ID U1FL06_TRESO Unreviewed; 405 AA.
AC U1FL06;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE Short=TER {ECO:0000256|HAMAP-Rule:MF_01838};
DE EC=1.3.1.44 {ECO:0000256|HAMAP-Rule:MF_01838};
GN Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN ORFNames=HMPREF1325_1518 {ECO:0000313|EMBL:ERF60503.1};
OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF60503.1, ECO:0000313|Proteomes:UP000016412};
RN [1] {ECO:0000313|EMBL:ERF60503.1, ECO:0000313|Proteomes:UP000016412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF60503.1,
RC ECO:0000313|Proteomes:UP000016412};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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:0000256|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:0000256|ARBA:ARBA00001615, ECO:0000256|HAMAP-
CC Rule:MF_01838};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01838}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_01838}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000256|HAMAP-
CC Rule:MF_01838}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERF60503.1}.
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DR EMBL; AUZJ01000042; ERF60503.1; -; Genomic_DNA.
DR RefSeq; WP_021330555.1; NZ_AVQI01000084.1.
DR AlphaFoldDB; U1FL06; -.
DR STRING; 1125725.HMPREF1325_1518; -.
DR PATRIC; fig|1125725.3.peg.1531; -.
DR eggNOG; COG3007; Bacteria.
DR OrthoDB; 9802260at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000016412; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01838};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01838};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01838}.
FT DOMAIN 91..327
FT /note="Trans-2-enoyl-CoA reductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF12241"
FT DOMAIN 335..398
FT /note="Enoyl reductase FAD binding"
FT /evidence="ECO:0000259|Pfam:PF07055"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 57..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 83..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 120..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 148..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 283..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT SITE 84
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
SQ SEQUENCE 405 AA; 44089 MW; CE5D50A4A5EA84E2 CRC64;
MIIKPMVRSS ICINAHPVGC AKETENEIAY IKAQKEKRGI KGAKEGGAGP KTVLVLGCST
GYGLASRIVA AFEYGADTIG VSFEKAGTET KGGTPGWYNN AAFDRAAKKE GLASVTLNAD
AFADETRALV IDEVKKLGAK FDLIIYSLAS PVRTDPDTKV LYKSVIKPRG KPYSGKCIDI
MTETLKDSSA EPATEEEIAS TIKVMGGDDW RRWIKQLSDA GVLAQGCRTI AYSYIGPELS
HAIYRDGTIG TAKLDLEKAA LDLDKELKSS VGGGAYISVN KGLVTRSSAV IPIISLYLSI
LFKVMKEKGT HEGCIEQMER LFTERLYTAD GTVPTDSEHR IRIDDLELAD DVQKKCLERM
KSVTQENLRD LCDLEGYKHD FLAANGFDIA GVDYDKDVAR MDTID
//
