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Database: UniProt
Entry: A0A1L3MWT6_9BACI
LinkDB: A0A1L3MWT6_9BACI
Original site: A0A1L3MWT6_9BACI 
ID   A0A1L3MWT6_9BACI        Unreviewed;       136 AA.
AC   A0A1L3MWT6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Probable nitronate monooxygenase {ECO:0000256|ARBA:ARBA00013457};
DE   AltName: Full=Propionate 3-nitronate monooxygenase {ECO:0000256|ARBA:ARBA00031155};
GN   ORFNames=A9C19_20210 {ECO:0000313|EMBL:APH06809.1};
OS   Bacillus weihaiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH06809.1, ECO:0000313|Proteomes:UP000181936};
RN   [1] {ECO:0000313|EMBL:APH06809.1, ECO:0000313|Proteomes:UP000181936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alg07 {ECO:0000313|EMBL:APH06809.1,
RC   ECO:0000313|Proteomes:UP000181936};
RX   PubMed=27901120; DOI=10.1038/srep38248;
RA   Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT   "Complete genome sequence and transcriptomic analysis of a novel marine
RT   strain Bacillus weihaiensis reveals the mechanism of brown algae
RT   degradation.";
RL   Sci. Rep. 6:38248-38248(2016).
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:0000256|ARBA:ARBA00003535}.
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:0000256|ARBA:ARBA00000219};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the nitronate monooxygenase family. NMO class I
CC       subfamily. {ECO:0000256|ARBA:ARBA00009881}.
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DR   EMBL; CP016020; APH06809.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L3MWT6; -.
DR   STRING; 1547283.A9C19_20210; -.
DR   KEGG; bwh:A9C19_20210; -.
DR   OrthoDB; 9778912at2; -.
DR   Proteomes; UP000181936; Chromosome.
DR   GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004136; NMO.
DR   PANTHER; PTHR42747; NITRONATE MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR42747:SF3; NITRONATE MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF03060; NMO; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE   3: Inferred from homology;
KW   Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000181936}.
FT   DOMAIN          1..128
FT                   /note="Nitronate monooxygenase"
FT                   /evidence="ECO:0000259|Pfam:PF03060"
SQ   SEQUENCE   136 AA;  15146 MW;  679634E4DD2E511B CRC64;
     MDGRGLMASI CLGAEGVQMG TAFLTCIESG ASEIHKEEVL HTPENQTIMT RSFSGKWARG
     IKNEFIFEMQ KSEELLPNFP VQNTLTKGIR KAATLQKNRE FMSLWSGQSP RLAKKQTVKS
     LIESIVEEAT LILSNK
//
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