ID A9BQX0_DELAS Unreviewed; 357 AA.
AC A9BQX0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Propionate 3-nitronate monooxygenase {ECO:0000256|ARBA:ARBA00031155};
GN OrderedLocusNames=Daci_0279 {ECO:0000313|EMBL:ABX32925.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX32925.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX32925.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX32925.1; -; Genomic_DNA.
DR RefSeq; WP_012202218.1; NC_010002.1.
DR AlphaFoldDB; A9BQX0; -.
DR STRING; 398578.Daci_0279; -.
DR GeneID; 24115600; -.
DR KEGG; dac:Daci_0279; -.
DR eggNOG; COG2070; Bacteria.
DR HOGENOM; CLU_038732_5_0_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd04730; NPD_like; 1.
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 Dioxygenase {ECO:0000313|EMBL:ABX32925.1};
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:UP000000784}.
FT DOMAIN 12..347
FT /note="Nitronate monooxygenase"
FT /evidence="ECO:0000259|Pfam:PF03060"
SQ SEQUENCE 357 AA; 36583 MW; D6B1F7D2F5B38C0D CRC64;
MSTEKTAWMA RLGMRHPIIQ APMAGTSTPA LAAAVTEAGG LGSLGIGASG TEQARQQIVQ
TRALTSGAFN VNLFCHRPAR ADAQREAAWL AHLAPEFARF GAKPPAGLNE IYATAVGNAA
LQAMLLQERP AVVSFHFGLP EQGFIDALRA AGVVTLASAT SLDEARQVEQ AGVDAIVAQG
VEAGGHRGTF DPAQDRMMGT FALVRVLARN TALPVIAAGG IMDGEGIAAA LGLGACAAQL
GTAFILCPES SASPAFRAEL RSERAHHTGI TAAISGRPAR GMVNRLHALG ASHGQPLPDY
PRVYDAGKAL HQAASAQGSS DYAAHWAGQG APLAREMPAA ALVQTLAGEL ASAQAGR
//