NMO_STAAN
ID NMO_STAAN Reviewed; 355 AA.
AC Q99VF6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SA0781;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000018; BAB42020.1; -; Genomic_DNA.
DR PIR; A89858; A89858.
DR RefSeq; WP_000267236.1; NC_002745.2.
DR AlphaFoldDB; Q99VF6; -.
DR SMR; Q99VF6; -.
DR EnsemblBacteria; BAB42020; BAB42020; BAB42020.
DR KEGG; sau:SA0781; -.
DR HOGENOM; CLU_038732_5_1_9; -.
DR OMA; MDNARPF; -.
DR Proteomes; UP000000751; 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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 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_0000360897"
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; 38634 MW; 6B64191B9A986085 CRC64;
MWNKNRLTQM LSIEYPIIQA GMAGSTTPKL VASVSNSGGL GTIGAGYFNT QQLEDEIDYV
RQLTSNSFGV NVFVPSQQSY TSSQIENMNA WLKPYRRALH LEEPVVKIIE EQQFKCHIDT
IIKKQVPVCC FTFGIPNESI IERLKEANIK LIGTATSVDE AIANEKAGMD AIVAQGSEAG
GHRGSFLKPK NQLPMVGTIS LVPQIVDVVS IPVIAAGGIM DGRGVLASIV LGAEGVQMGT
AFLTSQDSNA SELLRDAIIN SKETDTVVTK AFSGKLARGI NNRFIEEMSQ YEGDIPDYPI
QNELTSSIRK AAANIGDKEL THMWSGQSPR LATTHPANTI MSNIINQINQ IMQYK