ID   FABG_CUPLA              Reviewed;         320 AA.
AC   P28643;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   28-JAN-2026, entry version 121.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE   Flags: Precursor;
GN   Name=CLKR27;
OS   Cuphea lanceolata (Cigar flower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Cuphea.
OX   NCBI_TaxID=3930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1376402; DOI=10.1007/bf00587569;
RA   Klein B., Pawlowski K., Hoericke-Grandpierre C., Schell J., Toepfer R.;
RT   "Isolation and characterization of a cDNA from Cuphea lanceolata encoding a
RT   beta-ketoacyl-ACP reductase.";
RL   Mol. Gen. Genet. 233:122-128(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH
CC         + H(+); 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. Plastid. Note=And non-
CC       photosynthetic plastids.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; X64566; CAA45866.1; -; mRNA.
DR   PIR; S22450; S22450.
DR   AlphaFoldDB; P28643; -.
DR   SMR; P28643; -.
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   FunFam; 3.40.50.720:FF:000194; 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR057326; KR_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR050259; SDR.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR   NCBIfam; NF005559; PRK07231.1; 1.
DR   NCBIfam; NF009466; PRK12826.1-2; 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..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           62..320
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase,
FT                   chloroplastic"
FT                   /id="PRO_0000031981"
FT   ACT_SITE        227
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         82..106
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  33103 MW;  06BAF0522B2B8C87 CRC64;
     MATATAAGCS GAVALKSLGG RRLCIPQQLS PVLAGFGSHA AKSFPILSTR SIATSGIRAQ
     VATAEKVSAG AGQSVESPVV IVTGASRGIG KAIALSLGKA GCKVLVNYAR SSKEAEEVSK
     EIEAFGGQAL TFGGDVSKEE DVEAMIKTAV DAWGTVDILV NNAGITRDGL LMRMKKSQWQ
     EVIDLNLTGV FLCTQAAAKI MMKKKKGRII NIASVVGLVG NAGQANYSAA KAGVIGFTKT
     VAREYASRNI NVNAVAPGFI SSDMTSKLGD DINKKILETI PLGRYGQPEE VAGLVEFLAI
     NPASSYVTGQ VFTIDGGMTM
//