ID   NMO_STAAR               Reviewed;         355 AA.
AC   Q6GIG7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Probable nitronate monooxygenase;
DE            Short=NMO;
DE            EC=1.13.12.- {ECO:0000250|UniProtKB:Q9HWH9};
DE   AltName: Full=Propionate 3-nitronate monooxygenase;
DE            Short=P3N monooxygenase;
GN   OrderedLocusNames=SAR0883;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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.
CC       Probably functions in the detoxification of P3N, a metabolic poison
CC       produced by plants and fungi as a defense mechanism.
CC       {ECO:0000250|UniProtKB:Q9HWH9}.
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:0000250|UniProtKB:D0V3Y4};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:Q9HWH9};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q9HWH9};
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; BX571856; CAG39889.1; -; Genomic_DNA.
DR   RefSeq; WP_000267243.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIG7; -.
DR   SMR; Q6GIG7; -.
DR   KEGG; sar:SAR0883; -.
DR   HOGENOM; CLU_038732_5_1_9; -.
DR   Proteomes; UP000000596; Chromosome.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004136; NMO.
DR   PANTHER; PTHR42747; NITRONATE MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR42747:SF3; NITRONATE MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF03060; NMO; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE   3: Inferred from homology;
KW   Detoxification; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..355
FT                   /note="Probable nitronate monooxygenase"
FT                   /id="PRO_0000360894"
FT   BINDING         71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         175
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         180
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         218
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT   BINDING         237..240
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWH9"
SQ   SEQUENCE   355 AA;  38621 MW;  6FA4F34F5A7C61AD CRC64;
     MWNKNRLTQM LSIEYPIIQA GMAGSTTPKL VASVSNSGGL GTIGAGYFNT QQLEDEIDYV
     RQLTSNSFGV NVFVPSQQSY TSSQIENMNA WLKPYRRALH LEEPVVKITE EQQFKCHIDT
     IIKKQVPVCC FTFGIPNESI IKRLKEANIK LIGTATSVDE AIANEKAGMD AIVAQGSEAG
     GHRGSFLKPK NQLPMVGTIS LVPQIVDVVS IPVIAAGGIM DGRGVLASIV LGAEGVQMGT
     AFLTSQDSNA SELLRDAIIN SKETDTVVTK AFSGKLARGI NNRFIEEMSQ YEGDIPDYPI
     QNELTSSIRK AAANIGDKEL THMWSGQSPR LATTHPANTI MSNIINQINQ IMQYK
//