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AZOR_COPPD
ID   AZOR_COPPD              Reviewed;         201 AA.
AC   B5Y659;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=COPRO5265_1481;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001145; ACI17053.1; -; Genomic_DNA.
DR   RefSeq; WP_012543705.1; NC_011295.1.
DR   AlphaFoldDB; B5Y659; -.
DR   SMR; B5Y659; -.
DR   STRING; 309798.COPRO5265_1481; -.
DR   EnsemblBacteria; ACI17053; ACI17053; COPRO5265_1481.
DR   KEGG; cpo:COPRO5265_1481; -.
DR   eggNOG; COG1182; Bacteria.
DR   HOGENOM; CLU_088964_3_1_9; -.
DR   OMA; HASGWLR; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000001732; 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   3: Inferred from homology;
KW   Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..201
FT                   /note="FMN-dependent NADH:quinone oxidoreductase"
FT                   /id="PRO_1000138972"
FT   BINDING         92..95
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
FT   BINDING         136..139
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   201 AA;  23175 MW;  68CD52D6CBEA61B9 CRC64;
     MAKVLYVKAN PKNNEESRTF RISEHFINEY KKAHPEDEII ELDLYKENIH FLSKEEINTI
     MSKDKSNLKD HPVLKYTYQF AEADKYVIAT PMWNLSIPAI LKAYFDYITV TGITFKYTEN
     GAVGLLKNKK AVVIMSTGGE YLTPPFDQWN FASTYVTTMF KFFGVEDVSL IAAQRLDIIG
     EDVEKRVSDA MKEAEQLAKQ F
 
 
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