AZOR1_BACAN
ID AZOR1_BACAN Reviewed; 220 AA.
AC Q81UB2; Q6I2J7; Q6KWC6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase 1 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN Name=azoR1 {ECO:0000255|HAMAP-Rule:MF_01216};
GN OrderedLocusNames=BA_0966, GBAA_0966, BAS0908;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones. {ECO:0000255|HAMAP-
CC Rule:MF_01216}.
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:0000255|HAMAP-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: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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01216}.
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DR EMBL; AE016879; AAP24957.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53234.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30073.1; -; Genomic_DNA.
DR RefSeq; NP_843471.1; NC_003997.3.
DR RefSeq; WP_001044344.1; NZ_WXXJ01000014.1.
DR RefSeq; YP_027183.1; NC_005945.1.
DR PDB; 3U7I; X-ray; 1.75 A; A/B/C/D=1-220.
DR PDB; 4M0C; X-ray; 2.07 A; A/B=1-220.
DR PDBsum; 3U7I; -.
DR PDBsum; 4M0C; -.
DR AlphaFoldDB; Q81UB2; -.
DR SMR; Q81UB2; -.
DR STRING; 261594.GBAA_0966; -.
DR DNASU; 1088173; -.
DR EnsemblBacteria; AAP24957; AAP24957; BA_0966.
DR EnsemblBacteria; AAT30073; AAT30073; GBAA_0966.
DR GeneID; 45021014; -.
DR KEGG; ban:BA_0966; -.
DR KEGG; bar:GBAA_0966; -.
DR KEGG; bat:BAS0908; -.
DR PATRIC; fig|198094.11.peg.959; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_3_0_9; -.
DR OMA; QFKAHHR; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 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 3D-structure; Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..220
FT /note="FMN-dependent NADH:quinone oxidoreductase 1"
FT /id="PRO_0000245873"
FT BINDING 18..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3U7I"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3U7I"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3U7I"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3U7I"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:3U7I"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3U7I"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3U7I"
FT HELIX 192..211
FT /evidence="ECO:0007829|PDB:3U7I"
SQ SEQUENCE 220 AA; 25369 MW; B37E289D2AD1A0A5 CRC64;
MNKTLIINAH PKVDDTSSVS IKVFKHFLES YKELISNNET IEQINLYDDV VPMIDKTVLS
AWEKQGNGQE LTREEQKVTE RMSEILQQFK SANTYVIVLP LHNFNIPSKL KDYMDNIMIA
RETFKYTETG SVGLLKDGRR MLVIQASGGI YTNDDWYTDV EYSHKYLKAM FNFLGIEDYQ
IVRAQGTAVL DPTEVLQNAY KEVEEAASRL ANKYIFSLEE
