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 27-MAR-2024, entry version 108. 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; Bacillota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniPathway; UPA00094; -. DR Proteomes; UP000001415; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR CDD; cd05372; ENR_SDR; 1. DR Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1. DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. 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; 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 //