AZR_BACSU
ID AZR_BACSU Reviewed; 174 AA.
AC O07529; Q796Y0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=FMN-dependent NADPH-azoreductase;
DE EC=1.7.-.-;
DE AltName: Full=Azobenzene reductase;
GN Name=azr; Synonyms=yhdA; OrderedLocusNames=BSU09340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, AND FUNCTION.
RC STRAIN=ISW1214;
RX PubMed=16861800; DOI=10.1271/bbb.60014;
RA Sugiura W., Yoda T., Matsuba T., Tanaka Y., Suzuki Y.;
RT "Expression and characterization of the genes encoding azoreductases from
RT Bacillus subtilis and Geobacillus stearothermophilus.";
RL Biosci. Biotechnol. Biochem. 70:1655-1665(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
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 [4]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16752898; DOI=10.1021/bi052478r;
RA Deller S., Sollner S., Trenker-El-Toukhy R., Jelesarov I., Guebitz G.M.,
RA Macheroux P.;
RT "Characterization of a thermostable NADPH:FMN oxidoreductase from the
RT mesophilic bacterium Bacillus subtilis.";
RL Biochemistry 45:7083-7091(2006).
RN [5]
RP INDUCTION BY CELL ENVELOPE STRESS.
RX PubMed=16816187; DOI=10.1128/jb.00310-06;
RA Jordan S., Junker A., Helmann J.D., Mascher T.;
RT "Regulation of LiaRS-dependent gene expression in Bacillus subtilis:
RT identification of inhibitor proteins, regulator binding sites, and target
RT genes of a conserved cell envelope stress-sensing two-component system.";
RL J. Bacteriol. 188:5153-5166(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FMN.
RG Midwest center for structural genomics (MCSG);
RT "Azobenzene reductase from Bacillus subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RC STRAIN=168;
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the putative NADPH-dependent azobenzene FMN-reductase
RT yhdA from Bacillus subtilis, Northeast structural genomics target SR135.";
RL Submitted (MAR-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic azo
CC compounds to the corresponding amines. Requires NADPH, but not NADH, as
CC an electron donor for its activity. {ECO:0000269|PubMed:16752898,
CC ECO:0000269|PubMed:16861800}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16752898, ECO:0000269|PubMed:16861800};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for NADPH {ECO:0000269|PubMed:16752898};
CC KM=20 uM for FMN {ECO:0000269|PubMed:16752898};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16752898, ECO:0000269|Ref.6,
CC ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC O07529; O07529: azr; NbExp=6; IntAct=EBI-7168398, EBI-7168398;
CC -!- INDUCTION: Part of the yhcYZ-yhdA operon that is induced by the two-
CC component regulatory system LiaS/LiaR in response to cell envelope
CC stress. {ECO:0000269|PubMed:16816187}.
CC -!- SIMILARITY: Belongs to the azoreductase type 2 family. {ECO:0000305}.
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DR EMBL; AB071368; BAB85976.1; -; mRNA.
DR EMBL; Y14079; CAA74434.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12762.1; -; Genomic_DNA.
DR PIR; G69824; G69824.
DR RefSeq; NP_388815.1; NC_000964.3.
DR RefSeq; WP_003244703.1; NZ_JNCM01000035.1.
DR PDB; 1NNI; X-ray; 2.50 A; 1=1-174.
DR PDB; 2GSW; X-ray; 2.92 A; A/B/C/D=1-174.
DR PDB; 3GFQ; X-ray; 3.00 A; A/B/C/D=1-174.
DR PDB; 3GFR; X-ray; 2.40 A; A/B/C/D=1-174.
DR PDB; 3GFS; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-174.
DR PDBsum; 1NNI; -.
DR PDBsum; 2GSW; -.
DR PDBsum; 3GFQ; -.
DR PDBsum; 3GFR; -.
DR PDBsum; 3GFS; -.
DR AlphaFoldDB; O07529; -.
DR SMR; O07529; -.
DR MINT; O07529; -.
DR STRING; 224308.BSU09340; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; O07529; -.
DR PRIDE; O07529; -.
DR DNASU; 936266; -.
DR EnsemblBacteria; CAB12762; CAB12762; BSU_09340.
DR GeneID; 936266; -.
DR KEGG; bsu:BSU09340; -.
DR PATRIC; fig|224308.179.peg.1007; -.
DR eggNOG; COG0431; Bacteria.
DR InParanoid; O07529; -.
DR OMA; PEYHSGM; -.
DR PhylomeDB; O07529; -.
DR BioCyc; BSUB:BSU09340-MON; -.
DR BRENDA; 1.7.1.6; 658.
DR SABIO-RK; O07529; -.
DR EvolutionaryTrace; O07529; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..174
FT /note="FMN-dependent NADPH-azoreductase"
FT /id="PRO_0000360624"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT BINDING 15..16
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT BINDING 73..76
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3GFS"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3GFS"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3GFS"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:3GFS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3GFS"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3GFS"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:3GFR"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3GFS"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3GFS"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3GFS"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:3GFS"
SQ SEQUENCE 174 AA; 18904 MW; A51E12FF6D9099D1 CRC64;
MNMLVINGTP RKHGRTRIAA SYIAALYHTD LIDLSEFVLP VFNGEAEQSE LLKVQELKQR
VTKADAIVLL SPEYHSGMSG ALKNALDFLS SEQFKYKPVA LLAVAGGGKG GINALNNMRT
VMRGVYANVI PKQLVLDPVH IDVENATVAE NIKESIKELV EELSMFAKAG NPGV
