ID A0A1G8PEJ4_9BRAD Unreviewed; 269 AA.
AC A0A1G8PEJ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN ORFNames=SAMN05216338_103315 {ECO:0000313|EMBL:SDI90160.1};
OS Bradyrhizobium sp. Rc2d.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855321 {ECO:0000313|EMBL:SDI90160.1, ECO:0000313|Proteomes:UP000198770};
RN [1] {ECO:0000313|EMBL:SDI90160.1, ECO:0000313|Proteomes:UP000198770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rc2d {ECO:0000313|EMBL:SDI90160.1,
RC ECO:0000313|Proteomes:UP000198770};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000175,
CC ECO:0000256|PIRNR:PIRNR000094};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000256|ARBA:ARBA00009233,
CC ECO:0000256|PIRNR:PIRNR000094}.
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DR EMBL; FNCU01000033; SDI90160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PEJ4; -.
DR STRING; 1855321.SAMN05216338_103315; -.
DR OrthoDB; 9803628at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000198770; Unassembled WGS sequence.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05372; ENR_SDR; 1.
DR Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 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 PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 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 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000094};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000094}.
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT BINDING 17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 23..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 68..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 193..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ SEQUENCE 269 AA; 28870 MW; 718727C700B6EFA4 CRC64;
MAQNSGLMQG KRGVILGVAN NRSIAWGIAK ACRAAGAELA FTYQGDALKK RVEPLAAEVG
GLVLGHCDVT DAATIDAAFA VLREKWGKID FLVHAIAYGE QLDGRYVDTT QENFSKSMLI
SCYSFTAVAQ RAEKLMTDGG SLITLSYYGA EKWMPHYNVM GVAKAALEAS VRYLAADLGE
KNIRVNAISA GPIKTLAASG IGDFRYILKW NEYNAPMRRN VSAEDVGGSA LYFLSDLSRG
VTGEVHHVDS GYHVLGMKRP DAPDISLGG
//
