ID   FABV_RUMCH              Reviewed;         395 AA.
AC   B8I4V6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-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=Ccel_2273;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001348; ACL76610.1; -; Genomic_DNA.
DR   RefSeq; WP_015925702.1; NC_011898.1.
DR   AlphaFoldDB; B8I4V6; -.
DR   SMR; B8I4V6; -.
DR   STRING; 394503.Ccel_2273; -.
DR   EnsemblBacteria; ACL76610; ACL76610; Ccel_2273.
DR   KEGG; cce:Ccel_2273; -.
DR   eggNOG; COG3007; Bacteria.
DR   HOGENOM; CLU_057698_1_0_9; -.
DR   OMA; EGCIEQI; -.
DR   OrthoDB; 678530at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001349; 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; Reference proteome.
FT   CHAIN           1..395
FT                   /note="Trans-2-enoyl-CoA reductase [NADH]"
FT                   /id="PRO_1000188361"
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   395 AA;  44116 MW;  D3E2ACB03B4173C8 CRC64;
     MIVTPKFRGF ICTTSHPVGC EYSVMNQVEY IKNQKKINGA KKVLVIGAST GYGLASRITA
     AFGCGAATIG IFFERPGSKN KTASAGWYNS AAFEKMAKEE GLYAKSINGD AFSNEIKQKT
     IDLIKKDLGK VDMVVYSLAS PRRTHPVTGE VFNSVIKPIR EAYTSKTVDF HTQLVSETTI
     EPASDDEIRQ TIAVMGGEDW SMWMDALKKA DVLEDNVMTL AYSYVGPEVT HSVYREGTIG
     KAKDDLEATA IKINENLRTI GGKAYVSINK AVVTQASAAI PVISLYVSAL FKVMKEKNIH
     EGCIEQMYRM FNDRLYSGDL KLDSKGRICM DDLEMRPEVQ NEVTKLWNEA NNDNVKDITD
     IEGYRREFFR LFGFEFEDVD YNADVDIEVN IEGLY