ID D4I2K1_ERWAC Unreviewed; 399 AA.
AC D4I2K1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE Short=ENR {ECO:0000256|HAMAP-Rule:MF_01838};
DE EC=1.3.1.9 {ECO:0000256|HAMAP-Rule:MF_01838};
GN Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN OrderedLocusNames=EAMY_1757 {ECO:0000313|EMBL:CBA20707.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA20707.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA20707.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-
CC carbon double bond in an enoyl moiety that is covalently linked to an
CC acyl carrier protein (ACP). {ECO:0000256|HAMAP-Rule:MF_01838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.44;
CC Evidence={ECO:0000256|ARBA:ARBA00001615};
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|HAMAP-Rule:MF_01838};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01838}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01838}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000256|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; FN434113; CBA20707.1; -; Genomic_DNA.
DR RefSeq; WP_004157528.1; NC_013961.1.
DR AlphaFoldDB; D4I2K1; -.
DR STRING; 665029.EAMY_1757; -.
DR GeneID; 8911610; -.
DR KEGG; eam:EAMY_1757; -.
DR PATRIC; fig|665029.3.peg.1692; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OrthoDB; 9802260at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001841; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 1.
DR PANTHER; PTHR37480:SF1; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01838};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01838}.
FT DOMAIN 82..318
FT /note="Trans-2-enoyl-CoA reductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF12241"
FT DOMAIN 324..387
FT /note="Enoyl reductase FAD binding"
FT /evidence="ECO:0000259|Pfam:PF07055"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
SQ SEQUENCE 399 AA; 43219 MW; E9BD2941791B047D CRC64;
MIIKPRIRGF ICVTAHPAGC KANVEKQIDY VTAQGAITSG PKKVLVIGAS TGYGLAARIS
AAFGCASDTL GVFFERPGEA NKPATAGWYN SAAFEELATA KGLYAKSING DAYSDAVKQK
TIELIKQDLG QVDLVVYSLA APRRTHPKTG EVFNSALKPI GKSLTTRGLN TDKETITDVS
LEPASQEEID GTVAVMGGED WQMWIDALLE AGVLAEGAKT TAFTYLGEKI THDIYWNGSI
GEAKKDLDKR VLAIRNTLAA HGNGDARVSV LKAVVTQASS AIPVMPLYLS LLFKVMKEKG
THEGCIEQVY GLFKDSLYNA APIIDETGRL RADYKELQPE VQEEVSALWP TVSNENLNQL
TDFVGYKTEF MHLFGFGLEG VDYEADVDPD VKIKNLVQM
//
