ID   FABG_THEMA              Reviewed;         246 AA.
AC   Q9X248;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE   AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase;
DE   AltName: Full=Beta-ketoacyl-ACP reductase;
GN   Name=fabG; OrderedLocusNames=TM_1724;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC       substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC       in the elongation cycle of fatty acid biosynthesis. {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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36790.1; -; Genomic_DNA.
DR   PIR; H72219; H72219.
DR   RefSeq; NP_229523.1; NC_000853.1.
DR   RefSeq; WP_004082240.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X248; -.
DR   SMR; Q9X248; -.
DR   STRING; 243274.TM_1724; -.
DR   PaxDb; 243274-THEMA_05620; -.
DR   EnsemblBacteria; AAD36790; AAD36790; TM_1724.
DR   KEGG; tma:TM1724; -.
DR   eggNOG; COG1028; Bacteria.
DR   InParanoid; Q9X248; -.
DR   OrthoDB; 9803333at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR   GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
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; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..246
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT                   /id="PRO_0000054693"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         62..63
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   246 AA;  26402 MW;  8C08904D28099142 CRC64;
     MRLEGKVCLI TGAASGIGKA TTLLFAQEGA TVIAGDISKE NLDSLVKEAE GLPGKVDPYV
     LNVTDRDQIK EVVEKVVQKY GRIDVLVNNA GITRDALLVR MKEEDWDAVI NVNLKGVFNV
     TQMVVPYMIK QRNGSIVNVS SVVGIYGNPG QTNYAASKAG VIGMTKTWAK ELAGRNIRVN
     AVAPGFIETP MTEKLPEKAR ETALSRIPLG RFGKPEEVAQ VILFLASDES SYVTGQVIGI
     DGGLVI
//