ID FABI_ECO57 Reviewed; 262 AA. AC P0AEK5; P29132; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 01-MAY-2013, entry version 64. 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=Z2512, ECs1861; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond CC in an enoyl moiety that is covalently linked to an acyl carrier CC protein (ACP). Involved in the elongation cycle of fatty acid CC which are used in the lipid metabolism and in the biotin CC biosynthesis (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD(+) = trans- CC 2,3-dehydroacyl-[acyl-carrier-protein] + NADH. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- MISCELLANEOUS: The antibiotic diazaborine interferes with the CC activity by binding to the protein (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. FabI subfamily. 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; AE005174; AAG56524.1; -; Genomic_DNA. DR EMBL; BA000007; BAB35284.1; -; Genomic_DNA. DR PIR; E90861; E90861. DR PIR; H85757; H85757. DR RefSeq; NP_287908.1; NC_002655.2. DR RefSeq; NP_309888.1; NC_002695.1. DR ProteinModelPortal; P0AEK5; -. DR SMR; P0AEK5; 2-260. DR MINT; MINT-1251192; -. DR STRING; 155864.Z2512; -. DR PRIDE; P0AEK5; -. DR EnsemblBacteria; AAG56524; AAG56524; Z2512. DR EnsemblBacteria; BAB35284; BAB35284; BAB35284. DR GeneID; 912787; -. DR GeneID; 961367; -. DR KEGG; ece:Z2512; -. DR KEGG; ecs:ECs1861; -. DR PATRIC; 18353671; VBIEscCol44059_2052. DR eggNOG; COG0623; -. DR KO; K00208; -. DR OMA; DCDVGSD; -. DR ProtClustDB; PRK07984; -. DR BioCyc; ECOL386585:GJFA-1837-MONOMER; -. DR UniPathway; UPA00078; -. DR UniPathway; UPA00094; -. DR BindingDB; P0AEK5; -. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. PE 3: Inferred from homology; KW Antibiotic resistance; Biotin biosynthesis; Complete proteome; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 262 Enoyl-[acyl-carrier-protein] reductase FT [NADH] FabI. FT /FTId=PRO_0000054900. FT NP_BIND 19 20 NAD (By similarity). FT NP_BIND 64 65 NAD (By similarity). FT NP_BIND 192 196 NAD (By similarity). FT ACT_SITE 146 146 Proton acceptor (By similarity). FT ACT_SITE 156 156 Proton acceptor (By similarity). FT BINDING 13 13 NAD; via carbonyl oxygen (By similarity). FT BINDING 40 40 NAD (By similarity). FT BINDING 92 92 NAD; via carbonyl oxygen (By similarity). FT BINDING 95 95 Substrate; via amide nitrogen and FT carbonyl oxygen (By similarity). FT BINDING 163 163 NAD (By similarity). FT SITE 201 201 Involved in acyl-ACP binding (By FT similarity). FT SITE 204 204 Involved in acyl-ACP binding (By FT similarity). FT SITE 205 205 Involved in acyl-ACP binding (By FT similarity). SQ SEQUENCE 262 AA; 27864 MW; 436A89AF349D1866 CRC64; MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG FSIAAMNELE LK //