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InterPro: IPR011284 3-oxoacyl-(acyl-carrier-protein) reductase

Protein matchesHelp
UniProtKB
Matches:
1486 proteins
AccessionHelp IPR011284 3oxo_ACP_reduc
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR002347 Glucose/ribitol dehydrogenase
Contains IPR016040 NAD(P)-binding domain
IPR020904 Short-chain dehydrogenase/reductase, conserved site
GO Term annotationHelp
Process GO:0006633 fatty acid biosynthetic process
GO:0055114 oxidation reduction
Function GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase activity
GO:0051287 NAD or NADH binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis found in many plant and bacterial species. This enzyme is involved in type II fatty acid biosynthesis, where the individual metabolic transformations are carried out by different enzymes rather than by a single enzyme as occurs in type I fatty acid biosynthesis [1].

Structural studies show that the enzyme is a tetramer which forms a typical Rossman fold [2, 3]. Unlike other members of the short-chain dehydrogenase/reductase superfamily, the enzyme undergoes a marked conformational change upon binding of the NADP(H)cofactor. This conformational change aligns the side chains of the catalytic triad at the active site in an active conformation and increases the affinity of the enzyme for its substrate.

Structural linksHelp
SCOP: c.2.1.2
CATH: 3.40.50.720
Database linksHelp
Enzyme: EC:1.1.1.100

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011284 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O67610 3-oxoacyl-[acyl-carrier-protein] reductase

P33207 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic

P73574 3-oxoacyl-[acyl-carrier-protein] reductase 1

Q93X62 3-oxoacyl-[acyl-carrier-protein] reductase 1, chloroplastic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR020904 Short-chain dehydrogenase/reductase, conserved site
IPR011284 3-oxoacyl-(acyl-carrier-protein) reductase
IPR016040 NAD(P)-binding domain
IPR002347 Glucose/ribitol dehydrogenase
IPR002198 Short-chain dehydrogenase/reductase SDR
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Campbell JW, Cronan JE Jr.
Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery.
Annu. Rev. Microbiol. 55 305-32 2001 [PubMed: 11544358]
http://dx.doi.org/10.1146/annurev.micro.55.1.305
2. Price AC, Zhang YM, Rock CO, White SW.
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Biochemistry 40 12772-81 2001 [PubMed: 11669613]
http://dx.doi.org/10.1021/bi010737g
3. Wickramasinghe SR, Inglis KA, Urch JE, Muller S, van Aalten DM, Fairlamb AH.
Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis.
Biochem. J. 393 447-57 2006 [PubMed: 16225460]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=16225460&action=stream&blobtype=pdf

Additional ReadingHelp
Poncet-Montange G, Ducasse-Cabanot S, Quemard A, Labesse G, Cohen-Gonsaud M.
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 923-5 [PubMed: 17642518]
http://dx.doi.org/10.1107/S0907444907024158
Zaccai NR, Carter LG, Berrow NS, Sainsbury S, Nettleship JE, Walter TS, Harlos K, Owens RJ, Wilson KS, Stuart DI, Esnouf RM.
Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution.
Proteins 70 2008 562-7 [PubMed: 17894349]
http://dx.doi.org/10.1002/prot.21624
Mao Q, Duax WL, Umland TC.
Crystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 106-9 [PubMed: 17277451]
Tang Y, Lee HY, Tang Y, Kim CY, Mathews I, Khosla C.
Structural and functional studies on SCO1815: a beta-ketoacyl-acyl carrier protein reductase from Streptomyces coelicolor A3(2).
Biochemistry 45 2006 14085-93 [PubMed: 17115703]
http://dx.doi.org/10.1021/bi061187v
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InterPro 23.1