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Database: UniProt
Entry: B8AT02_ORYSI
LinkDB: B8AT02_ORYSI
Original site: B8AT02_ORYSI 
ID   B8AT02_ORYSI            Unreviewed;       308 AA.
AC   B8AT02;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=OsI_15572 {ECO:0000313|EMBL:EEC77135.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC77135.1, ECO:0000313|Proteomes:UP000007015};
RN   [1] {ECO:0000313|EMBL:EEC77135.1, ECO:0000313|Proteomes:UP000007015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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; CM000129; EEC77135.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8AT02; -.
DR   STRING; 39946.B8AT02; -.
DR   EnsemblPlants; BGIOSGA015233-TA; BGIOSGA015233-PA; BGIOSGA015233.
DR   Gramene; BGIOSGA015233-TA; BGIOSGA015233-PA; BGIOSGA015233.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   OMA; EGRCKQK; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000007015; Chromosome 4.
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   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   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:UP000007015}.
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT   BINDING         82..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         215..219
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         248
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ   SEQUENCE   308 AA;  31600 MW;  2E4033B5B8B5AF06 CRC64;
     MATSATAGAA AAVASPAVAP RGAAVAAVAR RGFVSFGAAA AARSRAVRSG GFSGVRTHVA
     AVEQALVQDA TKLEAPVVIV TGASRGIGKA TALALGKAGC KVLVNYARSS KEAEEVSKEI
     EACGGQAITF GGDVSKEADV DSMMKANILL SGITRDTLLM RMKKSQWQDV IDLNLTGVFL
     CTQAATKIMM KKKKGKIINI ASVVGLVGNI GQANYSAAKA GVIGLTKTVA REYASRNINV
     NAIAPGFIAS DMTAELGEDL EKKILSTIPL GRYGKPEEVA GLVEFLALNP AANYITGQVL
     TIDGGMVM
//
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