FABI_SALTY
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 03-AUG-2022, entry version 151.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 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 -!- 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}.
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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; P16657; -.
DR EnsemblBacteria; AAL20618; AAL20618; 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-MON; -.
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:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 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
