ID A0A0A0LQU1_CUCSA Unreviewed; 329 AA.
AC A0A0A0LQU1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00012948, ECO:0000256|RuleBase:RU366074};
DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948, ECO:0000256|RuleBase:RU366074};
GN ORFNames=Csa_2G350440 {ECO:0000313|EMBL:KGN62361.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN62361.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN62361.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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 Evidence={ECO:0000256|ARBA:ARBA00001572,
CC ECO:0000256|RuleBase:RU366074};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU366074}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU366074}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU366074}. Plastid
CC {ECO:0000256|RuleBase:RU366074}. Note=And non-photosynthetic plastids.
CC {ECO:0000256|RuleBase:RU366074}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CM002923; KGN62361.1; -; Genomic_DNA.
DR RefSeq; XP_004142941.1; XM_004142893.2.
DR AlphaFoldDB; A0A0A0LQU1; -.
DR STRING; 3659.A0A0A0LQU1; -.
DR EnsemblPlants; KGN62361; KGN62361; Csa_2G350440.
DR GeneID; 101221932; -.
DR Gramene; KGN62361; KGN62361; Csa_2G350440.
DR KEGG; csv:101221932; -.
DR eggNOG; KOG1200; Eukaryota.
DR OMA; KHMVDAG; -.
DR OrthoDB; 2263846at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000029981; Chromosome 2.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
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; NADPH-DEPENDENT REDUCTASE BACG; 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 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU366074};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU366074};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU366074};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU366074};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR611284-2};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366074};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981}.
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT BINDING 93..96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 236..240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ SEQUENCE 329 AA; 34311 MW; A89D6B44ED4A3697 CRC64;
MAAVTGSSAV AFSKVGIVGK FEGGVDRRAS SVQQWSPICN GAGSNQLRGC FGLQLRSKSS
FASTGIKAQV ATAEQASIKE VQQVEAPVAI VTGASRGIGK AIALSLGKAG CKVLVNYARS
SKEAEEVSKE IEGFGGQAIT FGGDMSKEAD VDSMMKTAID TWGTVDILIN NAGITRDGLL
MRMKTSQWQE VIDLNLTGVY LCTQAASKIM MKKKKGRIIN IASVVGLVGN VGQANYSAAK
AGVIGFTKSV AKEYASRNIN VNAIAPGFIA SDMTAKLGAE IEKKILSTIP LARYGQPEEV
AGLVEFLALN PAASYITGQV LTIDGGMVM
//