ID   FABG_HAEIN              Reviewed;         242 AA.
AC   P43713;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 145.
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=HI_0155;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21824.1; -; Genomic_DNA.
DR   PIR; D64051; D64051.
DR   RefSeq; NP_438325.1; NC_000907.1.
DR   AlphaFoldDB; P43713; -.
DR   SMR; P43713; -.
DR   STRING; 71421.HI_0155; -.
DR   EnsemblBacteria; AAC21824; AAC21824; HI_0155.
DR   KEGG; hin:HI_0155; -.
DR   PATRIC; fig|71421.8.peg.159; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OrthoDB; 9804774at2; -.
DR   PhylomeDB; P43713; -.
DR   BioCyc; HINF71421:G1GJ1-167-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000579; 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: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; 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..242
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT                   /id="PRO_0000054673"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         10..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..58
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..153
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   242 AA;  25507 MW;  B3DE2E2C020D2F71 CRC64;
     MQGKIALVTG STRGIGRAIA EELSSKGAFV IGTATSEKGA EAISAYLGDK GKGLVLNVTD
     KESIETLLEQ IKNDFGDIDI LVNNAGITRD NLLMRMKDEE WFDIMQTNLT SVYHLSKAML
     RSMMKKRFGR IINIGSVVGS TGNPGQTNYC AAKAGVVGFS KSLAKEVAAR GITVNVVAPG
     FIATDMTEVL TDEQKAGILS NVPAGRLGEA KDIAKAVAFL ASDDAGYITG TTLHVNGGLY
     LS
//