FABI_ENTFA
ID FABI_ENTFA Reviewed; 250 AA.
AC Q820V5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI;
DE Short=ENR;
DE EC=1.3.1.9;
DE AltName: Full=NADH-dependent enoyl-ACP reductase;
GN Name=fabI; OrderedLocusNames=EF_0282;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP ACTIVITY REGULATION.
RX PubMed=18335995; DOI=10.1021/bi800023a;
RA Xu H., Sullivan T.J., Sekiguchi J., Kirikae T., Ojima I., Stratton C.F.,
RA Mao W., Rock F.L., Alley M.R., Johnson F., Walker S.G., Tonge P.J.;
RT "Mechanism and inhibition of saFabI, the enoyl reductase from
RT Staphylococcus aureus.";
RL Biochemistry 47:4228-4236(2008).
CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an
CC enoyl moiety that is covalently linked to an acyl carrier protein
CC (ACP). Involved in the elongation cycle of fatty acid which are used in
CC the lipid metabolism (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC -!- ACTIVITY REGULATION: Inhibited by triclosan and its diphenyl ether
CC analgues. {ECO:0000269|PubMed:18335995}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; AE016830; AAO80145.1; -; Genomic_DNA.
DR RefSeq; NP_814074.1; NC_004668.1.
DR RefSeq; WP_002387650.1; NZ_KE136524.1.
DR AlphaFoldDB; Q820V5; -.
DR SMR; Q820V5; -.
DR STRING; 226185.EF_0282; -.
DR EnsemblBacteria; AAO80145; AAO80145; EF_0282.
DR KEGG; efa:EF0282; -.
DR PATRIC; fig|226185.45.peg.3047; -.
DR eggNOG; COG0623; Bacteria.
DR HOGENOM; CLU_010194_10_1_9; -.
DR OMA; GILDMIH; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..250
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT /id="PRO_0000407977"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 18..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 26767 MW; A0A4DA491D22F78E CRC64;
MFLQNKNVVV MGVANKKSIA WGCAKALKDQ GANVIYTYQN ERMKKQVVKL ADENDLLVEC
DVASDASIQA AFETIKNEVG TIDGLVHAIA FAKKEELSGN VSDITRDGFL LAQDISSYSL
LAVTHYAKPL LNPGSGIVTL TYLGSERAIP NYNMMGIAKA SLETAVKYLA FELAADKIRV
NGISAGAIKT LAVTGVKDYD QLISISNERT PDKTGVTIEE VGNTCAFLVS DLASGVVGDI
IYVDKGVHLT
