ID   FABV_BURCA              Reviewed;         400 AA.
AC   Q1BJC5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000255|HAMAP-Rule:MF_01838};
DE            Short=ENR {ECO:0000255|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=Bcen_5407;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01838}.
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:0000255|HAMAP-Rule:MF_01838};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01838}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC   -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01838}.
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DR   EMBL; CP000379; ABF80280.1; -; Genomic_DNA.
DR   RefSeq; WP_011548967.1; NC_008061.1.
DR   AlphaFoldDB; Q1BJC5; -.
DR   SMR; Q1BJC5; -.
DR   EnsemblBacteria; ABF80280; ABF80280; Bcen_5407.
DR   KEGG; bcn:Bcen_5407; -.
DR   HOGENOM; CLU_057698_1_0_4; -.
DR   OMA; EGCIEQI; -.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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; PTHR37480; 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; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..400
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT                   /id="PRO_1000070466"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         48..53
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         74..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         111..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         139..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         273..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   SITE            75
FT                   /note="Plays an important role in discriminating NADH
FT                   against NADPH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
SQ   SEQUENCE   400 AA;  43414 MW;  A9DD325F0A550166 CRC64;
     MIIKPRVRGF ICVTTHPVGC EANVKEQIDY VTSHGPIANG PKKVLVIGAS TGYGLAARIS
     AAFGSGADTL GVFFERAGSE TKPGTAGWYN SAAFEKFAAE KGLYARSING DAFSDKVKQV
     TIDTIKQDLG KVDLVVYSLA APRRTHPKTG ETISSTLKPV GKAVTFRGLD TDKEVIREVS
     LEPATQEEID GTVAVMGGED WQMWIDALDE AGVLADGAKT TAFTYLGEQI THDIYWNGSI
     GEAKKDLDKK VLSIRDKLAA HGGDARVSVL KAVVTQASSA IPMMPLYLSL LFKVMKETGT
     HEGCIEQVYG LLKDSLYGAT PHVDEEGRLR ADYKELDPQV QDKVVAMWDK VTNENLYEMT
     DFAGYKTEFL RLFGFEIAGV DYDADVNPDV KIPGIIDTTV