ID   FABV_CLOPE              Reviewed;         389 AA.
AC   Q8XIP1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CPE2074;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81780.1; -; Genomic_DNA.
DR   RefSeq; WP_011010749.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIP1; -.
DR   SMR; Q8XIP1; -.
DR   STRING; 195102.gene:10491344; -.
DR   EnsemblBacteria; BAB81780; BAB81780; BAB81780.
DR   KEGG; cpe:CPE2074; -.
DR   HOGENOM; CLU_057698_1_0_9; -.
DR   OMA; EGCIEQI; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000818; 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; IPR036291; NAD(P)-bd_dom_sf.
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.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..389
FT                   /note="Trans-2-enoyl-CoA reductase [NADH]"
FT                   /id="PRO_0000220041"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         47..52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         73..74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         110..111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         138..139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         272..274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   SITE            74
FT                   /note="Plays an important role in discriminating NADH
FT                   against NADPH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
SQ   SEQUENCE   389 AA;  43138 MW;  36E1230CC803E7C5 CRC64;
     MIVEPKFRGF ICTTSHPIGC KKNVENQIEY VKENGKIEGA KRVLVLGAST GYGLASAIVA
     SEACDAEVLG VSFEREAKGK RTASAGWYNI ESLKKFVEGE GKKFISVNGD AFSNEVKSEV
     IDLIKENMGK VDLVIYSLAA PKRKDPVSGE VYSSCLKTVG APFTSKTLDF HTGEIQNITI
     NPATEEEIEG TRKVMGGEDW MLWIEALKEA NVLENGVKTI AYSYIGPEVT YPIYREGTIG
     RAKNDLEKTA GEITKVLKSL NGEGYISVNK ALVTQASSAI PIVSLYISIL YKVMKEKGTH
     EGCIEQIYRM FKELYEGNLN LDSENRIRID DLEMAEDVQK AIEEIWPQIT SENVFELSDA
     EDFKKEFFKL FGFGLEGVDY SEDVDITTV