FABI_RHIML
ID FABI_RHIML Reviewed; 55 AA.
AC Q9X450;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
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;
DE Flags: Fragment;
GN Name=fabI;
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=104A14;
RX PubMed=10094701; DOI=10.1128/jb.181.7.2217-2224.1999;
RA Summers M.L., Denton M.C., McDermott T.R.;
RT "Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium
RT meliloti are in an operon that is inducible by phosphate stress and
RT controlled by phoB.";
RL J. Bacteriol. 181:2217-2224(1999).
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 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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; AF095903; AAD24359.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X450; -.
DR SMR; Q9X450; -.
DR UniPathway; UPA00094; -.
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:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..>55
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT /id="PRO_0000054907"
FT BINDING 20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 26..27
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT NON_TER 55
SQ SEQUENCE 55 AA; 5905 MW; 0FC6A58A8F0C3C50 CRC64;
MSIPTVKAKL LQGRKGLIVG IANDRSIAWG RARAFRALGA EIAVTYLNDK ALPLV