ID A0A179ES79_ENTTH Unreviewed; 206 AA.
AC A0A179ES79;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-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=acpH {ECO:0000313|EMBL:GEK37275.1};
GN Synonyms=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN ORFNames=A6E74_05110 {ECO:0000313|EMBL:OAQ56101.1}, CK496_10570
GN {ECO:0000313|EMBL:ASZ08328.1}, ETH01_15620
GN {ECO:0000313|EMBL:GEK37275.1};
OS Enterococcus thailandicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=417368 {ECO:0000313|EMBL:OAQ56101.1, ECO:0000313|Proteomes:UP000078516};
RN [1] {ECO:0000313|EMBL:OAQ56101.1, ECO:0000313|Proteomes:UP000078516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0711D 46 {ECO:0000313|EMBL:OAQ56101.1,
RC ECO:0000313|Proteomes:UP000078516};
RA Beukers A.G., Zaheer R., Goji N., Cook S.R., Amoako K., Chaves A.V.,
RA Ward M.P., Mcallister T.A.;
RT "Draft genome of an Enterococcus thailandicus strain isolated from bovine
RT feces.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ASZ08328.1, ECO:0000313|Proteomes:UP000217197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a523 {ECO:0000313|Proteomes:UP000217197}, and A523
RC {ECO:0000313|EMBL:ASZ08328.1};
RA Ybazeta G., Douglas L., Graham J., Fraleigh N., Murad Y., Perez J.,
RA Diaz-Mitoma F., Nokhbeh R.;
RT "Whole genome sequencing and hybrid de novo assembly of Enterococcus
RT thailandicus a523.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEK37275.1, ECO:0000313|Proteomes:UP000321361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101867 {ECO:0000313|EMBL:GEK37275.1,
RC ECO:0000313|Proteomes:UP000321361};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Enterococcus thailandicus NBRC 101867.";
RL Submitted (JUL-2019) 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; CP023074; ASZ08328.1; -; Genomic_DNA.
DR EMBL; BJUG01000007; GEK37275.1; -; Genomic_DNA.
DR EMBL; LWMN01000011; OAQ56101.1; -; Genomic_DNA.
DR RefSeq; WP_067482848.1; NZ_LWMN01000011.1.
DR AlphaFoldDB; A0A179ES79; -.
DR GeneID; 77488079; -.
DR KEGG; eth:CK496_10570; -.
DR PATRIC; fig|417368.6.peg.653; -.
DR OrthoDB; 9805013at2; -.
DR Proteomes; UP000078516; Unassembled WGS sequence.
DR Proteomes; UP000217197; Chromosome.
DR Proteomes; UP000321361; 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:SF7; 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:UP000078516}.
FT DOMAIN 3..201
FT /note="Flavodoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF02525"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT BINDING 146..149
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ SEQUENCE 206 AA; 23225 MW; B108BEBD4A8ED6DA CRC64;
MSSVLIVKGH PLTAEESRSV KALSTFLTSY KESHPEDEIT ILDLYRDDIP EIDEELLSGW
EVLRTGADFS ELTEKQQHKI ARFNELTEQF LAADKIVIAN ALWNLNIPTR LKAWFDTVNV
AGKTFKYTEN GPQGLVQGKK ALHIQSNGGI YQGQDFASQY VKGILNFIGI DEIDQLFIEG
IDYTPDRAEE LMQEALDKAT QLGKDF
//
