ID W9UW00_9GAMM Unreviewed; 398 AA.
AC W9UW00;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=D791_01540 {ECO:0000313|EMBL:EXJ11408.1};
OS Nitrincola nitratireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1229521 {ECO:0000313|EMBL:EXJ11408.1, ECO:0000313|Proteomes:UP000019464};
RN [1] {ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|Proteomes:UP000019464};
RA Singh A., Pinnaka A.K., Vaidya B.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXJ11408.1, ECO:0000313|Proteomes:UP000019464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK23 {ECO:0000313|EMBL:EXJ11408.1,
RC ECO:0000313|Proteomes:UP000019464};
RX PubMed=26481633; DOI=10.1016/j.syapm.2015.09.002;
RA Singh A., Vaidya B., Tanuku N.R., Pinnaka A.K.;
RT "Nitrincola nitratireducens sp. nov. isolated from a haloalkaline crater
RT lake.";
RL Syst. Appl. Microbiol. 38:555-562(2015).
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:EXJ11408.1}.
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DR EMBL; AONB01000006; EXJ11408.1; -; Genomic_DNA.
DR RefSeq; WP_036509671.1; NZ_AONB01000006.1.
DR AlphaFoldDB; W9UW00; -.
DR STRING; 1229521.D791_01540; -.
DR PATRIC; fig|1229521.3.peg.1560; -.
DR OrthoDB; 9802260at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000019464; 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}.
FT DOMAIN 81..316
FT /note="Trans-2-enoyl-CoA reductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF12241"
FT DOMAIN 322..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 398 AA; 43481 MW; 587C7549F1F4AB0E CRC64;
MIITPKIRGF ICTTTHPVGC EANVKEQIAY TLAKGKIDGP KRVLVLGASS GYGLSSRIAA
AFGSDAATIG VFFEKPATEK KPGTAGWHNA AAFERLAHEA GLYAKSINGD AFSNEARAKV
IELIKADLGQ IDLVVYSLAS PVRKLPDTGE VIRSVLKPIG EPYRSTAIDT NKDIITEAEI
GPATQEEVDA TVKVMGGEDW ALWIDALSAA GVLAPECKTV AYSYIGTDIT WPIYWHGALG
KAKQHLDDTA KRLNAQLSAT GGQANVAVLK SVVTQASSAI PVMPLYLSMV FKVMKEQGLH
EGCMEQVYRL FSTGLYSDQA EIDSEGRYRM DDWELRDDVQ EACRKLWPQV TSENLFELTD
YAYYKTEFLK LFGFGIDGVD YEQDVNPLEE FDVISLDA
//
