NMO_STAAT
ID NMO_STAAT Reviewed; 355 AA.
AC A8Z1H7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=USA300HOU_0879;
OS Staphylococcus aureus (strain USA300 / TCH1516).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=451516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300 / TCH1516;
RX PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT "Subtle genetic changes enhance virulence of methicillin resistant and
RT sensitive Staphylococcus aureus.";
RL BMC Microbiol. 7:99-99(2007).
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; CP000730; ABX28900.1; -; Genomic_DNA.
DR RefSeq; WP_000267247.1; NC_010079.1.
DR AlphaFoldDB; A8Z1H7; -.
DR SMR; A8Z1H7; -.
DR KEGG; sax:USA300HOU_0879; -.
DR HOGENOM; CLU_038732_5_1_9; -.
DR OMA; MDNARPF; -.
DR BioCyc; SAUR451516-HMP:GTV5-897-MON; -.
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_0000360900"
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; 38548 MW; 2ABD713D5FDA7DB6 CRC64;
MWNKNRLTQM LSIEYPIIQA GMAGSTTPKL VASVSNSGGL GTIGAGYFNT QQLEDEIDYV
RQLTSNSFGV NVFVPSQQSY TSSQIENMNA WLKPYRRALH LEEPVVKITE EQQFKCHIDT
IIKKQVPVCC FTFGIPSEQI ISRLKAANVK LIGTATSVDE AIANEKAGMD AIVAQGSEAG
GHRGSFLKPK NQLPMVGTIS LVPQIVDVVS IPVIAAGGIM DGRGVLASIV LGAEGVQMGT
AFLTSQDSNA SELLRDAIIN SKETDTVITK AFSGKLARGI NNRFIEEMSQ YEGDIPDYPI
QNELTSSIRK AAANIGDKEL IHMWSGQSPR LATTHPANTI MSNIINQINQ IMQYK