ID A0A0H4KE69_9BACI Unreviewed; 211 AA.
AC A0A0H4KE69; A0A1X7FVR5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=FMN dependent NADH:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000256|HAMAP-Rule:MF_01216};
GN Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN ORFNames=B1B01_19880 {ECO:0000313|EMBL:OXS66244.1}, BEH_02325
GN {ECO:0000313|EMBL:AKO91056.1}, CJ485_12790
GN {ECO:0000313|EMBL:RJS65584.1}, SAMN06296056_106125
GN {ECO:0000313|EMBL:SMF59600.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:AKO91056.1, ECO:0000313|Proteomes:UP000036202};
RN [1] {ECO:0000313|EMBL:AKO91056.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91056.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKO91056.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91056.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000215399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:OXS66244.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS66244.1}, and SGD-14
RC {ECO:0000313|EMBL:SMF59600.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Proteomes:UP000192915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:RJS65584.1, ECO:0000313|Proteomes:UP000274910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PK5_39 {ECO:0000313|EMBL:RJS65584.1,
RC ECO:0000313|Proteomes:UP000274910};
RA Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., Bajic V.B.,
RA Hirt H.;
RT "Complete genomes of four Endophytic plant-growth promoting Bacillus that
RT were isolated from a desert in Pakistan.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC cleavage of the azo bond in aromatic azo compounds to the corresponding
CC amines. {ECO:0000256|HAMAP-Rule:MF_01216}.
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones. {ECO:0000256|HAMAP-
CC Rule:MF_01216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+);
CC Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) =
CC 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH;
CC Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:71579; EC=1.7.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00023925};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC Evidence={ECO:0000256|ARBA:ARBA00023925};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01216};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01216};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01216}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000256|HAMAP-Rule:MF_01216}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01216}.
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DR EMBL; CP011974; AKO91056.1; -; Genomic_DNA.
DR EMBL; MWSI01000006; OXS66244.1; -; Genomic_DNA.
DR EMBL; NQYF01000001; RJS65584.1; -; Genomic_DNA.
DR EMBL; FXAJ01000006; SMF59600.1; -; Genomic_DNA.
DR RefSeq; WP_040060743.1; NZ_NQYF01000001.1.
DR AlphaFoldDB; A0A0H4KE69; -.
DR GeneID; 72761140; -.
DR KEGG; beo:BEH_02325; -.
DR PATRIC; fig|135735.6.peg.423; -.
DR OrthoDB; 9805013at2; -.
DR Proteomes; UP000036202; Chromosome.
DR Proteomes; UP000192915; Unassembled WGS sequence.
DR Proteomes; UP000215399; Unassembled WGS sequence.
DR Proteomes; UP000274910; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_01216; Azoreductase_type1; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR023048; NADH:quinone_OxRdtase_FMN_depd.
DR PANTHER; PTHR43741; FMN-DEPENDENT NADH-AZOREDUCTASE 1; 1.
DR PANTHER; PTHR43741:SF7; FMN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01216};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01216};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01216};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01216}; Reference proteome {ECO:0000313|Proteomes:UP000036202}.
FT DOMAIN 3..206
FT /note="Flavodoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF02525"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ SEQUENCE 211 AA; 23521 MW; 0E5C2787743C07F0 CRC64;
MAKVLYITAH PHDEKTSYSM AAGQAFVTAY KEQNPSDEIV HIDLYKENIP HIDADIFSGW
GKLQSGSEFD QLSKEEQSKV ARLAELNEQF ISADKYVFVT PLWNFSFPPV MKAYLDSVAV
AGKSFKYTEQ GPVGLLTDKK ALHIQARGGY YSEGPAADLE MGHRYIGIMM NFFGVPSFDG
LFIEGHNAEP NKAEQIKEDG IARAKELAKS F
//
