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FABG_STAAC
ID   FABG_STAAC              Reviewed;         246 AA.
AC   Q5HGK2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=SACOL1245;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW38079.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000046; AAW38079.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5HGK2; -.
DR   SMR; Q5HGK2; -.
DR   EnsemblBacteria; AAW38079; AAW38079; SACOL1245.
DR   KEGG; sac:SACOL1245; -.
DR   HOGENOM; CLU_010194_1_3_9; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000530; 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   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   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 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.
FT   CHAIN           1..246
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT                   /id="PRO_0000054683"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
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;  26146 MW;  2BD7CA319D3A37C5 CRC64;
     MKMTKSALVT GASRGIGRSI ALQLAEEGYN VAVNYAGSKE KAEAVVEEIK AKGVDSFAIQ
     ANVADADEVK AMIKEVVSQF GSLDVLVNNA GITRDNLLMR MKEQEWDDVI DTNLKGVFNC
     IQKATPQMLR QRSGAIINLS SVVGAVGNPG QANYVATKAG VIGLTKSAAR ELASRGITVN
     AVAPGFIVSD MTDALSDELK EQMLTQIPLA RFGQDTDIAN TVAFLASDKA KYITGQTIHV
     NGGMYM
 
 
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