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 16-JUN-2009, entry version 66. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH]; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; Synonyms=envM; OrderedLocusNames=HI1734; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; 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., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23379.1; -; Genomic_DNA. DR PIR; B64139; B64139. DR RefSeq; NP_439876.2; -. DR HSSP; P29132; 1DFI. DR SMR; P44432; 2-259. DR GeneID; 950535; -. DR GenomeReviews; L42023_GR; HI1734. DR KEGG; hin:HI1734; -. DR TIGR; HI1734; -. DR HOGENOM; P44432; -. DR BioCyc; HINF71421:HI_1734-MON; -. DR BRENDA; 1.3.1.9; 109. DR BindingDB; P44432; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NAD...; IEA:EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR PANTHER; PTHR19410:SF12; Enoyl-ACP_rdct; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Fatty acid biosynthesis; Lipid synthesis; Membrane; NAD; KW Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 262 Enoyl-[acyl-carrier-protein] reductase FT [NADH]. FT /FTId=PRO_0000054901. FT NP_BIND 10 36 NAD (By similarity). FT ACT_SITE 156 156 Proton acceptor (By similarity). 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 //