ID R0GR68_9BRAS Unreviewed; 319 AA.
AC R0GR68;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=CARUB_v10009774mg {ECO:0000313|EMBL:EOA38281.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA38281.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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|ARBA:ARBA00011881,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB870805; EOA38281.1; -; Genomic_DNA.
DR RefSeq; XP_006305383.1; XM_006305321.1.
DR AlphaFoldDB; R0GR68; -.
DR STRING; 81985.R0GR68; -.
DR GeneID; 17899743; -.
DR KEGG; crb:17899743; -.
DR eggNOG; KOG1200; Eukaryota.
DR OrthoDB; 2263846at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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: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 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU366074};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW 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:UP000029121}.
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT BINDING 83..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 226..230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ SEQUENCE 319 AA; 33556 MW; 4A611B087BA8EF37 CRC64;
MATTVAGPRL FSLKAAGKLG YREISQVRQL APFHSAMPHF GMLRCGSRNP FTTSAVKAQA
TATEQSPGEV VQKVESPVVV VTGASRGIGK AIALALGKAG CKVLVNYARS AKEAEEVSRQ
IEEYGGQAIT FGGDVSKSAD VDAMMKTALD KWGTIDVVVN NAGITRDTLL IRMKQSQWDE
VIALNLTGVF LCTQAAIKIM NKKRKGRVIN ISSVVGLIGN IGQANYAAAK GGVISFSKTA
AREGASRNIN VNVVCPGFIA SDMTAELGED MEKKIMGTIP LGRYGKPEEV AGLVEFLALS
PAASYITGQA FTIDGGIAI
//
