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Information on EC 2.3.1.16 - acetyl-CoA C-acyltransferase and Organism(s) Pseudomonas fragi and UniProt Accession P28790

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EC Tree
IUBMB Comments
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
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This record set is specific for:
Pseudomonas fragi
UNIPROT: P28790
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas fragi
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
elovl6, elovl5, 3-ketoacyl-coa thiolase, beta-ketothiolase, 3-oxoacyl-coa thiolase, acaa2, 3-ketothiolase, elovl-6, thiolase i, thiolase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-ketoacyl CoA thiolase
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3-ketoacyl coenzyme A thiolase
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3-ketoacyl thiolase
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3-ketoacyl-CoA thiolase
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3-ketothiolase
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3-oxoacyl-CoA thiolase
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3-oxoacyl-coenzyme A thiolase
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6-oxoacyl-CoA thiolase
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acetoacetyl-CoA beta-ketothiolase
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acetyl-CoA acyltransferase
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acyltransferase, acetyl coenzyme A
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beta-ketoacyl coenzyme A thiolase
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beta-ketoacyl-CoA thiolase
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beta-ketoadipyl coenzyme A thiolase
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beta-ketoadipyl-CoA thiolase
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beta-ketothiolase
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KAT
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ketoacyl-CoA acyltransferase
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ketoacyl-coenzyme A thiolase
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long-chain 3-oxoacyl-CoA thiolase
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oxoacyl-coenzyme A thiolase
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pro-3-ketoacyl-CoA thiolase
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SCP2/3-oxoacyl-CoA thiolase
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thiloase B
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thiolase A
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thiolase I
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thiolase II
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thiolase III
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multifunctional enzyme: 2-enoyl-CoA hydratase, 3-ketoacyl-CoA thiolase, 3-hydroxyacyl-CoA dehydrogenase
acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
show the reaction diagram
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:acetyl-CoA C-acyltransferase
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. In the second step the acyl group is transferred to CoA. Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. cf. EC 2.3.1.9, acetyl-CoA C-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-97-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
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?
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA + 3-oxoacyl-CoA
acyl-CoA + acetyl-CoA
show the reaction diagram
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pI: 4.9
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B-0771
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FADA_PSEFR
391
0
41606
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
240000
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multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, gel filtration
42000
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2 * 73000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, SDS-PAGE
73000
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2 * 73000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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2 * 73000 + 2 * 42000, multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16, SDS-PAGE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
multienzyme complex: EC 4.2.1.17, EC 1.1.1.35, EC 5.3.3.3, EC 5.1.2.3, EC 2.3.1.16
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imamura, S.; Ueda, S.; Mizugaki, M.; Kawaguchi, A.
Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of the fatty acid oxidation system
J. Biochem.
107
184-189
1990
Pseudomonas fragi
Manually annotated by BRENDA team
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.
111
8-15
1992
Pseudomonas fragi (P28790), Pseudomonas fragi, Pseudomonas fragi B-0771 (P28790), Pseudomonas fragi B-0771
Manually annotated by BRENDA team