ID FABV_CLOB8 Reviewed; 398 AA.
AC A6LV73;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Cbei_2086;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
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 Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) 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; CP000721; ABR34253.1; -; Genomic_DNA.
DR RefSeq; WP_012058312.1; NC_009617.1.
DR AlphaFoldDB; A6LV73; -.
DR SMR; A6LV73; -.
DR KEGG; cbe:Cbei_2086; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000565; 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 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; IPR036291; NAD(P)-bd_dom_sf.
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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..398
FT /note="Trans-2-enoyl-CoA reductase [NADH]"
FT /id="PRO_1000088450"
FT ACT_SITE 235
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 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 274..276
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 398 AA; 45231 MW; 03BBD68944600C23 CRC64;
MIFKPELIKG IAKTSHPYGC RKEVLNQIEY CKNAKQFHGP KKVLIIGASS GFGLATRISL
AFGGAKADTI GVSFETGITD RRTGTAGWYN NIFFKEFAEK EGLIAKNFIG DAFSDEVKEN
VIKYIKNEFG KIDLLIYSLA SPRRKDPKTG NIYDSTLKTT SGEFQGPTID METDELVTTK
VNSATDKEIE ATKKVMGGED WSEWCKLLLE NDCLSDKAIT ISYSYIGASR TYKIYREGTI
GEAKRHLENT AIQIDKEWQK KINGKAFVSV NKAIVTKASA YIPSFSLYAA VLYKVMKEKN
LHENCIMQMQ RMFADKIYAE NLLEFDDSGR LRMDDWELRE DVQSEVNELW EKITPDNFKI
LSDYDGYKKE FMQLNGFEID GVNYSEDIDI EALKRLEP
//
