AZOR1_PSEPK
ID AZOR1_PSEPK Reviewed; 203 AA.
AC Q88IY3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; OrderedLocusNames=PP_2866;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN68474.1; -; Genomic_DNA.
DR RefSeq; NP_745010.1; NC_002947.4.
DR RefSeq; WP_010953771.1; NC_002947.4.
DR PDB; 4C0W; X-ray; 1.60 A; A=1-201.
DR PDB; 4C0X; X-ray; 1.50 A; A=1-201.
DR PDB; 4C14; X-ray; 1.90 A; A=1-203.
DR PDBsum; 4C0W; -.
DR PDBsum; 4C0X; -.
DR PDBsum; 4C14; -.
DR AlphaFoldDB; Q88IY3; -.
DR SMR; Q88IY3; -.
DR STRING; 160488.PP_2866; -.
DR EnsemblBacteria; AAN68474; AAN68474; PP_2866.
DR KEGG; ppu:PP_2866; -.
DR PATRIC; fig|160488.4.peg.3038; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_0_0_6; -.
DR OMA; GAPFYNF; -.
DR PhylomeDB; Q88IY3; -.
DR BioCyc; PPUT160488:G1G01-3045-MON; -.
DR BRENDA; 1.7.1.17; 5092.
DR Proteomes; UP000000556; 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..203
FT /note="FMN-dependent NADH:quinone oxidoreductase 1"
FT /id="PRO_0000245952"
FT BINDING 9
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 15..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 95..98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT BINDING 139..142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4C0X"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4C0X"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4C0X"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4C0X"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:4C0X"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:4C0X"
SQ SEQUENCE 203 AA; 21365 MW; AFCB5A15FF8D8FCF CRC64;
MKLLHIDSSI LGDNSASRQL SREVVEAWKA ADPSVEVVYR DLAADAIAHF SAATLVAAGT
PEDVRDAAQA FEAKLSAETL EEFLAADAVV IGAPMYNFTV PTQLKAWIDR VAVAGKTFRY
TEAGPQGLCG NKKVVLVSTA GGLHAGQPTG AGHEDFLKVF LGFIGITDLE IVRAHGLAYG
PEQRSQAIDA AQAQIASELF AAA
