ID   FABG2_BRANA             Reviewed;         328 AA.
AC   Q93X67;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase 2, chloroplastic;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase 2;
DE   Flags: Precursor;
GN   Name=bkr2;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Jet neuf; TISSUE=Embryo;
RA   McDonald F.S., White A.J., Elborough K.M., Slabas A.R.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=And non-
CC       photosynthetic plastids. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AJ243084; CAC41363.1; -; mRNA.
DR   RefSeq; NP_001302983.1; NM_001316054.1.
DR   AlphaFoldDB; Q93X67; -.
DR   SMR; Q93X67; -.
DR   EnsemblPlants; CDY54831; CDY54831; GSBRNA2T00014699001.
DR   GeneID; 106361756; -.
DR   Gramene; CDY54831; CDY54831; GSBRNA2T00014699001.
DR   KEGG; bna:106361756; -.
DR   OMA; CQKHMVD; -.
DR   OrthoDB; 2263846at2759; -.
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:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05333; BKR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..66
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           67..328
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000031978"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         90..114
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  34374 MW;  AFB61AF1C665545F CRC64;
     MATTSIAGPR LTSLKTAAGK LGYREICHVR QWAPVHSPMP HFGMLRCGSR RPFATSSSTV
     VQAQAQATAA EQSTGEEEAV PKVESPVVVV TGASRGIGKA IALSLGKAGC KVLVNYARSA
     KEAEQVSKQI EAYGGQAITF GGDVSKEADV DAMMKTAVDA WGTIDVVVNN AGITRDTLLI
     RMKKSQWDEV IDLNLTGVFL CTQAATKIMM KKRKGRIINI ASVVGLIGNI GQANYAAAKA
     GVIGFSKTAA REGASRNINV NVVCPGFIAS DMTAKLGEDM EKKILGTIPL GRYGQPEDVA
     GLVEFLALSP AASYITGQAF TIDGGIAI
//