 ACCESSION WP_000665977 VERSION WP_000665977.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 392) AUTHORS Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K. TITLE The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation JOURNAL Biochemistry 48 (46), 11011-11025 (2009) PUBMED 19842716 REFERENCE 2 (residues 1 to 392) AUTHORS Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E. TITLE Phylogenetic analysis of the thiolase family. Implications for the evolutionary origin of peroxisomes JOURNAL J Mol Evol 35 (2), 147-155 (1992) PUBMED 1354266 REFERENCE 3 (residues 1 to 392) AUTHORS LYNEN,F. and OCHOA,S. TITLE Enzymes of fatty acid metabolism JOURNAL Biochim Biophys Acta 12 (1-2), 299-314 (1953) PUBMED 13115439 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 11481662 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..392 /organism="Salmonella" /db_xref="taxon:590" Protein 1..392 /product="acetyl-CoA C-acetyltransferase" /EC_number="2.3.1.9" /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase activity [Evidence IEA]" /calculated_mol_wt=40779 Region 1..392 /region_name="PRK05790" /note="putative acyltransferase; Provisional" /db_xref="CDD:180261" ORIGIN 1 mkevvivgal rtpigcfqgt larhsavelg smvvkalier tgvdanaide vilgqvltag 61 agqnparqsa ikgglpttvs aitindvcgs glkalhlatq aiqcgeadiv iaggqenmsr 121 aphvlndsrs galpdadnlv dslvhdglwd afndyhigvt aenlareygi srelqdayal 181 ssqqkaraai dtgrfkdeiv pivtqrngqt aivdtdeqpr adasaeglal lhpafdslgs 241 vtagnassin dgaaavmmms eakaqalglp vlarirafas vgvdpalmgi apvyatrrcl 301 eragwqltev dlieaneafa aqalsvgkml ewderrvnvn ggaialghpi gasgcrilvs 361 lvhemvkrda rkglatlcig ggqgvaltie rd