FABG_HAEIN
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 03-AUG-2022, entry version 139.
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; Proteobacteria; 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 RefSeq; WP_005694436.1; 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 OMA; KMPERDY; -.
DR PhylomeDB; P43713; -.
DR BioCyc; HINF71421:G1GJ1-167-MON; -.
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 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; 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
