ID K0AB01_EXIAB Unreviewed; 209 AA.
AC K0AB01;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=azoR2 {ECO:0000313|EMBL:AFS70693.1};
GN Synonyms=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN OrderedLocusNames=Eab7_1582 {ECO:0000313|EMBL:AFS70693.1};
OS Exiguobacterium antarcticum (strain B7).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1087448 {ECO:0000313|EMBL:AFS70693.1, ECO:0000313|Proteomes:UP000006274};
RN [1] {ECO:0000313|EMBL:AFS70693.1, ECO:0000313|Proteomes:UP000006274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|Proteomes:UP000006274};
RX PubMed=23144424; DOI=10.1128/JB.01791-12;
RA Carneiro A.R., Ramos R.T., Dall'Agnol H., Pinto A.C., de Castro Soares S.,
RA Santos A.R., Guimaraes L.C., Almeida S.S., Barauna R.A., das Gracas D.A.,
RA Franco L.C., Ali A., Hassan S.S., Nunes C.I., Barbosa M.S., Fiaux K.K.,
RA Aburjaile F.F., Barbosa E.G., Bakhtiar S.M., Vilela D., Nobrega F.,
RA Dos Santos A.L., Carepo M.S., Azevedo V., Schneider M.P., Pellizari V.H.,
RA Silva A.;
RT "Genome sequence of Exiguobacterium antarcticum B7, isolated from a biofilm
RT in Ginger Lake, King George Island, Antarctica.";
RL J. Bacteriol. 194:6689-6690(2012).
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; CP003063; AFS70693.1; -; Genomic_DNA.
DR RefSeq; WP_014970549.1; NC_018665.1.
DR AlphaFoldDB; K0AB01; -.
DR KEGG; ean:Eab7_1582; -.
DR PATRIC; fig|1087448.3.peg.1635; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_3_0_9; -.
DR Proteomes; UP000006274; 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}.
FT DOMAIN 3..204
FT /note="Flavodoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF02525"
FT BINDING 100..103
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT BINDING 144..147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ SEQUENCE 209 AA; 23836 MW; DB60DAD2D415A9B1 CRC64;
MSRLLFIEAN DSTHQSKGIS SEMNETFLSS YRTHHPEDDI IVLNLFEERL PFFDLKLAMS
AAKLFRGESL DTDESVPVEK LQEYLRGFLE ADKIVFSFPM WNLTVPAPLH NYMDYLAQAG
QTFRYTPDGS VGLVKGKQVL LLHSRGGDYS TPDKVDTDHA VRYMIDILRF FGIEDVETII
LEGHQQYPDQ AEHLIKKALS ACEKAGQQF
//
