FABV_PSEAE
ID FABV_PSEAE Reviewed; 398 AA.
AC Q9HZP8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000303|PubMed:19933806};
DE Short=ENR {ECO:0000303|PubMed:19933806};
DE EC=1.3.1.9 {ECO:0000269|PubMed:19933806};
DE AltName: Full=Trans-2-enoyl-CoA reductase {ECO:0000303|PubMed:19933806};
DE Short=TER {ECO:0000303|PubMed:19933806};
DE EC=1.3.1.44 {ECO:0000269|PubMed:19933806};
GN Name=fabV {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=PA2950;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP TYR-235 AND LYS-244, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19933806; DOI=10.1128/aac.01152-09;
RA Zhu L., Lin J., Ma J., Cronan J.E., Wang H.;
RT "Triclosan resistance of Pseudomonas aeruginosa PAO1 is due to FabV, a
RT triclosan-resistant enoyl-acyl carrier protein reductase.";
RL Antimicrob. Agents Chemother. 54:689-698(2010).
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). It can use both crotonyl-CoA and trans-2-
CC decenoyl-ACP. It is able to convert trans-2-enoyl-ACP of different
CC length (C2 to C16) to the corresponding acyl-ACP.
CC {ECO:0000269|PubMed:19933806}.
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:0000269|PubMed:19933806};
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:0000269|PubMed:19933806};
CC -!- ACTIVITY REGULATION: Not sensitive to tricolsan.
CC {ECO:0000269|PubMed:19933806}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=691 uM for trans-2-decenoyl-ACP {ECO:0000269|PubMed:19933806};
CC KM=704.3 uM for crotonyl-CoA {ECO:0000269|PubMed:19933806};
CC Vmax=7.9 nmol/min/mg enzyme for reductase activity with crotonyl-CoA
CC {ECO:0000269|PubMed:19933806};
CC Vmax=243.3 nmol/min/mg enzyme for reductase activity with trans-2-
CC decenoyl-ACP {ECO:0000269|PubMed:19933806};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:19933806}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce significantly
CC more unsaturated fatty acids than wild-type. The ratio of unsaturated
CC fatty acids to saturated fatty acids in wild-type is 0.76, whereas in
CC the fabV mutant this ratio is increased to 1.12. The major unsaturated
CC fatty acid is the C16:1. When triclosan is added to the reaction
CC mixture, the reductase activity decreases to 15% of the untreated wild-
CC type. {ECO:0000269|PubMed:19933806}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; AE004091; AAG06338.1; -; Genomic_DNA.
DR PIR; A83277; A83277.
DR RefSeq; NP_251640.1; NC_002516.2.
DR RefSeq; WP_003102929.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q9HZP8; -.
DR SMR; Q9HZP8; -.
DR STRING; 287.DR97_4989; -.
DR PaxDb; Q9HZP8; -.
DR PRIDE; Q9HZP8; -.
DR DNASU; 882931; -.
DR EnsemblBacteria; AAG06338; AAG06338; PA2950.
DR GeneID; 882931; -.
DR KEGG; pae:PA2950; -.
DR PATRIC; fig|208964.12.peg.3096; -.
DR PseudoCAP; PA2950; -.
DR HOGENOM; CLU_057698_1_0_6; -.
DR InParanoid; Q9HZP8; -.
DR OMA; EGCIEQI; -.
DR PhylomeDB; Q9HZP8; -.
DR BioCyc; PAER208964:G1FZ6-3001-MON; -.
DR BRENDA; 1.3.1.9; 5087.
DR SABIO-RK; Q9HZP8; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..398
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_0000220046"
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"
FT MUTAGEN 235
FT /note="Y->F: It retains 17% of the reductase activity of
FT the wild-type. Loss of reductase activity; when associated
FT with M-244."
FT /evidence="ECO:0000269|PubMed:19933806"
FT MUTAGEN 244
FT /note="K->M: It retains 1.7% of the reductase activity of
FT the wild-type. Loss of reductase activity; when associated
FT with F-235."
FT /evidence="ECO:0000269|PubMed:19933806"
SQ SEQUENCE 398 AA; 43528 MW; 2C1EF224AB15DACE CRC64;
MIIKPRVRGF ICVTTHPAGC EANVKQQIDY VEAKGPVVNG PKKVLVIGSS TGYGLAARIT
AAFGSGADTL GVFFERPGSE SKPGTAGWYN SAAFEKFAHE KGLYARSING DAFSDEVKRL
TIETIKRDLG KVDLVVYSLA APRRTHPKSG EVFSSTLKPI GKSVSFRGLD TDKEVIKDVV
LEAASDQEVA DTVAVMGGED WQMWIDALLE ADVLADGAKT TAFTYLGEKI THDIYWNGSI
GAAKKDLDQK VLGIRDKLAP LGGDARVSVL KAVVTQASSA IPMMPLYLSL LFKVMKEQGT
HEGCIEQVDG LYRESLYGAE PRLDEEGRLR ADYKELQPEV QSRVEELWDK VTNENLYELT
DFAGYKSEFL NLFGFEVAGV DYEQDVNPDV QIANLIQA
