AZOR_YERPE
ID AZOR_YERPE Reviewed; 201 AA.
AC Q8ZE60; Q0WEJ8;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216};
GN OrderedLocusNames=YPO2323, y2010, YP_2110;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4] {ECO:0007744|PDB:4ESE}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH FMN.
RA Tan K., Gu M., Kwon K., Anderson W.F., Joachimiak A.;
RT "The crystal structure of acyl carrier protein phosphodiesterase from
RT Yersinia pestis CO92 in complex with FMN.";
RL Submitted (APR-2012) to the PDB data bank.
RN [5] {ECO:0007744|PDB:5JRO}
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS).
RA Tan K., Gu M., Kwon K., Anderson W.F., Joachimiak A.;
RT "The crystal structure of azoreductase from Yersinia pestis CO92 in its Apo
RT form.";
RL Submitted (MAY-2016) to the PDB data bank.
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; AL590842; CAL20951.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85576.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62319.1; -; Genomic_DNA.
DR PIR; AD0283; AD0283.
DR RefSeq; WP_002211004.1; NZ_WUCM01000054.1.
DR RefSeq; YP_002347290.1; NC_003143.1.
DR PDB; 4ESE; X-ray; 1.45 A; A=1-201.
DR PDB; 5JRO; X-ray; 2.54 A; A/B=1-201.
DR PDBsum; 4ESE; -.
DR PDBsum; 5JRO; -.
DR AlphaFoldDB; Q8ZE60; -.
DR SMR; Q8ZE60; -.
DR STRING; 214092.YPO2323; -.
DR PaxDb; Q8ZE60; -.
DR DNASU; 1146957; -.
DR EnsemblBacteria; AAM85576; AAM85576; y2010.
DR EnsemblBacteria; AAS62319; AAS62319; YP_2110.
DR GeneID; 66841327; -.
DR KEGG; ype:YPO2323; -.
DR KEGG; ypk:y2010; -.
DR KEGG; ypm:YP_2110; -.
DR PATRIC; fig|214092.21.peg.2728; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_0_0_6; -.
DR OMA; AGITFKY; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..201
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_0000166318"
FT BINDING 10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4ESE"
FT BINDING 16..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4ESE"
FT BINDING 96..99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4ESE"
FT BINDING 140..143
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:4ESE"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4ESE"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4ESE"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:4ESE"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4ESE"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:4ESE"
SQ SEQUENCE 201 AA; 21600 MW; 05F597A420E789D0 CRC64;
MSKVLVLKSS ILATSSQSNQ LADFFVEQWQ AAHAGDQITV RDLAAQPIPV LDGELVGALR
PSGTALTPRQ QEALALSDEL IAELQANDVI VIAAPMYNFN IPTQLKNYFD MIARAGVTFR
YTEKGPEGLV TGKRAIILTS RGGIHKDTPT DLVVPYLRLF LGFIGITDVE FVFAEGIAYG
PEVATKAQAD AKTLLAQVVA A
