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Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase and Organism(s) Haloferax mediterranei and UniProt Accession I3R3D1

for references in articles please use BRENDA:EC2.3.1.9
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EC Tree
IUBMB Comments
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
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This record set is specific for:
Haloferax mediterranei
UNIPROT: I3R3D1 not found.
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Word Map
The taxonomic range for the selected organisms is: Haloferax mediterranei
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
acetoacetyl-coa thiolase, acetyl-coa acetyltransferase, erg10, acoat, acetyl-coa c-acetyltransferase, cytosolic acetoacetyl-coa thiolase, 2-methylacetoacetyl-coa thiolase, osat1, acetoacetyl coa thiolase, aact2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-methylacetoacetyl-CoA thiolase
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3-oxothiolase
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acetoacetyl CoA thiolase
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acetoacetyl-CoA thiolase
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acetyl coenzyme A thiolase
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acetyl-CoA acetyltransferase
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acetyl-CoA:N-acetyltransferase
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acetyltransferase, acetyl coenzyme A
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beta-acetoacetyl coenzyme A thiolase
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HFX_1022
I3R3D1; I3R3D0
locus name, subunit PhaAbeta
HFX_1023
I3R3D1; I3R3D0
locus name, subunit PhaAalpha
HFX_6003
I3RA72; I3RA71
locus name, subunit BktBbeta
HFX_6004
I3RA72; I3RA71
locus name, subunit BktBalpha
thiolase II
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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condensation
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thiolytic cleavage
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-46-7
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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
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
show the reaction diagram
I3R3D1; I3R3D0, I3RA72; I3RA71
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?
additional information
?
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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
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
I3R3D1; I3R3D0, I3RA72; I3RA71
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
I3R3D1; I3R3D0, I3RA72; I3RA71
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F6JY46_HALME
383
0
40444
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
I3R3D1; I3R3D0, I3RA72; I3RA71
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
I3R3D1; I3R3D0, I3RA72; I3RA71
the enzyme has biotechnological potential in haloarchaea for production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) with controllable 3-oxopentano content, from unrelated cheap carbon sources
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hou, J.; Feng, B.; Han, J.; Liu, H.; Zhao, D.; Zhou, J.; Xiang, H.
Haloarchaeal-type beta-ketothiolases involved in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in Haloferax mediterranei
Appl. Environ. Microbiol.
79
5104-5111
2013
Haloferax mediterranei (I3R3D1 and I3R3D0), Haloferax mediterranei (I3RA72 and I3RA71), Haloferax mediterranei, Haloferax mediterranei DSM 1411 (I3R3D1 and I3R3D0), Haloferax mediterranei DSM 1411 (I3RA72 and I3RA71)
Manually annotated by BRENDA team