ID   D8SMD0_SELML            Unreviewed;       313 AA.
AC   D8SMD0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=SELMODRAFT_271709 {ECO:0000313|EMBL:EFJ14471.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ14471.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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:RU366074}.
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DR   EMBL; GL377627; EFJ14471.1; -; Genomic_DNA.
DR   RefSeq; XP_002984421.1; XM_002984375.1.
DR   AlphaFoldDB; D8SMD0; -.
DR   STRING; 88036.D8SMD0; -.
DR   EnsemblPlants; EFJ14471; EFJ14471; SELMODRAFT_271709.
DR   GeneID; 9644450; -.
DR   Gramene; EFJ14471; EFJ14471; SELMODRAFT_271709.
DR   KEGG; smo:SELMODRAFT_271709; -.
DR   eggNOG; KOG1200; Eukaryota.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   InParanoid; D8SMD0; -.
DR   OMA; LFGVQCD; -.
DR   OrthoDB; 2263846at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001514; 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: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; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF13561; adh_short_C2; 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:UP000001514}.
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT   BINDING         77..80
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         220..224
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         253
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ   SEQUENCE   313 AA;  32596 MW;  47D07F1874F95E6B CRC64;
     MASASLISGF ATTTPAAAPA LQSRQHLRFG RNLQLCSSLG VRSSCSSSAI RAQVATATEP
     SHEATKLVEA PVSVVTGASR GIGKAIALAL GAAGGKVLVN YARSSKEAED VASQIEELGG
     SALVYGGDVS KEEDVEALFK AVIDKWGTID ILVNNAGITR DTLLMRMKKS QWDEVINLNL
     SGVFLCTQAA TKVMMKKKKG RIINISSVVG VTGNAGQANY SAAKAGVIGF TKTVAREYAG
     RSITANAIAP GFIASDMTAK LGDEIEKKIL QTIPLGRYGQ PEEVAGLVKF LALDPAAAYI
     TGQVFNIDGG MVM
//