AC MF_01838; DC Protein; auto TR HAMAP; MF_01838; -; 1; level=0 XX Names: FabV_reductase XX ID FABV case or DE RecName: Full=Trans-2-enoyl-CoA reductase [NADH]; DE Short=TER; DE EC=1.3.1.44; else DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH]; DE Short=ENR; DE EC=1.3.1.9; end case GN Name=fabV; XX case or 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). 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; else 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). 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; end case CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the TER reductase family. XX DR Pfam; PF07055; Eno-Rase_FAD_bd; 1; trigger=no XX KW Fatty acid biosynthesis KW Fatty acid metabolism KW Lipid metabolism KW Lipid biosynthesis KW NAD KW Oxidoreductase XX case or GO GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity else GO GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity end case GO GO:0051287; F:NAD binding GO GO:0006633; P:fatty acid biosynthetic process XX FT From: FABV_CLOAB (Q97LU2) FT BINDING 47..52 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G-x-S-[STN]-x-[YF] FT BINDING 74..75 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [YLF]-E FT BINDING 111..112 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: D-[AGV] FT BINDING 139..140 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [VLIA]-A FT BINDING 274..276 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [LIV]-x-T FT ACT_SITE 235 FT /note="Proton donor" FT Condition: Y FT BINDING 225 FT /ligand="substrate" FT Condition: Y FT BINDING 244 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: K FT SITE 75 FT /note="Plays an important role in discriminating NADH FT against NADPH" FT Condition: E XX Size: 389-406; Related: None; Template: Q62L02; Q9KRA3; Q97LU2; Q73Q47; Q2P9J6; Q8Z9U1; Q9HZP8; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in PHOPR, VIBCH, VIBPA, VIBVU, VIBVY Plasmid: None Comments: None XX # Revision 1.27 2023/02/17 //