ID FABI_SALTY Reviewed; 262 AA. AC P16657; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 164. 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=STM1700; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-93. RC STRAIN=AG701; RX PubMed=2687243; DOI=10.1128/jb.171.12.6555-6565.1989; RA Turnowsky F., Fuchs K., Jeschek C., Hoegenauer G.; RT "envM genes of Salmonella typhimurium and Escherichia coli."; RL J. Bacteriol. 171:6555-6565(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP PROTEIN SEQUENCE OF 2-11. RC STRAIN=SL1344; RX PubMed=8559071; DOI=10.1111/j.1365-2958.1995.mmi_17030523.x; RA Qi S.Y., Li Y., Szyroki A., Giles I.G., Moir A., O'Connor C.D.; RT "Salmonella typhimurium responses to a bactericidal protein from human RT neutrophils."; RL Mol. Microbiol. 17:523-531(1995). 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 and in the biotin biosynthesis (By similarity). CC {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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- MISCELLANEOUS: The antibiotic diazaborine interferes with the activity CC by binding to the protein. 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; M31806; AAA27059.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20618.1; -; Genomic_DNA. DR PIR; B43729; B43729. DR RefSeq; NP_460659.1; NC_003197.2. DR RefSeq; WP_000506505.1; NC_003197.2. DR AlphaFoldDB; P16657; -. DR SMR; P16657; -. DR STRING; 99287.STM1700; -. DR PaxDb; 99287-STM1700; -. DR GeneID; 1253219; -. DR KEGG; stm:STM1700; -. DR PATRIC; fig|99287.12.peg.1794; -. DR HOGENOM; CLU_010194_10_1_6; -. DR OMA; GILDMIH; -. DR PhylomeDB; P16657; -. DR BioCyc; SENT99287:STM1700-MONOMER; -. DR UniPathway; UPA00078; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000001014; Chromosome. 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:0009102; P:biotin biosynthetic process; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. 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 NCBIfam; NF005938; PRK07984.1; 1. 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. PE 1: Evidence at protein level; KW Antibiotic resistance; Biotin biosynthesis; Direct protein sequencing; 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:0000269|PubMed:8559071" FT CHAIN 2..262 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI" FT /id="PRO_0000054910" 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 40 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" FT MUTAGEN 93 FT /note="G->S: Diazaborine resistance." FT /evidence="ECO:0000269|PubMed:2687243" SQ SEQUENCE 262 AA; 27761 MW; 185A199EB359F643 CRC64; MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSSIV LPCDVAEDAS IDAMFAELGN VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKVAHDIS SYSFVAMAKA CRTMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG FSIAAMNELE LK //