3-ketoacyl-CoA thiolase

Details

Name
3-ketoacyl-CoA thiolase
Synonyms
  • 2.3.1.16
  • Acetyl-CoA acyltransferase
  • Beta-ketothiolase
  • faoB
  • Fatty acid oxidation complex subunit beta
Gene Name
fadA
Organism
Pseudomonas fragi
Amino acid sequence
>lcl|BSEQ0017385|3-ketoacyl-CoA thiolase
MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKVLERNSKVDPGEVEDVIWG
CVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSALHTAAQAIMTGNGDVFVVG
GVEHMGHVSMMHGVDPNPHMSLYAAKASGMMGLTAEMLGKMHGISREQQDAFAVRSHQLA
HKATVEGKFKDEIIPMQGYDENGFLKIFDYDETIRPDTTLESLAALKPAFNPKGGTVTAG
TSSQITDGASCMIVMSAQRAKDLGLEPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAG
LNMADIDFIELNEAFAAQALPVLKDLKVLDKMNEKVNLHGGAIALGHPFGCSGARISGTL
LNVMKQNGGTFGLSTMCIGLGQGIATVFERV
Number of residues
391
Molecular Weight
41605.72
Theoretical pI
7.0
GO Classification
Functions
acetyl-CoA C-acyltransferase activity
Processes
fatty acid beta-oxidation
Components
cytoplasm
General Function
Acetyl-coa c-acyltransferase activity
Specific Function
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0008093|2148 bp
ATGATTTACGAAGGTAAAGCCATCACGGTTACGGCTCTTGAAAGTGGCATCGTCGAACTG
AAGTTCGACCTCAAGGGTGAGTCCGTCAACAAATTCAACCGTCTAACCCTGAACGAATTG
CGTCAGGCGGTAGATGCGATCAAGGCCGACGCTTCGGTCAAGGGTGTCATCGTTTCCAGC
GGTAAAGACGTATTTATCGTCGGCGCCGACATCACCGAATTCGTCGAAAACTTCAAGTTG
CCGGATGCCGAGCTGATTGCTGGCAACCTCGAAGCCAACAAGATCTTCAGCGATTTTGAA
GACCTCAATGTACCCACCGTCGCAGCCATCAATGGCATCGCGTTGGGCGGTGGCCTGGAA
ATGTGCCTGGCAGCCGACTTCCGGGTCATGGCCGACAGCGCCAAGATCGGCCTGCCGGAA
GTCAAACTGGGCATCTACCCGGGCTTTGGCGGCACCGTACGTCTGCCACGCCTGATCGGT
GTTGATAACGCGGTTGAGTGGATTGCCTCCGGCAAGGAAAACCGCGCAGAAGACGCTCTG
AAAGTCAGCGCCGTTGATGCTGTTGTCACTGCTGACAAGCTGGGCGCAGCTGCCCTGGAC
CTGATCAAGCGCGCCATCAGTGGCGAACTGGACTACAAGGCCAAGCGTCAGCCGAAGCTG
GAAAAACTCAAGCTCAACGCTATCGAACAAATGATGGCTTTCGAAACCGCCAAAGGTTTC
GTGGCTGGCCAGGCCGGCCCGAACTACCCGGCCCCGGTTGAAGCGATCAAGACCATCCAG
AAAGCCGCGAACTTCGGTCGTGACAAAGCCCTGGAAGTGGAAGCTGCAGGTTTCGCCAAG
CTGGCCAAAACCAGCGCCTCGAACTGCCTGATCGGCCTGTTCCTGAACGATCAGGAACTG
AAGAAAAAGGCCAAGGTCTACGACAAGATCGCCAAAGACGTGAAGCAGGCCGCCGTTCTG
GGCGCCGGCATCATGGGTGGCGGCATTGCCTATCAGTCGGCGTCCAAAGGCACGCCGATC
CTGATGAAGGACATCAACGAGCACGGTATCGAGCAGGGCCTGGCTGAAGCCGCCAAGCTG
CTGGTAGGTCGCGTTGATAAAGGTCGCATGACCCCGGCAAAAATGGCTGAAGTGCTGAAC
GGCATTCGTCCTACTCTGTCCTACGGCGATTTCGGCAACGTCGACCTGGTGGTCGAAGCG
GTTGTCGAGAACCCGAAGGTCAAGCAGGCCGTGTTGGCGGAAGTGGAAAACCACGTTCGC
GAAGACGCCATCCTCGCTTCCAACACCTCGACCATTTCCATCAGCTTGCTGGCCAAGGCC
CTCAAGCGTCCGGAAAACTTCGTCGGCATGCACTTCTTCAACCCGGTACACATGATGCCG
CTGGTTGAAGTGATCCGTGGCGAGAAGTCCAGCGACCTGGCCGTGGCCACCACCGTTGCC
TACGCCAAGAAAATGGGCAAGAACCCGATCGTGGTCAACGACTGCCCGGGCTTCCTGGTC
AACCGCGTACTGTTCCCGTACTTCGGCGGTTTCGCCAAGCTGGTCAGCGCCGGTGTCGAC
TTTGTGCGTATCGACAAAGTGATGGAAAAATTCGGCTGGCCGATGGGCCCGGCGTACCTG
ATGGACGTGGTCGGTATCGACACTGGCCACCACGGTCGCGACGTGATGGCTGAAGGCTTC
CCGGACCGCATGAAAGACGACCGCCGCTCGGCGATCGATGCGCTGTACGAGGCCAAGCGC
CTGGGTCAGAAGAACGGCAAGGGCTTCTACGCCTACGAGGCTGACAAAAAGGGCAAGCAG
AAGAAACTGGTTGATTCGAGCGTGCTTGAAGTGCTCAAACCAATCGTTTACGAGCAGCGC
GACGTGACCGACGAAGACATCATCAACTGGATGATGATCCCGCTGTGCCTGGAAACCGTG
CGTTGCCTGGAAGACGGTATCGTTGAAACTGCAGCCGAGGCCGATATGGGCCTGGTCTAC
GGCATTGGCTTCCCGCTGTTCCGTGGTGGCGCGCTGCGCTACATCGATTCGATCGGTGTT
GCAGAGTTCGTCGCCCTGGCCGATCAGTACGCTGAACTGGGCGCGCTGTACCACCCGACT
GCGAAGCTGCGTGAGATGGCCAAGAACGGCCAGAGCTTCTTCGGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP28790
UniProtKB Entry NameFADA_PSEFR
GenBank Protein ID391839
GenBank Gene IDD10390
General References
  1. Sato S, Hayashi M, Imamura S, Ozeki Y, Kawaguchi A: Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation. J Biochem. 1992 Jan;111(1):8-15. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB082493,6,9,12,15-PENTAOXATRICOSAN-1-OLexperimentalunknownDetails