NMO_STAS1
ID NMO_STAS1 Reviewed; 355 AA.
AC Q49W60;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=SSP1854;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18999.1; -; Genomic_DNA.
DR RefSeq; WP_011303536.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49W60; -.
DR SMR; Q49W60; -.
DR STRING; 342451.SSP1854; -.
DR EnsemblBacteria; BAE18999; BAE18999; SSP1854.
DR KEGG; ssp:SSP1854; -.
DR PATRIC; fig|342451.11.peg.1850; -.
DR eggNOG; COG2070; Bacteria.
DR HOGENOM; CLU_038732_5_1_9; -.
DR OMA; MDNARPF; -.
DR OrthoDB; 275153at2; -.
DR Proteomes; UP000006371; 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; Reference proteome.
FT CHAIN 1..355
FT /note="Probable nitronate monooxygenase"
FT /id="PRO_0000360903"
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 219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 238..241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
SQ SEQUENCE 355 AA; 38661 MW; 6CFF39090AE90B53 CRC64;
MKLSTRVTGL LNVKYPIIQA GMAGSTTPEL VATVSNAGGL GTIGAGYFSS DRLEQEITYL
QELTDLPYAV NLFVPSDKLY IPEKVEHMNA WLKPYRRAFN IEEPVINMTE KQQFKDAIDL
VIEKGVPAVS FTFGIPEQTV IEKLKERHIK LIGTATSVEE AIANESAGMD MVIAQGSEAG
GHRGAFSETA SQLTPLIGTM SLVPQMVDQI NIPVVAAGGI MDGRGLVASM VLGAEGVQMG
TAFLTSDESG ASQLYKHAIS QSKETDTVVT NVITGKPARG IENEFIHKMN EYDDEIPDYP
IQNQLTNALR KEAANKGNAQ WTHLWSGQSP RLVQHMSAWA LIENVVKQAN EIMNR