ID   FABV_BRAHW              Reviewed;         392 AA.
AC   C0QVH0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000255|HAMAP-Rule:MF_01838};
DE            Short=TER {ECO:0000255|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.44 {ECO:0000255|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=BHWA1_02011;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT   intestine.";
RL   PLoS ONE 4:E4641-E4641(2009).
CC   -!- FUNCTION: Involved in the fatty acid synthesis (FAS II). Catalyzes the
CC       reduction of a carbon-carbon double bond in an enoyl moiety that is
CC       covalently linked to a coenzyme A (CoA). {ECO:0000255|HAMAP-
CC       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: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; CP001357; ACN84471.1; -; Genomic_DNA.
DR   RefSeq; WP_012671510.1; NC_012225.1.
DR   AlphaFoldDB; C0QVH0; -.
DR   SMR; C0QVH0; -.
DR   STRING; 565034.BHWA1_02011; -.
DR   EnsemblBacteria; ACN84471; ACN84471; BHWA1_02011.
DR   GeneID; 63963163; -.
DR   KEGG; bhy:BHWA1_02011; -.
DR   eggNOG; COG3007; Bacteria.
DR   HOGENOM; CLU_057698_1_0_12; -.
DR   OMA; EGCIEQI; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001803; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; 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..392
FT                   /note="Trans-2-enoyl-CoA reductase [NADH]"
FT                   /id="PRO_1000188355"
FT   ACT_SITE        237
FT                   /note="Proton donor"
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         141..142
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         276..278
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   392 AA;  43652 MW;  BC7612E6EB107C4A CRC64;
     MVVEPKILNN ICITAHPLGC AKEVENHINY VKSQPKVKSN VKNALILGAS GGYGLASRIA
     IAYGLGAKTM SVSFEKGATA RRTATPGWYN NEAFSAFAKK DGIEDKNLIL DAFLNASKEE
     VIKEAKTFFN GEKIDLLIYS LAAPVRMDES TGTLYRSSLK PIGKKYNGIG VDFLTEELLE
     VSIDPANEDD IKSTVKVMGG EDWKLWTDAL LNADLLAENA INVAYSYIGP EMTKAVYREG
     TIGKAKDHLE ATAHELDKEM QEKIKGHAYV SVNKAVVTRS SAVIPTVPLY IGILFKVMKN
     KGLHEGCIEQ MYRLLNEKLY NGGEVPVDSD NRIRLDDWEL REDVQKEVLD SWNKLTKDNL
     KEIADLALFR KDYMNMHGFD EEGIDYSQDV QI