NMO_BACSU
ID NMO_BACSU Reviewed; 347 AA.
AC O05413; Q796A1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Name=yrpB; OrderedLocusNames=BSU26800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA Duesterhoeft A., Ehrlich S.D.;
RT "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT operon reveals two new extracytoplasmic function RNA polymerase sigma
RT factors SigV and SigZ.";
RL Microbiology 143:2939-2943(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; U93875; AAB80891.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14621.1; -; Genomic_DNA.
DR PIR; B69978; B69978.
DR RefSeq; NP_390557.1; NC_000964.3.
DR RefSeq; WP_003229861.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O05413; -.
DR SMR; O05413; -.
DR STRING; 224308.BSU26800; -.
DR PaxDb; O05413; -.
DR PRIDE; O05413; -.
DR EnsemblBacteria; CAB14621; CAB14621; BSU_26800.
DR GeneID; 936455; -.
DR KEGG; bsu:BSU26800; -.
DR PATRIC; fig|224308.179.peg.2911; -.
DR eggNOG; COG2070; Bacteria.
DR InParanoid; O05413; -.
DR OMA; MDNARPF; -.
DR PhylomeDB; O05413; -.
DR BioCyc; BSUB:BSU26800-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IBA:GO_Central.
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..347
FT /note="Probable nitronate monooxygenase"
FT /id="PRO_0000360890"
FT BINDING 69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 171
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 213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 232..235
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
SQ SEQUENCE 347 AA; 38069 MW; B150932712F10D6E CRC64;
MNEFMKKFSL TKPIIQAPMA GGITKPRLAS AVSNQGALGS LASGYLTPDL LEQQIKEIFE
LTDAPFQINV FVPLGLEMPP KDQIKKWKEN IPLANQVNQF TSVQEEWDDF YQKIDLILKY
KVKACSFTFD LPPEDAVKEL KTAGCCLIGT ASTVEEALLM EERGMDIVVL QGSEAGGHRG
AFLPSKGESA VGLMALIPQA ADALSVPVIA AGGMIDHRGV KAALTLGAQG VQIGSAFLIC
HESNAHPVHK QKILEANEAD TKLTTLFSGK EARGIVNKWM EENEQFETQT LPYPYQNTLT
KAMRQKASLQ NNHDQMSLWA GQGIRSLTEE ISVKQLLNQL CQEDIKI
