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Database: UniProt
Entry: K9T6N7_9CYAN
LinkDB: K9T6N7_9CYAN
Original site: K9T6N7_9CYAN 
ID   K9T6N7_9CYAN            Unreviewed;       202 AA.
AC   K9T6N7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=FMN dependent NADH:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000256|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN   ORFNames=Ple7327_2827 {ECO:0000313|EMBL:AFY78088.1};
OS   Pleurocapsa sp. PCC 7327.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY78088.1, ECO:0000313|Proteomes:UP000010382};
RN   [1] {ECO:0000313|EMBL:AFY78088.1, ECO:0000313|Proteomes:UP000010382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY78088.1,
RC   ECO:0000313|Proteomes:UP000010382};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished genome of Pleurocapsa sp. PCC 7327.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01216}.
CC   -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC       stress caused by electrophilic quinones. {ECO:0000256|HAMAP-
CC       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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00023925};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC         Evidence={ECO:0000256|ARBA:ARBA00023925};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01216};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01216};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01216}.
CC   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01216}.
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DR   EMBL; CP003590; AFY78088.1; -; Genomic_DNA.
DR   RefSeq; WP_015144389.1; NC_019689.1.
DR   AlphaFoldDB; K9T6N7; -.
DR   STRING; 118163.Ple7327_2827; -.
DR   KEGG; plp:Ple7327_2827; -.
DR   PATRIC; fig|118163.3.peg.3154; -.
DR   eggNOG; COG1182; Bacteria.
DR   HOGENOM; CLU_088964_0_0_3; -.
DR   Proteomes; UP000010382; 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   PANTHER; PTHR43741; FMN-DEPENDENT NADH-AZOREDUCTASE 1; 1.
DR   PANTHER; PTHR43741:SF4; FMN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01216};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01216};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01216};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01216}; Reference proteome {ECO:0000313|Proteomes:UP000010382}.
FT   DOMAIN          4..197
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
FT   BINDING         10
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         16..18
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         96..99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         137..140
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   202 AA;  22857 MW;  D60668ED01F97FD3 CRC64;
     MSCILHLDSS SRGSRSISRA LTKEFVARWL QIHPGDRVTY RDVGQYPVPP VDEAWIAASF
     SKSEDLAPEL ASALSVSDEL IDELLIADRY VFGIPMYNFS ISANFKAYID QIVRVNRTFT
     SDWQGLVKNK KMLIITTRGG SYSDASSNQL DFQEPYLRTV FEFIGITDIT FIHAENLTMG
     DESRQQSLRE AHIAIQNLVA IW
//
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