ID FABI_HAEIN Reviewed; 262 AA. AC P44432; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 157. 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; Synonyms=envM; OrderedLocusNames=HI_1734; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; 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). RN [2] RP ACTIVITY REGULATION. RX PubMed=12109908; DOI=10.1021/jm020050+; RA Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., Burgess W.J., RA Heerding D.A., Yuan C.C., Head M.S., Payne D.J., Rittenhouse S.F., RA Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., Keller P.M., RA Polizzi B.J., Qiu X., Janson C.A., Huffman W.F.; RT "Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP RT reductase (FabI)."; RL J. Med. Chem. 45:3246-3256(2002). RN [3] RP ACTIVITY REGULATION. RX PubMed=12699381; DOI=10.1021/jm0204035; RA Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., DeWolf W.E. Jr., RA Elkins P.A., Head M.S., Jakas D.R., Janson C.A., Keller P.M., Manley P.J., RA Moore T.D., Payne D.J., Pearson S., Polizzi B.J., Qiu X., Rittenhouse S.F., RA Uzinskas I.N., Wallis N.G., Huffman W.F.; RT "Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases RT FabI and FabK."; RL J. Med. Chem. 46:1627-1635(2003). 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 NADH + H(+); 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 1,4-benzodiazepine and CC naphthyridinone derivatives. {ECO:0000269|PubMed:12109908, CC ECO:0000269|PubMed:12699381}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. 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; L42023; AAC23379.1; -; Genomic_DNA. DR PIR; B64139; B64139. DR SMR; P44432; -. DR STRING; 71421.HI_1734; -. DR BindingDB; P44432; -. DR ChEMBL; CHEMBL5291548; -. DR EnsemblBacteria; AAC23379; AAC23379; HI_1734. DR KEGG; hin:HI_1734; -. DR PATRIC; fig|71421.8.peg.1815; -. DR eggNOG; COG0623; Bacteria. DR HOGENOM; CLU_010194_10_1_6; -. DR OMA; AAECADY; -. DR OrthoDB; 9803628at2; -. DR PhylomeDB; P44432; -. DR BioCyc; HINF71421:G1GJ1-1750-MONOMER; -. DR SABIO-RK; P44432; -. DR UniPathway; UPA00094; -. DR CDD; cd05372; ENR_SDR; 1. DR FunFam; 3.40.50.720:FF:000054; Enoyl-[acyl-carrier-protein] reductase [NADH]; 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], CHLOROPLASTIC; 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. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR Proteomes; UP000000579; Chromosome. DR AlphaFoldDB; P44432; -. PE 3: Inferred from homology; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..262 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI" FT /id="PRO_0000054901" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 19..20 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 64..65 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 192..196 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 201 FT /note="Involved in acyl-ACP binding" FT /evidence="ECO:0000250" FT SITE 204 FT /note="Involved in acyl-ACP binding" FT /evidence="ECO:0000250" FT SITE 205 FT /note="Involved in acyl-ACP binding" FT /evidence="ECO:0000250" SQ SEQUENCE 262 AA; 28119 MW; 71CEF6189795388E CRC64; MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE FAKEFGSDIV LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL DGDYVNAATR EGYRIAHDIS AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE RAIPNYNVMC LAKASLEAAT RVMAADLGKE GIRVNAISAG PIRTLAASGI KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI TGEIVHVDAG FSITAMGELG EE //