ID   FABG_AGGAC              Reviewed;         242 AA.
AC   P70720;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 115.
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;
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RX   PubMed=9020051; DOI=10.1006/bbrc.1996.5917;
RA   Yoshida Y., Nakano Y., Yamashita Y., Koga T.;
RT   "The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its
RT   adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA.";
RL   Biochem. Biophys. Res. Commun. 230:220-225(1997).
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; D88189; BAA13560.1; -; Genomic_DNA.
DR   RefSeq; WP_005545124.1; NZ_VSEW01000004.1.
DR   AlphaFoldDB; P70720; -.
DR   SMR; P70720; -.
DR   STRING; 714.ACT75_06515; -.
DR   GeneID; 77211127; -.
DR   eggNOG; COG1028; Bacteria.
DR   OMA; HGNAGQI; -.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05333; BKR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011285; FabG-rel.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01831; fabG_rel; 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   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..242
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT                   /id="PRO_0000054663"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         9..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   242 AA;  25987 MW;  1BC08625504F9D19 CRC64;
     MSETILITGS SRGIGKAIAL RLAQAGFDIV VHCRSRIEEA EAVAQAVREL GQNARVLQFD
     VSCRSEAADK LTADVEAHGA YYGVVLNAGL TRDNAFPALT DEDWDRVLRT NLDGFYNVLH
     PIMMPMIRRR KAGRIVCITS VSGLIGNRGQ VNYSASKAGI IGAAKALAVE LAKRKITVNC
     VAPGLIDTDI LDENVPIDEI LKMIPAGRMG DPEEVAHAVN FLMGEKAAYV TRQVIAVNGG
     LC
//