ID A0A0J0Y468_9SPHI Unreviewed; 397 AA.
AC A0A0J0Y468;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE Short=ENR {ECO:0000256|HAMAP-Rule:MF_01838};
DE EC=1.3.1.9 {ECO:0000256|HAMAP-Rule:MF_01838};
GN Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN ORFNames=AB669_15000 {ECO:0000313|EMBL:KLT65015.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65015.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT65015.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT65015.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|HAMAP-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};
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;
CC Evidence={ECO:0000256|HAMAP-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:KLT65015.1}.
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DR EMBL; LECU01000006; KLT65015.1; -; Genomic_DNA.
DR RefSeq; WP_047800093.1; NZ_LECU01000006.1.
DR AlphaFoldDB; A0A0J0Y468; -.
DR STRING; 1663685.AB669_15000; -.
DR PATRIC; fig|1663685.3.peg.3145; -.
DR OrthoDB; 9802260at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000036014; Unassembled WGS sequence.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IEA:UniProtKB-EC.
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}; Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT DOMAIN 81..316
FT /note="Trans-2-enoyl-CoA reductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF12241"
FT DOMAIN 323..385
FT /note="Enoyl reductase FAD binding"
FT /evidence="ECO:0000259|Pfam:PF07055"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 47..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 73..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 110..111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 138..139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT BINDING 272..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT SITE 74
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
SQ SEQUENCE 397 AA; 43109 MW; 861FE967EA700C8F CRC64;
MIIEPRMRGF ICLTAHPDGC AQNVKNQIEY VKSKGAINGP KKVLVIGAST GFGLASRITA
AYGSDAATIG VFFEKAPSAG KTASPGWYNS AAFEKEAHAS GLYAKSINGD AFSNEIKQQT
IDLIKADLGQ IDLVIYSLAS PVRKHPVTEV LHRSTLKPIG TIYTNKTVDF HTGNVTEISI
EPATDEDIAN TVAVMGGEDW AMWIDALKAE NLLAEGATTV AYSYIGPALT EPVYRKGTIG
RAKDNLEATA FTITDKLKDI SGQAYVSVNK ALVTQASSAI PVIPLYISLL YKIMKEEGIH
EGTIEQIQRL YADRLYTGSD IPLDEKGRIR IDDWEMRDDV QAKVAKLWDD ATTETLPAIG
DLAGYRSDFL SLFGFEIDGV DYEKDANEVV EIEGLVS
//
