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Database: UniProt
Entry: L9U707_9GAMM
LinkDB: L9U707_9GAMM
Original site: L9U707_9GAMM 
ID   L9U707_9GAMM            Unreviewed;       403 AA.
AC   L9U707;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   13-SEP-2023, entry version 45.
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=HALTITAN_2691 {ECO:0000313|EMBL:ELY20562.1};
OS   Halomonas titanicae BH1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY20562.1, ECO:0000313|Proteomes:UP000011651};
RN   [1] {ECO:0000313|EMBL:ELY20562.1, ECO:0000313|Proteomes:UP000011651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH1 {ECO:0000313|EMBL:ELY20562.1,
RC   ECO:0000313|Proteomes:UP000011651};
RX   PubMed=23516210;
RA   Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M.,
RA   Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.;
RT   "Draft Genome of the Marine Gammaproteobacterium Halomonas titanicae.";
RL   Genome Announc. 1:E0008313-E0008313(2013).
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:ELY20562.1}.
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DR   EMBL; AOPO01000015; ELY20562.1; -; Genomic_DNA.
DR   RefSeq; WP_009288181.1; NZ_AOPO01000015.1.
DR   AlphaFoldDB; L9U707; -.
DR   GeneID; 69282122; -.
DR   PATRIC; fig|1204738.3.peg.4066; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000011651; 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          83..318
FT                   /note="Trans-2-enoyl-CoA reductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF12241"
FT   DOMAIN          329..392
FT                   /note="Enoyl reductase FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF07055"
FT   ACT_SITE        236
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         49..54
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         75..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         112..113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         140..141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   BINDING         274..276
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
FT   SITE            76
FT                   /note="Plays an important role in discriminating NADH
FT                   against NADPH"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01838"
SQ   SEQUENCE   403 AA;  44390 MW;  774745E184681E9B CRC64;
     MIIKPKVRGF ICTTTHPIGC EQNVREQIEA TRARGLDKQA GPKKVLVIGA SSGYGLAARI
     TAAFGYGADT LGVFFEKPAT DKKPGTAGWY NSAAFDKFAK QEGLYSKSIN GDAFSHEARE
     KAIELIKQDM GEIDLVVYSL ASPVRKLPDS GELKRSSLKP IGETYRATAI DTNKDAIIEA
     EVEPATQQEI DDTITVMGGE DWELWMEALD QAGVLAKGAR SVAFSYIGTE ITWPIYWHGA
     LGKAKEDLDR AAAAIDAKLK ETGGGANVAV LKSVVTQASA AIPVMPLYIA MVYRIMKEQG
     LHEGTIDQLN RLFGEQLYSA QGKRGEMVTD EVGRLRLDDW ELRDDVQQAC QDLWPEVTTE
     NLFEITDYAG YKHEFLKLFG FERDDVDYDA DVNPEVTFDV VNL
//
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