EzCatDB: D00545
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DB codeD00545
RLCP classification9.5010.536200.8010 : Hydride transfer
CATH domainDomain 1-.-.-.-
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.100

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

Q8I2S7
Protein name
3-oxoacyl-[acyl-carrier-protein] reductase
beta-ketoacyl-[acyl-carrier protein](ACP) reductase
beta-ketoacyl acyl carrier protein (ACP) reductase
beta-ketoacyl reductase
beta-ketoacyl thioester reductase
beta-ketoacyl-ACP reductase
beta-ketoacyl-acyl carrier protein reductase
3-ketoacyl acyl carrier protein reductase
NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
3-oxoacyl-[ACP]reductase
(3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase
Synonyms3-oxoacyl-(Acyl-carrier protein) reductase, putative
EC 1.1.1.100
RefSeqXP_001352100.1 (Protein)
XM_001352064.1 (DNA/RNA sequence)
PfamPF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis
MAP01040Biosynthesis of unsaturated fatty acids

UniProtKB:Accession NumberQ8I2S7
Entry nameQ8I2S7_PLAF7
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00005C00685C00080C00006C01271
CompoundNADPH3-Oxoacyl-[acyl-carrier protein]H+NADP+(3R)-3-Hydroxyacyl-[acyl-carrier protein]
Typeamide group,amine group,nucleotidecarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide groupothersamide group,amine group,nucleotidecarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group
ChEBI16474

15378
18009

PubChem5884

1038
5886

             
2c07AUnboundUnbound UnboundUnbound

Active-site residues
resource
literature [15]
pdbCatalytic residuescomment
          
2c07ASER 199;TYR 212;LYS 216
invisible 248-252

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig.3b, p.342
[13]p.458-459
[14]Fig.7B, p.424-425

references
[1]
PubMed ID6756317
JournalArch Biochem Biophys
Year1982
Volume218
Pages77-91
AuthorsShimakata T, Stumpf PK
TitlePurification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves.
[2]
PubMed ID1562581
JournalBiochim Biophys Acta
Year1992
Volume1120
Pages151-9
AuthorsSheldon PS, Kekwick RG, Smith CG, Sidebottom C, Slabas AR
Title3-Oxoacyl-[ACP] reductase from oilseed rape (Brassica napus).
[3]
PubMed ID8550484
JournalJ Bacteriol
Year1996
Volume178
Pages571-3
AuthorsShen Z, Byers DM
TitleIsolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and fabF genes involved in fatty acid biosynthesis.
[4]
PubMed ID9342868
JournalPlant Physiol
Year1997
Volume115
Pages501-10
AuthorsXu X, Dietrich CR, Delledonne M, Xia Y, Wen TJ, Robertson DS, Nikolau BJ, Schnable PS
TitleSequence analysis of the cloned glossy8 gene of maize suggests that it may code for a beta-ketoacyl reductase required for the biosynthesis of cuticular waxes.
[5]
PubMed ID9761917
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages427-9
AuthorsRafferty JB, Fisher M, Langridge SJ, Martindale W, Thomas NC, Simon JW, Bithell S, Slabas AR, Rice DW
TitleCrystallization of the NADP-dependent beta-keto acyl carrier protein reductase from Escherichia coli.
[6]
PubMed ID10666637
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages86-8
AuthorsFisher M, Sedelnikova SE, Martindale W, Thomas NC, Simon JW, Slabas AR, Rafferty JB
TitleCrystallization of the NADP-dependent beta-keto acyl-carrier protein reductase from Brassica napus.
[7]
PubMed ID10747933
JournalJ Biol Chem
Year2000
Volume275
Pages16857-64
AuthorsKremer L, Douglas JD, Baulard AR, Morehouse C, Guy MR, Alland D, Dover LG, Lakey JH, Jacobs WR Jr, Brennan PJ, Minnikin DE, Besra GS
TitleThiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis.
[8]
PubMed ID10801480
JournalStructure Fold Des
Year2000
Volume8
Pages339-47
AuthorsFisher M, Kroon JT, Martindale W, Stuitje AR, Slabas AR, Rafferty JB
TitleThe X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed ID11669613
JournalBiochemistry
Year2001
Volume40
Pages12772-81
AuthorsPrice AC, Zhang YM, Rock CO, White SW
TitleStructure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Related PDB1i01
Related UniProtKBP0AEK2
[10]
PubMed ID12079383
JournalJ Mol Biol
Year2002
Volume320
Pages249-61
AuthorsCohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A
TitleCrystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.
[11]
PubMed ID11932442
JournalMicrobiology
Year2002
Volume148
Pages951-60
AuthorsMarrakchi H, Ducasse S, Labesse G, Montrozier H, Margeat E, Emorine L, Charpentier X, Daffe M, Quemard A
TitleMabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II.
[12]
PubMed ID14527946
JournalJ Biol Chem
Year2003
Volume278
Pages52935-43
AuthorsZhang YM, Wu B, Zheng J, Rock CO
TitleKey residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.
[13]
PubMed ID12524453
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages455-60
AuthorsYang JK, Park MS, Waldo GS, Suh SW
TitleDirected evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis.
[14]
CommentsX-ray crystallography
PubMed ID15016358
JournalStructure (Camb)
Year2004
Volume12
Pages417-28
AuthorsPrice AC, Zhang YM, Rock CO, White SW
TitleCofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.
Related PDB1q7b,1q7c
[15]
PubMed ID16225460
JournalBiochem J
Year2006
Volume393
Pages447-57
AuthorsWickramasinghe SR, Inglis KA, Urch JE, Muller S, van Aalten DM, Fairlamb AH
TitleKinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis.
Related PDB2c07

comments
This enzyme is homologous to the counterpart enzymes from other bacteria (S00328 in EzCatDB).
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys. The conformation of these residues seems to be similar to that of the homologous enzymes. Thus, the catalytic site seems to catalyze the following reaction.
(A) Hydride transfer from NADPH to keto-substrate (Reduction):

createdupdated
2011-07-082012-06-01
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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