AZOR4_BACAN
ID AZOR4_BACAN Reviewed; 208 AA.
AC Q81JP2; Q6HQ88; Q6KJM2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase 4 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase 4 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase 4 {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase 4 {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN Name=azoR4 {ECO:0000255|HAMAP-Rule:MF_01216};
GN OrderedLocusNames=BA_5660, GBAA_5660, BAS5262;
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}.
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; AE016879; AAP29294.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57550.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34812.1; -; Genomic_DNA.
DR RefSeq; NP_847808.1; NC_003997.3.
DR RefSeq; WP_000170049.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031500.1; NC_005945.1.
DR PDB; 3P0R; X-ray; 1.80 A; A=1-208.
DR PDBsum; 3P0R; -.
DR AlphaFoldDB; Q81JP2; -.
DR SMR; Q81JP2; -.
DR STRING; 260799.BAS5262; -.
DR DNASU; 1085393; -.
DR EnsemblBacteria; AAP29294; AAP29294; BA_5660.
DR EnsemblBacteria; AAT34812; AAT34812; GBAA_5660.
DR GeneID; 45025237; -.
DR KEGG; ban:BA_5660; -.
DR KEGG; bar:GBAA_5660; -.
DR KEGG; bat:BAS5262; -.
DR PATRIC; fig|198094.11.peg.5620; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_3_1_9; -.
DR OMA; HASGWLR; -.
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..208
FT /note="FMN-dependent NADH:quinone oxidoreductase 4"
FT /id="PRO_0000245876"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3P0R"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3P0R"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:3P0R"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3P0R"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3P0R"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:3P0R"
SQ SEQUENCE 208 AA; 22840 MW; A7361329D57EBDD6 CRC64;
MTKVLFVKAN NRPAEQAVSV KLYEAFLASY KEAHPNDTVV ELDLYKEELP YVGVDMINGT
FKAGKGFDLT EEEAKAVAVA DKYLNQFLEA DKVVFGFPLW NLTIPAVLHT YIDYLNRAGK
TFKYTPEGPV GLIGDKKIAL LNARGGVYSE GPAAEVEMAV KYVASMMGFF GATNMETVVI
EGHNQFPDKA EEIITAGLEE AAKVANKF
