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Entry: A0A1H8YFD9_9PSEU
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ID   A0A1H8YFD9_9PSEU        Unreviewed;       230 AA.
AC   A0A1H8YFD9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN04489732_11587 {ECO:0000313|EMBL:SEP50960.1};
OS   Amycolatopsis saalfeldensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP50960.1, ECO:0000313|Proteomes:UP000198582};
RN   [1] {ECO:0000313|EMBL:SEP50960.1, ECO:0000313|Proteomes:UP000198582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP50960.1,
RC   ECO:0000313|Proteomes:UP000198582};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01216}.
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DR   EMBL; FOEF01000015; SEP50960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8YFD9; -.
DR   STRING; 394193.SAMN04489732_11587; -.
DR   Proteomes; UP000198582; Unassembled WGS sequence.
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:UP000198582}.
FT   DOMAIN          10..183
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
FT   BINDING         16
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         22..24
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         109..112
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   230 AA;  24893 MW;  355451FEC6395DF7 CRC64;
     MTDMLTEALL LHLDSSADGA ESVSRRLTAL FASAWRGPVR RRDLAEEPVP LIRAPYTTLG
     RRVERRGATA LDDVAALAAD EGELREWALT RPLIDQVRAA HTVLLGVPMY NFTVPATLKA
     WIDRLTFPGA FTGPATGEQV LRGTNFVVVL ARGGGYGPGT PREAFDFQLP YLRAYLTNLG
     VAPERLSFVK AELTRVREIP ALAGMEPLAA ESLATAIAEV TELAGKLQAQ
//
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