ID   FABG6_BRANA             Reviewed;         201 AA.
AC   P27582;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 3.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE   Flags: Fragments;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   PROTEIN SEQUENCE OF 35-62 AND 81-84.
RC   TISSUE=Seed;
RX   PubMed=1562581; DOI=10.1016/0167-4838(92)90263-d;
RA   Sheldon P.S., Kekwick R.G.O., Smith C.G., Sidebottom C.M., Slabas A.R.;
RT   "3-oxoacyl-[ACP] reductase from oilseed rape (Brassica napus).";
RL   Biochim. Biophys. Acta 1120:151-159(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-201, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=1575676; DOI=10.1042/bj2830321;
RA   Slabas A.R., Chase D., Nishida I., Murata N., Sidebottom C.M., Safford R.,
RA   Sheldon P.S., Kekwick R.G.O., Hardie D.G., Mackintosh R.W.;
RT   "Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein)
RT   reductase. Sequence identities with the nodG-gene product of the nitrogen-
RT   fixing soil bacterium Rhizobium meliloti.";
RL   Biochem. J. 283:321-326(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Note=And non-photosynthetic
CC       plastids.
CC   -!- TISSUE SPECIFICITY: Embryo and leaf tissues.
CC   -!- MISCELLANEOUS: Exhibits a marked preference for acyl-carrier protein
CC       derivatives over CoA derivatives as substrates.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; X64463; CAA45793.1; -; mRNA.
DR   PIR; S22417; S22417.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP;
KW   Oxidoreductase; Plastid.
FT   CHAIN           1..201
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT                   /id="PRO_0000054661"
FT   ACT_SITE        108
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000305"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000305"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  21047 MW;  FD51B2E369D2D967 CRC64;
     ATAQEQPEGE APDKVESPVV XXXEAXIVLV NYAREADVDA MMKDAVDYWG QIDVIANNAG
     ITVIALNLTG VFLCSQAATK IMMKKRKGRI INIASVVGLI GNIGQANYAA AKAGVIGFSK
     TAAREGASRN INVNVVCPGF IASEMTAKLG EDMEKKILGT IPLGRYGQPE DVAGLVEFLA
     LSPAASYITG QTFTIDGGIA I
//