EzCatDB: S00328
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DB codeS00328
RLCP classification9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : 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,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,D00545,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

P0AEK2C3NP04Q9KQH7Q9RPT1Q5NF68Q2YMG6P50941Q3JQ67P0A5Y4O67610Q81JG6P0A0H9A3DDY9
Protein name3-oxoacyl-[acyl-carrier-protein] reductase
3-oxoacyl-[acyl-carrier-protein] reductaseRhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase

3-oxoacyl-[acyl-carrier-protein] reductase
3-oxoacyl-[acyl-carrier-protein] reductase3-oxoacyl-[acyl-carrier-protein] reductase
3-oxoacyl-[acyl-carrier-protein] reductase
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
SynonymsEC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
NoneEC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
EC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
3-oxoacyl-(Acyl-carrier-protein) reductase
EC 1.1.1.100
Short-chain dehydrogenase/reductase SDR:Glucose/ribitol dehydrogenase
EC 1.1.1.100
EC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
3-oxoacyl-(Acyl-carrier-protein) reductase
EC 1.1.1.100
EC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
EC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
3-oxoacyl-(Acyl-carrier-protein) reductase
EC 1.1.1.100
3-ketoacyl-acyl carrier protein reductase
3-oxoacyl-[acyl-carrier-protein] reductase
EC 1.1.1.100
RefSeqNP_415611.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489361.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
YP_002878083.1 (Protein)
NC_012668.1 (DNA/RNA sequence)
NP_231655.1 (Protein)
NC_002505.1 (DNA/RNA sequence)
NP_252077.1 (Protein)
NC_002516.2 (DNA/RNA sequence)
YP_170324.1 (Protein)
NC_006570.2 (DNA/RNA sequence)
YP_413943.1 (Protein)
NC_007618.1 (DNA/RNA sequence)
NP_221114.1 (Protein)
NC_000963.1 (DNA/RNA sequence)
YP_334286.1 (Protein)
NC_007434.1 (DNA/RNA sequence)
NP_215999.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
NP_335981.1 (Protein)
NC_002755.2 (DNA/RNA sequence)
YP_006514867.1 (Protein)
NC_018143.1 (DNA/RNA sequence)
NP_214176.1 (Protein)
NC_000918.1 (DNA/RNA sequence)
NP_846231.1 (Protein)
NC_003997.3 (DNA/RNA sequence)
YP_020629.1 (Protein)
NC_007530.2 (DNA/RNA sequence)
YP_029953.1 (Protein)
NC_005945.1 (DNA/RNA sequence)
NP_371755.1 (Protein)
NC_002758.2 (DNA/RNA sequence)
YP_001037361.1 (Protein)
NC_009012.1 (DNA/RNA sequence)
PfamPF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]

PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]

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

UniProtKB:Accession NumberP0AEK2C3NP04Q9KQH7Q9RPT1Q5NF68Q2YMG6P50941Q3JQ67P0A5Y4O67610Q81JG6P0A0H9A3DDY9
Entry nameFABG_ECOLIC3NP04_VIBCJFABG_VIBCHRHLG_PSEAEQ5NF68_FRATTQ2YMG6_BRUA2FABG_RICPRQ3JQ67_BURP1FABG_MYCTUFABG_AQUAEQ81JG6_BACANFABG_STAAMA3DDY9_CLOTH
Activity(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
SubunitHomotetramer.
Homotetramer (By similarity).


Homotetramer.
Homotetramer.Homotetramer.
Homotetramer.
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

             
1i01AUnboundUnbound UnboundUnbound
1i01BUnboundUnbound UnboundUnbound
1i01CUnboundUnbound UnboundUnbound
1i01DUnboundUnbound UnboundUnbound
1i01EUnboundUnbound UnboundUnbound
1i01FUnboundUnbound UnboundUnbound
1i01GUnboundUnbound UnboundUnbound
1i01HUnboundUnbound UnboundUnbound
1q7bAUnboundUnbound Bound:NAPUnbound
1q7bBUnboundUnbound Bound:NAPUnbound
1q7bCUnboundUnbound Bound:NAPUnbound
1q7bDUnboundUnbound Bound:NAPUnbound
1q7cAUnboundUnbound Bound:NAPUnbound
1q7cBUnboundUnbound Bound:NAPUnbound
3op4AUnboundAnalogue:ACT Bound:NAPUnbound
3op4BUnboundAnalogue:ACT Bound:NAPUnbound
3rroAUnboundUnbound UnboundUnbound
3rroBUnboundUnbound UnboundUnbound
3rshAUnboundUnbound Bound:NAPUnbound
3rshBUnboundUnbound Bound:NAPUnbound
2b4qAUnboundUnbound Bound:NAPUnbound
2b4qBUnboundUnbound UnboundUnbound
3lylAUnboundUnbound UnboundUnbound
3lylBUnboundUnbound UnboundUnbound
3lylCUnboundUnbound UnboundUnbound
3lylDUnboundUnbound UnboundUnbound
3emkAUnboundUnbound UnboundUnbound
3emkBUnboundUnbound UnboundUnbound
3emkCUnboundUnbound UnboundUnbound
3emkDUnboundUnbound UnboundUnbound
3ennAUnboundUnbound UnboundUnbound
3ennBUnboundUnbound UnboundUnbound
3ennCUnboundUnbound UnboundUnbound
3ennDUnboundUnbound UnboundUnbound
3f9iAUnboundUnbound UnboundUnbound
3f9iBUnboundUnbound UnboundUnbound
3ftpAUnboundUnbound UnboundUnbound
3ftpBUnboundUnbound UnboundUnbound
3ftpCUnboundUnbound UnboundUnbound
3ftpDUnboundUnbound UnboundUnbound
1uzlAUnboundUnbound UnboundUnbound
1uzlBUnboundUnbound UnboundUnbound
1uzmAUnboundUnbound UnboundUnbound
1uzmBUnboundUnbound UnboundUnbound
1uznAUnboundUnbound Analogue:NAPUnbound
1uznBUnboundUnbound UnboundUnbound
2ntnAUnboundUnbound UnboundUnbound
2ntnBUnboundUnbound UnboundUnbound
2p68AUnboundUnbound UnboundUnbound
2p68BUnboundUnbound UnboundUnbound
2pnfAUnboundUnbound UnboundUnbound
2pnfBUnboundUnbound UnboundUnbound
2uvdAUnboundUnbound UnboundUnbound
2uvdBUnboundUnbound UnboundUnbound
2uvdCUnboundUnbound UnboundUnbound
2uvdDUnboundUnbound UnboundUnbound
2uvdEUnboundUnbound UnboundUnbound
2uvdFUnboundUnbound UnboundUnbound
2uvdGUnboundUnbound UnboundUnbound
2uvdHUnboundUnbound UnboundUnbound
3osuAUnboundUnbound UnboundUnbound
3osuBUnboundUnbound UnboundUnbound
2hq1AUnboundUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;P0AEK2 & literature [14]
pdbCatalytic residuescomment
          
1i01ASER 138;       ;LYS 155
invisible Y151
1i01BSER 138;TYR 151;LYS 155
 
1i01CSER 138;TYR 151;LYS 155
 
1i01DSER 138;TYR 151;LYS 155
 
1i01ESER 138;TYR 151;LYS 155
 
1i01FSER 138;       ;LYS 155
invisible Y151
1i01G       ;TYR 151;LYS 155
invisible S138
1i01H       ;TYR 151;LYS 155
invisible S138
1q7bASER 138;TYR 151;LYS 155
 
1q7bBSER 138;TYR 151;LYS 155
 
1q7bCSER 138;TYR 151;LYS 155
 
1q7bDSER 138;TYR 151;LYS 155
 
1q7cASER 138;       ;LYS 155
mutant Y151F
1q7cBSER 138;       ;LYS 155
mutant Y151F
3op4ASER 142;TYR 155;LYS 159
 
3op4BSER 142;TYR 155;LYS 159
 
3rroASER 142;TYR 155;LYS 159
 
3rroBSER 142;TYR 155;LYS 159
 
3rshASER 142;TYR 155;LYS 159
invisible 195-197
3rshBSER 142;TYR 155;LYS 159
invisible 195
2b4qASER 148;TYR 162;LYS 166
 
2b4qBSER 148;TYR 162;LYS 166
 
3lylASER 141;TYR 154;LYS 158
 
3lylBSER 141;TYR 154;LYS 158
 
3lylCSER 141;TYR 154;LYS 158
 
3lylDSER 141;TYR 154;LYS 158
 
3emkASER 139;TYR 152;LYS 156
invisible 190-194
3emkBSER 139;TYR 152;LYS 156
invisible 186-197
3emkCSER 139;TYR 152;LYS 156
invisible 185-194
3emkDSER 139;TYR 152;LYS 156
invisible 187-194
3ennASER 139;TYR 152;LYS 156
invisible 188-195
3ennBSER 139;TYR 152;LYS 156
invisible 188-193
3ennCSER 139;TYR 152;LYS 156
invisible 187-197
3ennDSER 139;TYR 152;LYS 156
invisible 187-197
3f9iASER 135;TYR 148;LYS 152
invisible 86-98, 139-140, 183-188
3f9iBSER 135;TYR 148;LYS 152
invisible 88-98, 140
3ftpASER 143;TYR 156;LYS 160
 
3ftpBSER 143;TYR 156;LYS 160
 
3ftpCSER 143;TYR 156;LYS 160
 
3ftpDSER 143;TYR 156;LYS 160
 
1uzlASER 140;TYR 153;LYS 157
invisible 95-99, 147-149
1uzlBSER 140;TYR 153;LYS 157
 
1uzmASER 140;TYR 153;LYS 157
invisible 94-98, 144-148
1uzmBSER 140;TYR 153;LYS 157
invisible 94-99, 143-149
1uznASER 140;TYR 153;LYS 157
 
1uznBSER 140;TYR 153;LYS 157
invisible 189-201
2ntnASER 140;TYR 153;LYS 157
invisible 92-99, 142-149, 196-198
2ntnBSER 140;TYR 153;LYS 157
invisible 92-99, 142-149, 189-202
2p68ASER 144;TYR 157;LYS 161
 
2p68BSER 144;TYR 157;LYS 161
invisible 199-203
2pnfASER 144;TYR 157;LYS 161
 
2pnfBSER 144;TYR 157;LYS 161
 
2uvdASER 141;TYR 154;LYS 158
 
2uvdBSER 141;TYR 154;LYS 158
 
2uvdCSER 141;TYR 154;LYS 158
 
2uvdDSER 141;TYR 154;LYS 158
 
2uvdESER 141;TYR 154;LYS 158
 
2uvdFSER 141;TYR 154;LYS 158
 
2uvdGSER 141;TYR 154;LYS 158
 
2uvdHSER 141;TYR 154;LYS 158
 
3osuASER 141;TYR 154;LYS 158
 
3osuBSER 141;TYR 154;LYS 158
 
2hq1ASER 142;TYR 155;LYS 159
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig.3, p.342
[13]p.458-459
[14]Fig.7, p.424-425
[17]Fig.2, p.566

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.
Related PDB1uzl,1uzm,1unz
[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 ID16624803
JournalJ Biol Chem
Year2006
Volume281
Pages18025-32
AuthorsMiller DJ, Zhang YM, Rock CO, White SW
TitleStructure of RhlG, an essential beta-ketoacyl reductase in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa.
Related PDB2b4q
[16]
PubMed ID17642518
JournalActa Crystallogr D Biol Crystallogr
Year2007
Volume63
Pages923-5
AuthorsPoncet-Montange G, Ducasse-Cabanot S, Quemard A, Labesse G, Cohen-Gonsaud M
TitleLack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
Related PDB2ntn
[17]
PubMed ID17894349
JournalProteins
Year2008
Volume70
Pages562-7
AuthorsZaccai NR, Carter LG, Berrow NS, Sainsbury S, Nettleship JE, Walter TS, Harlos K, Owens RJ, Wilson KS, Stuart DI, Esnouf RM
TitleCrystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution.
Related PDB2uvd

comments
Although this enzyme binds calcium ions, it is not involved in catalysis.
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
2004-05-122012-06-01


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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