ID A0A0B2C2L7_9SPHN Unreviewed; 197 AA.
AC A0A0B2C2L7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=PK98_07010 {ECO:0000313|EMBL:KHL26226.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26226.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL26226.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL26226.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHL26226.1}.
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DR EMBL; JTDN01000001; KHL26226.1; -; Genomic_DNA.
DR RefSeq; WP_039095308.1; NZ_JTDN01000001.1.
DR AlphaFoldDB; A0A0B2C2L7; -.
DR STRING; 1572751.PK98_07010; -.
DR OrthoDB; 9787136at2; -.
DR Proteomes; UP000030988; 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:UP000030988}.
FT DOMAIN 1..196
FT /note="Flavodoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF02525"
FT BINDING 15..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT BINDING 95..98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT BINDING 139..142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ SEQUENCE 197 AA; 21325 MW; 8AAC6EDABB096052 CRC64;
MQILRIDSAT TGDDSVSGRL TQMLLDHFTA AHPDATVISH DYGTDPLPHL TPVTTGAIRR
PEEARTPEMQ AAYPAERAIL DEFLASDIVI LGAPMYNFTI PSQLKAWIDR LGVPRVTFSY
DENGPKGLAG GRRVIVASSR GGDYNQGDAG EHQETYLKTV FNFLGIDPEF VRVNKAGFGP
EAVEAGLAAA KEEIAKL
//