NMO_PSEAE
ID NMO_PSEAE Reviewed; 351 AA.
AC Q9HWH9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nitronate monooxygenase {ECO:0000303|PubMed:25002579, ECO:0000303|PubMed:25384477};
DE Short=NMO {ECO:0000303|PubMed:25002579};
DE EC=1.13.12.- {ECO:0000269|PubMed:25002579};
DE AltName: Full=Propionate 3-nitronate monooxygenase {ECO:0000303|PubMed:20382807, ECO:0000303|PubMed:25384477};
DE Short=P3N monooxygenase {ECO:0000303|PubMed:20382807, ECO:0000303|PubMed:25384477};
GN Name=nmoA {ECO:0000303|PubMed:25384477};
GN OrderedLocusNames=PA4202 {ECO:0000312|EMBL:AAG07589.1};
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.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20382807; DOI=10.1128/aem.00267-10;
RA Nishino S.F., Shin K.A., Payne R.B., Spain J.C.;
RT "Growth of bacteria on 3-nitropropionic acid as a sole source of carbon,
RT nitrogen, and energy.";
RL Appl. Environ. Microbiol. 76:3590-3598(2010).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25384477; DOI=10.1128/jb.01991-14;
RA Vercammen K., Wei Q., Charlier D., Doetsch A., Hauessler S., Schulz S.,
RA Salvi F., Gadda G., Spain J., Rybtke M.L., Tolker-Nielsen T., Dingemans J.,
RA Ye L., Cornelis P.;
RT "Pseudomonas aeruginosa LysR PA4203 regulator NmoR acts as a repressor of
RT the PA4202 nmoA gene, encoding a nitronate monooxygenase.";
RL J. Bacteriol. 197:1026-1039(2015).
RN [4] {ECO:0007744|PDB:4Q4K}
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH FMN, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25002579; DOI=10.1074/jbc.m114.577791;
RA Salvi F., Agniswamy J., Yuan H., Vercammen K., Pelicaen R., Cornelis P.,
RA Spain J.C., Weber I.T., Gadda G.;
RT "The combined structural and kinetic characterization of a bacterial
RT nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO
RT class I and II.";
RL J. Biol. Chem. 289:23764-23775(2014).
CC -!- FUNCTION: Nitronate monooxygenase that uses molecular oxygen to
CC catalyze the oxidative denitrification of alkyl nitronates. The toxin
CC propionate 3-nitronate (P3N) is the best substrate (and the presumed
CC physiological substrate), but this enzyme is also active on other
CC primary and secondary nitronates such as propyl-1-nitronate,
CC ethylnitronate, pentyl-1-nitronate, butyl-1-nitronate and propyl-2-
CC nitronate (PubMed:25002579). Is likely involved in the degradation of
CC P3N, that allows P.aeruginosa PAO1 to grow on 3-nitropropionate/P3N as
CC the sole nitrogen source (PubMed:20382807). Also functions in the
CC detoxification of P3N, a metabolic poison produced by plants and fungi
CC as a defense mechanism (PubMed:25384477). Cannot oxidize nitroalkanes
CC such as 3-nitropropionate, nitroethane, 1-nitropropane, 1-nitrobutane,
CC 1-nitropentane, or 2-nitropropane (PubMed:25002579).
CC {ECO:0000269|PubMed:20382807, ECO:0000269|PubMed:25002579,
CC ECO:0000269|PubMed:25384477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 3 O2 + 3 propionate 3-nitronate = 3 3-oxopropanoate + 3
CC H(+) + H2O2 + 2 nitrate + nitrite; Xref=Rhea:RHEA:57332,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:136067;
CC Evidence={ECO:0000269|PubMed:25002579, ECO:0000305|PubMed:20382807};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:25002579};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:25002579};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for propionate 3-nitronate (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:25002579};
CC KM=5 mM for ethylnitronate (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25002579};
CC KM=6 mM for propyl-1-nitronate (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25002579};
CC Note=kcat is 1300 sec(-1) with propionate 3-nitronate as substrate.
CC kcat is 350 sec(-1) with ethylnitronate as substrate. kcat is 1120
CC sec(-1) with propyl-1-nitronate as substrate (at pH 7.5 and 30
CC degrees Celsius). {ECO:0000269|PubMed:25002579};
CC -!- INDUCTION: Expression is repressed by NmoR. Is cotranscribed with ddlA.
CC {ECO:0000269|PubMed:25384477}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene results in an increased
CC sensitivity of the cells to P3N. {ECO:0000269|PubMed:25384477}.
CC -!- MISCELLANEOUS: At physiological pH, 3-nitropropionate (3-NPA) exists in
CC equilibrium with its conjugate base, propionate-3-nitronate (P3N).
CC {ECO:0000305|PubMed:25384477}.
CC -!- MISCELLANEOUS: P3N is a potent irreversible inhibitor of the key enzyme
CC succinate dehydrogenase in the Krebs cycle and electron transport
CC chain. P3N has been shown to be a toxic metabolite to bacteria, plants,
CC fungi, mammals or any organism that uses succinate dehydrogenase.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family. NMO class I
CC subfamily. {ECO:0000305|PubMed:25002579}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG07589.1; -; Genomic_DNA.
DR PIR; F83121; F83121.
DR RefSeq; NP_252891.1; NC_002516.2.
DR RefSeq; WP_003114723.1; NZ_QZGE01000013.1.
DR PDB; 4Q4K; X-ray; 1.44 A; A/B=1-351.
DR PDBsum; 4Q4K; -.
DR AlphaFoldDB; Q9HWH9; -.
DR SMR; Q9HWH9; -.
DR STRING; 208964.PA4202; -.
DR PaxDb; Q9HWH9; -.
DR PRIDE; Q9HWH9; -.
DR EnsemblBacteria; AAG07589; AAG07589; PA4202.
DR GeneID; 879034; -.
DR KEGG; pae:PA4202; -.
DR PATRIC; fig|208964.12.peg.4402; -.
DR PseudoCAP; PA4202; -.
DR HOGENOM; CLU_038732_5_1_6; -.
DR InParanoid; Q9HWH9; -.
DR OMA; MDNARPF; -.
DR PhylomeDB; Q9HWH9; -.
DR BioCyc; PAER208964:G1FZ6-4275-MON; -.
DR BRENDA; 1.13.12.16; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IDA:PseudoCAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Flavoprotein; FMN; Monooxygenase;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Nitronate monooxygenase"
FT /id="PRO_5004326837"
FT BINDING 21
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT BINDING 69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT BINDING 176
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT BINDING 181
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT BINDING 218
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT BINDING 237..240
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25002579,
FT ECO:0007744|PDB:4Q4K"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4Q4K"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:4Q4K"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4Q4K"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4Q4K"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:4Q4K"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:4Q4K"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:4Q4K"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:4Q4K"
SQ SEQUENCE 351 AA; 36782 MW; C6C1509E3EACD5BE CRC64;
MTDRFTRLLG IQQPIIQAPM LGVSTPALAA AVSNAGGLGS IAITGSAAEK GRALIREVRG
LTDKPFNVNL FCHRPGQADP ARERAWLDYL KPLFAEFGAE PPVRLKNIYL SFLEDPTLLP
MLLEERPAAV SFHFGAPPRD QVRALQAVGI RVLVCATTPE EAALVEAAGA DAVVAQGIEA
GGHRGVFEPE RGDAAIGTLA LVRLLAARGS LPVVAAGGIM DGRGIRAALE LGASAVQMGT
AFVLCPESSA NAAYREALKG PRAARTALTV TMSGRSARGL PNRMFFDAAA PGVPPLPDYP
FVYDATKALQ TAALARGNHD FAAQWAGQGA ALARELPAAE LLRTLVEELR G
