NMO_PARPJ
ID NMO_PARPJ Reviewed; 366 AA.
AC B2TEK6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nitronate monooxygenase {ECO:0000305|PubMed:25002579};
DE Short=NMO {ECO:0000305|PubMed:25002579};
DE EC=1.13.12.- {ECO:0000269|PubMed:25002579};
DE AltName: Full=Propionate 3-nitronate monooxygenase {ECO:0000305|PubMed:25002579};
DE Short=P3N monooxygenase {ECO:0000305|PubMed:25002579};
GN OrderedLocusNames=Bphyt_4144 {ECO:0000312|EMBL:ACD18527.1};
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
RN [2]
RP FUNCTION.
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=20382807; DOI=10.1128/aem.00267-10;
RA Nishino S.F., Shin K.A., Payne R.B., Spain J.C.;
RT "Growth of bacteria on 3-nitropropionic acid as a sole source of carbon,
RT nitrogen, and energy.";
RL Appl. Environ. Microbiol. 76:3590-3598(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=25002579; DOI=10.1074/jbc.m114.577791;
RA Salvi F., Agniswamy J., Yuan H., Vercammen K., Pelicaen R., Cornelis P.,
RA Spain J.C., Weber I.T., Gadda G.;
RT "The combined structural and kinetic characterization of a bacterial
RT nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO
RT class I and II.";
RL J. Biol. Chem. 289:23764-23775(2014).
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 (PubMed:25002579). Is likely involved in the degradation of P3N, that
CC allows B.phytofirmans PsJN to grow on 3-nitropropionate/P3N as the sole
CC source of nitrogen and carbon (PubMed:20382807). Also probably
CC functions in the detoxification of P3N, a metabolic poison produced by
CC plants and fungi as a defense mechanism (PubMed:25002579). Cannot
CC oxidize nitroalkanes such as 3-nitropropionate, nitroethane, or 1-
CC nitropropane (PubMed:25002579). {ECO:0000269|PubMed:20382807,
CC ECO:0000269|PubMed:25002579}.
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:0000269|PubMed:25002579, ECO:0000305|PubMed:20382807};
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: At physiological pH, 3-nitropropionate (3-NPA) exists in
CC equilibrium with its conjugate base, propionate-3-nitronate (P3N).
CC {ECO:0000305}.
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|PubMed:25002579}.
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DR EMBL; CP001053; ACD18527.1; -; Genomic_DNA.
DR RefSeq; WP_012426043.1; NC_010676.1.
DR AlphaFoldDB; B2TEK6; -.
DR SMR; B2TEK6; -.
DR STRING; 398527.Bphyt_4144; -.
DR EnsemblBacteria; ACD18527; ACD18527; Bphyt_4144.
DR KEGG; bpy:Bphyt_4144; -.
DR eggNOG; COG2070; Bacteria.
DR HOGENOM; CLU_038732_5_1_4; -.
DR OMA; MDNARPF; -.
DR OrthoDB; 275153at2; -.
DR Proteomes; UP000001739; Chromosome 2.
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 1: Evidence at protein level;
KW Detoxification; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..366
FT /note="Nitronate monooxygenase"
FT /id="PRO_0000445422"
FT BINDING 74
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 181
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 186
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 223
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
FT BINDING 242..245
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HWH9"
SQ SEQUENCE 366 AA; 38062 MW; 062DF522D175541E CRC64;
MTDQTGKRAL LPLLGIDKPI IQAPMAGVST PALAAAVCNA GGLGSLGVGA MNADGARKVI
RETRALTDKP FNINVFCHRP AQADAAVEQQ WLSWLAPHFE KYGATPPAKL SDIYTSFLAD
PAMLAVFLEE KPAIVSFHFG LPSADVIAEL KKAGIRLLAS ATNLQEAAQV EAAGVDAIVA
QGIEAGGHRG VFDPDAFDDR LGTFALTRLL AKECRLPVIA AGGIMDGAGI AAALALGAQA
AQLGTAFVAC TETSIDEGYR RALLGEAARR TTFTAAISGR LARSMANSFT ALGADPRSPE
PATYPIAYDA GKALNAAAKA KGEFGYGAHW AGQAAALARS LPAAELVAQL ERELKQSIEQ
LRQFAN
