ID   NMO_PSESP               Reviewed;         349 AA.
AC   D0V3Y4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Nitronate monooxygenase {ECO:0000305|PubMed:20382807};
DE            Short=NMO {ECO:0000305|PubMed:20382807};
DE            EC=1.13.12.- {ECO:0000269|PubMed:20382807};
DE   AltName: Full=Propionate 3-nitronate monooxygenase {ECO:0000303|PubMed:20382807};
DE            Short=P3N monooxygenase {ECO:0000303|PubMed:20382807};
GN   Name=pnoA {ECO:0000303|PubMed:20382807, ECO:0000312|EMBL:ACX83564.1};
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=JS189;
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).
CC   -!- FUNCTION: Nitronate monooxygenase that uses molecular oxygen to
CC       catalyze the oxidative denitrification of alkyl nitronates. Acts on
CC       propionate 3-nitronate (P3N), the presumed physiological substrate. Is
CC       likely involved in the degradation of P3N, that allows Pseudomonas sp.
CC       JS189 to grow on 3-nitropropionate/P3N as the sole source of nitrogen,
CC       carbon, and energy (PubMed:20382807). Also probably functions in the
CC       detoxification of P3N, a metabolic poison produced by plants and fungi
CC       as a defense mechanism (By similarity). Is not active against 3-
CC       nitropropionate, nor with neutral or nitronate forms of 1-nitropropane,
CC       2-nitropropane, nitroethane, nitromethane, 1-nitropentane, and 2-
CC       nitroethanol (PubMed:20382807). {ECO:0000250|UniProtKB:Q9HWH9,
CC       ECO:0000269|PubMed:20382807}.
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:20382807};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000305|PubMed:20382807};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q9HWH9};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for propionate 3-nitronate {ECO:0000269|PubMed:20382807};
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:20382807}.
CC   -!- MISCELLANEOUS: At physiological pH, 3-nitropropionate (3-NPA) exists in
CC       equilibrium with its conjugate base, propionate-3-nitronate (P3N).
CC       {ECO:0000305}.
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}.
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DR   EMBL; GU014557; ACX83564.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0V3Y4; -.
DR   SMR; D0V3Y4; -.
DR   GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
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   Detoxification; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..349
FT                   /note="Nitronate monooxygenase"
FT                   /id="PRO_0000445423"
FT   BINDING         69
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         176
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         181
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         217
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         236..239
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
SQ   SEQUENCE   349 AA;  36457 MW;  E01472F50366F6FE CRC64;
     MSNSLLSLLN IELPIIQSPM VGVSTPRLAA AVSNAGGLGS IGIGASNVEQ ARAMLRETAA
     LTDRPFNVNL FCHVPARADA AREAQWLAFL APLFAEFESP APAALREIYT SFVEDFAMLE
     MLLEEKPAVV SFHFGLPPQS SIDALKDAGI VLLACVTNLA EAQQAEHAGV HALVAQGYEA
     GGHRGVFDPQ QDSEMGTFAL VRVLTDACQL PVIAAGGIMD GAGIKAVMQL GASAAQLGTA
     FILCPESSAN PAYRDALQGP RAHQTRVTSA ISGRPARGMV NRNYIDLETN APALPDYPIA
     YDANKALNAA AANKANTDFA VQWAGQGAPL ARSMPAAALV NLLAAEMKA