AZOR2_BACSU
ID AZOR2_BACSU Reviewed; 211 AA.
AC O32224;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase 2 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17284825};
GN Name=azoR2 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000303|PubMed:17725564};
GN Synonyms=yvaB; OrderedLocusNames=BSU33540;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=17284825; DOI=10.1271/bbb.60548;
RA Nishiya Y., Yamamoto Y.;
RT "Characterization of a NADH:dichloroindophenol oxidoreductase from Bacillus
RT subtilis.";
RL Biosci. Biotechnol. Biochem. 71:611-614(2007).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17725564; DOI=10.1111/j.1365-2958.2007.05891.x;
RA Toewe S., Leelakriangsak M., Kobayashi K., Van Duy N., Hecker M., Zuber P.,
RA Antelmann H.;
RT "The MarR-type repressor MhqR (YkvE) regulates multiple
RT dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-
RT methylhydroquinone and catechol in Bacillus subtilis.";
RL Mol. Microbiol. 66:40-54(2007).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=18208493; DOI=10.1111/j.1365-2958.2008.06110.x;
RA Leelakriangsak M., Huyen N.T.T., Toewe S., van Duy N., Becher D.,
RA Hecker M., Antelmann H., Zuber P.;
RT "Regulation of quinone detoxification by the thiol stress sensing
RT DUF24/MarR-like repressor, YodB in Bacillus subtilis.";
RL Mol. Microbiol. 67:1108-1124(2008).
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones (Probable). Contributes to
CC resistance to 2-methylhydroquinone (2-MHQ) and catechol
CC (PubMed:17725564, PubMed:18208493). Exhibits NADH-dependent 2,6-
CC dichloroindophenol (DCIP) oxidoreductase activity (PubMed:17284825).
CC {ECO:0000269|PubMed:17284825, ECO:0000269|PubMed:17725564,
CC ECO:0000269|PubMed:18208493, ECO:0000305|PubMed:18208493}.
CC -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC cleavage of the azo bond in aromatic azo compounds to the corresponding
CC amines (PubMed:17284825). Can reduce methyl red (PubMed:17284825).
CC {ECO:0000269|PubMed:17284825}.
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01216, ECO:0000269|PubMed:17284825};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC Evidence={ECO:0000269|PubMed:17284825};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:17284825};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:17284825};
CC -!- ACTIVITY REGULATION: Strongly inhibited by Pb(2+) and weakly inhibited
CC by Cu(2+), Hg(2+) and Fe(2+). Stable in presence of Ag(+).
CC {ECO:0000269|PubMed:17284825}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for 2,6-dichloroondophenol (DCIP) (at pH 7.5 and at 25
CC degrees Celsius) {ECO:0000269|PubMed:17284825};
CC KM=190 uM for NADH (at pH 7.5 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:17284825};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17284825};
CC Temperature dependence:
CC Activity increases linearly up to 40 degrees Celsius. Stable up to 55
CC degrees Celsius after incubation for 30 min at pH 7.5. During
CC incubation at 25 degrees Celsius for 16h, the enzyme is stable
CC between pH 5.5 and 9.0, where 80% activity is observed.
CC {ECO:0000269|PubMed:17284825};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:17284825}.
CC -!- INDUCTION: Repressed by MhqR. Induced by thiol specific stress
CC conditions, such as exposure to 2-methylhydroquinone (2-MHQ), catechol
CC or diamide. Not induced by oxidative stress due to hydrogen peroxide or
CC methylglyoxal. {ECO:0000269|PubMed:17725564}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is sensitive to 2-MHQ and
CC catechol. {ECO:0000269|PubMed:17725564}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL009126; CAB15359.1; -; Genomic_DNA.
DR PIR; H70026; H70026.
DR RefSeq; NP_391234.1; NC_000964.3.
DR RefSeq; WP_003243587.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32224; -.
DR SMR; O32224; -.
DR STRING; 224308.BSU33540; -.
DR jPOST; O32224; -.
DR PaxDb; O32224; -.
DR PRIDE; O32224; -.
DR EnsemblBacteria; CAB15359; CAB15359; BSU_33540.
DR GeneID; 936142; -.
DR KEGG; bsu:BSU33540; -.
DR PATRIC; fig|224308.179.peg.3639; -.
DR eggNOG; COG1182; Bacteria.
DR InParanoid; O32224; -.
DR OMA; AGITFKY; -.
DR PhylomeDB; O32224; -.
DR BioCyc; BSUB:BSU33540-MON; -.
DR SABIO-RK; O32224; -.
DR Proteomes; UP000001570; Chromosome.
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 GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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 Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Detoxification;
KW Direct protein sequencing; Flavoprotein; FMN; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17284825"
FT CHAIN 2..211
FT /note="FMN-dependent NADH:quinone oxidoreductase 2"
FT /id="PRO_0000166329"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ SEQUENCE 211 AA; 23272 MW; DE8C5ABFDCA423C0 CRC64;
MAKVLYITAH PHDEATSYSM ATGKAFIESY KEANPNDEVV HIDLYKENIP HIDADVFSGW
GKLQSGTGFE ELSESEKAKV GRLGELSDQF ASADKYVFVT PLWNFSFPPV MKAYLDSVAV
AGKSFKYTEQ GPVGLLTDKK AIHIQARGGY YSEGPAAEME MGHRYIGIMM NFFGVPSFDG
IFVEGHNAEP DKAQQIKEDA IARAKEAGKT F
