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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Bacillus anthracis and UniProt Accession Q81JG6

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IUBMB Comments
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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Bacillus anthracis
UNIPROT: Q81JG6
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Word Map
The taxonomic range for the selected organisms is: Bacillus anthracis
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-ketoacyl reductase, fabg1, beta-ketoacyl-acp reductase, fabg4, 3-oxoacyl-acp reductase, fabg3, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-acp reductase, fabg2, oar1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-oxoacyl-(acyl carrier protein) reductase
Q81JG6
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3-ketoacyl acyl carrier protein reductase
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3-ketoacyl-acyl carrier protein reductase
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3-oxoacyl-[ACP]reductase
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beta-ketoacyl acyl carrier protein (ACP) reductase
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beta-ketoacyl reductase
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beta-ketoacyl thioester reductase
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beta-ketoacyl-ACP reductase
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beta-ketoacyl-acyl carrier protein reductase
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beta-ketoacyl-[acyl-carrier protein] (ACP) reductase
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NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
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reductase, 3-oxoacyl-[acyl carrier protein]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-34-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Q81JG6
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
Q81JG6
diffraction to 2.4 A. Final model contains two tetramers displaying 222 symmetry and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
Q81JG6
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by nickel-affinity chromatography
Q81JG6
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q81JG6
PCR product recombined with pDONR221 and insert from this vector transferred in the LR reaction to the expression vector pET15g which adds a histidine tag and a 3C protease cleavage site, expressed in Escherichia coli B834(DE3) cells
Q81JG6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zaccai, N.R.; Carter, L.G.; Berrow, N.S.; Sainsbury, S.; Nettleship, J.E.; Walter, T.S.; Harlos, K.; Owens, R.J.; Wilson, K.S.; Stuart, D.I.; Esnouf, R.M.
Crystal structure of a 3-oxoacyl-(acyl carrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-.ANG. resolution
Proteins Struct. Funct. Bioinform.
70
562-567
2007
Bacillus anthracis (Q81JG6)
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Manually annotated by BRENDA team
Zaccai, N.; Carter, L.; Berrow, N.; Sainsbury, S.; Nettleship, J.; Walter, T.; Harlos, K.; Owens, R.; Wilson, K.; Stuart, D.; Esnouf, R.
Crystal structure of a 3-oxoacyl-(acyl carrier protein) reductase (BA3989) from Bacillus anthracis at 2.4 A resolution
Proteins Struct. Funct. Genet.
70
562-567
2008
Bacillus anthracis (Q81JG6)
Manually annotated by BRENDA team