DB code: S00553

RLCP classification 9.5010.536200.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.100
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 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 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q53WH2
3-oxoacyl-[acyl carrier protein] reductase
YP_145259.1 (Protein)
NC_006462.1 (DNA/RNA sequence)
PF00106 (adh_short)
[Graphical View]

KEGG enzyme 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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q53WH2 Q53WH2_THET8

KEGG Pathways
Map code Pathways E.C.
MAP00061 Fatty acid biosynthesis
MAP01040 Biosynthesis of unsaturated fatty acids

Compound table
Substrates Products Intermediates
KEGG-id C00005 C00685 C00080 C00006 C01271
E.C.
Compound NADPH 3-Oxoacyl-[acyl-carrier protein] H+ NADP+ (3R)-3-Hydroxyacyl-[acyl-carrier protein]
Type amide group,amine group,nucleotide carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group others amide group,amine group,nucleotide carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group
ChEBI 16474
 16474
 		15378
 15378
 		18009
 18009
PubChem 5884
 5884
 		1038
 1038
 		5886
 5886
2a4kA Unbound Unbound Unbound Unbound
2a4kB Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2a4kA SER 137;TYR 149;LYS 153 invisible 96-99
2a4kB ; ;LYS 153 invisible 92-103, 137-152, 184-193

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[8]
Fig.3b, p.342
[13]
p.458-459
[14]
Fig.7B, p.424-425

References
[1]
Resource
Comments
Medline ID
PubMed ID 6756317
Journal Arch Biochem Biophys
Year 1982
Volume 218
Pages 77-91
Authors Shimakata T, Stumpf PK
Title Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1562581
Journal Biochim Biophys Acta
Year 1992
Volume 1120
Pages 151-9
Authors Sheldon PS, Kekwick RG, Smith CG, Sidebottom C, Slabas AR
Title 3-Oxoacyl-[ACP] reductase from oilseed rape (Brassica napus).
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8550484
Journal J Bacteriol
Year 1996
Volume 178
Pages 571-3
Authors Shen Z, Byers DM
Title Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and fabF genes involved in fatty acid biosynthesis.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9342868
Journal Plant Physiol
Year 1997
Volume 115
Pages 501-10
Authors Xu X, Dietrich CR, Delledonne M, Xia Y, Wen TJ, Robertson DS, Nikolau BJ, Schnable PS
Title Sequence 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.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9761917
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 427-9
Authors Rafferty JB, Fisher M, Langridge SJ, Martindale W, Thomas NC, Simon JW, Bithell S, Slabas AR, Rice DW
Title Crystallization of the NADP-dependent beta-keto acyl carrier protein reductase from Escherichia coli.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10666637
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 86-8
Authors Fisher M, Sedelnikova SE, Martindale W, Thomas NC, Simon JW, Slabas AR, Rafferty JB
Title Crystallization of the NADP-dependent beta-keto acyl-carrier protein reductase from Brassica napus.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10747933
Journal J Biol Chem
Year 2000
Volume 275
Pages 16857-64
Authors Kremer L, Douglas JD, Baulard AR, Morehouse C, Guy MR, Alland D, Dover LG, Lakey JH, Jacobs WR Jr, Brennan PJ, Minnikin DE, Besra GS
Title Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10801480
Journal Structure Fold Des
Year 2000
Volume 8
Pages 339-47
Authors Fisher M, Kroon JT, Martindale W, Stuitje AR, Slabas AR, Rafferty JB
Title The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID
PubMed ID 11669613
Journal Biochemistry
Year 2001
Volume 40
Pages 12772-81
Authors Price AC, Zhang YM, Rock CO, White SW
Title Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Related PDB 1i01
Related UniProtKB P0AEK2
[10]
Resource
Comments
Medline ID
PubMed ID 12079383
Journal J Mol Biol
Year 2002
Volume 320
Pages 249-61
Authors Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A
Title Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11932442
Journal Microbiology
Year 2002
Volume 148
Pages 951-60
Authors Marrakchi H, Ducasse S, Labesse G, Montrozier H, Margeat E, Emorine L, Charpentier X, Daffe M, Quemard A
Title MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 14527946
Journal J Biol Chem
Year 2003
Volume 278
Pages 52935-43
Authors Zhang YM, Wu B, Zheng J, Rock CO
Title Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12524453
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 455-60
Authors Yang JK, Park MS, Waldo GS, Suh SW
Title Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15016358
Journal Structure (Camb)
Year 2004
Volume 12
Pages 417-28
Authors Price AC, Zhang YM, Rock CO, White SW
Title Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.
Related PDB 1q7b 1q7c
Related UniProtKB

Comments
This enzyme is homologous to the counterpart enzymes from other bacteria (S00328 in EzCatDB). This enzyme has a slightly longer chain than the homologue in the C-terminus.
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):

Created Updated
2011-07-08 2012-06-01