FABV_AERS4
ID FABV_AERS4 Reviewed; 397 AA.
AC A4SLJ1;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabV {ECO:0000303|PubMed:25370725};
DE Short=ENR {ECO:0000303|PubMed:25370725};
DE EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN OrderedLocusNames=ASA_1682;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=25370725; DOI=10.4014/jmb.1407.07021;
RA Khan R., Lee M.H., Joo H.J., Jung Y.H., Ahmad S., Choi J.H., Lee S.W.;
RT "Triclosan resistance in a bacterial fish pathogen, aeromonas salmonicida
RT subsp. salmonicida, is mediated by an enoyl reductase, FabV.";
RL J. Microbiol. Biotechnol. 25:511-520(2015).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction
CC of the carbon-carbon double bond in the enoyl moiety that is covalently
CC linked to an acyl carrier protein (ACP). {ECO:0000269|PubMed:25370725}.
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:0000255|HAMAP-Rule:MF_01838};
CC -!- ACTIVITY REGULATION: Resistant to triclosan.
CC {ECO:0000269|PubMed:25370725}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; CP000644; ABO89763.1; -; Genomic_DNA.
DR RefSeq; WP_005314774.1; NC_009348.1.
DR AlphaFoldDB; A4SLJ1; -.
DR SMR; A4SLJ1; -.
DR STRING; 382245.ASA_1682; -.
DR EnsemblBacteria; ABO89763; ABO89763; ASA_1682.
DR KEGG; asa:ASA_1682; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OMA; EGCIEQI; -.
DR OrthoDB; 678530at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000225; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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; PTHR37480; 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; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..397
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabV"
FT /id="PRO_0000433641"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 273..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
SQ SEQUENCE 397 AA; 43475 MW; 7A269E6F919FD175 CRC64;
MIIKPKVRGF ICTTTHPVGC EANVRRQIAY TQEQGMIANG PKRVLVIGAS TGYGLASRIA
TAFGSGAATI GVFFEKAGSE TKTATAGWYN SAAFDKAAKE AGLYAKSVNG DAFSNECRAK
VIELIKADLG QIDLVVYSLA SPVRKMPETG EVVRSALKPI GETYTTTAID TNKDQIITAT
VEPANEEEIQ NTITVMGGQD WELWMAALRD AGVLADGAKS VAYSYIGTDL TWPIYWHGTL
GRAKEDLDRA ATAIRGDLAA KGGTAHVAVL KSVVTQASSA IPVMPLYISM AFKIMKEKGI
HEGCMEQVYR MMRTRLYGEE LALDEQARIR MDDWELREDV QQTCRDLWPS ITTENLSELT
DYTGYKQEFL RLFGFGLAEV DYEADVNPDV KFDVVEL
