ID   FABG_SCHPO              Reviewed;         236 AA.
AC   O42866;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
GN   Name=oar2; ORFNames=SPAC3G9.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Involved in biosynthesis of fatty acids in mitochondria.
CC       {ECO:0000250}.
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   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA15911.1; -; Genomic_DNA.
DR   PIR; T11638; T11638.
DR   RefSeq; NP_594074.1; NM_001019511.2.
DR   AlphaFoldDB; O42866; -.
DR   SMR; O42866; -.
DR   STRING; 284812.O42866; -.
DR   MaxQB; O42866; -.
DR   PaxDb; 4896-SPAC3G9-02-1; -.
DR   EnsemblFungi; SPAC3G9.02.1; SPAC3G9.02.1:pep; SPAC3G9.02.
DR   GeneID; 2543512; -.
DR   KEGG; spo:SPAC3G9.02; -.
DR   PomBase; SPAC3G9.02; oar2.
DR   VEuPathDB; FungiDB:SPAC3G9.02; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   InParanoid; O42866; -.
DR   OMA; TCMITGG; -.
DR   PhylomeDB; O42866; -.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:O42866; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISO:PomBase.
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:0048038; F:quinone binding; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IC:PomBase.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43477; DIHYDROANTICAPSIN 7-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43477:SF1; DIHYDROANTICAPSIN 7-DEHYDROGENASE; 1.
DR   Pfam; PF13561; adh_short_C2; 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; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..236
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT                   /id="PRO_0000374026"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        155
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         115
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT   BINDING         151
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         184
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O93868"
FT   BINDING         186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:L0E2Z4"
SQ   SEQUENCE   236 AA;  25601 MW;  7F28C25E0C9251D9 CRC64;
     MRKVLITGGS SGLGKRIAQI WSQKGHQCHI VGRNEFHLKE TLQSLSVAKG QQHTLTIADV
     QSDMKNLKSI FESVEIDTVV HAAGVLQSSL CVRTSEKEID SIICTNLVSA IKLSKMAILE
     WFRNKNSERD RLILNISSRL STYALPGTSV YAASKAGLES FTKVLAAEVA SKGIRVNAIS
     PGYVDTPMLS SQIRAIAEKK VPIGRLASTD EIVDACTFLL DNRYTTGTIL PITGGL
//