AZOR_ENTFA
ID AZOR_ENTFA Reviewed; 208 AA.
AC Q831B2; Q6TFZ9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:15003265};
GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216};
GN Synonyms=azoA {ECO:0000303|PubMed:15003265}; OrderedLocusNames=EF_2601;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 19433 / DSM 20478 / JCM 8726 / NBRC 100481 / NCIMB 775;
RX PubMed=15003265; DOI=10.1016/j.pep.2003.12.016;
RA Chen H., Wang R.-F., Cerniglia C.E.;
RT "Molecular cloning, overexpression, purification, and characterization of
RT an aerobic FMN-dependent azoreductase from Enterococcus faecalis.";
RL Protein Expr. Purif. 34:302-310(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [3] {ECO:0007744|PDB:2HPV}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
RA Liu Z.J., Chen H., Chen L., Shah N., Rose J.P., Wang B.C.;
RT "Crystal structure of FMN-dependent azoreductase from Enterococcus faecalis
RT at 2.00 A resolution.";
RL Submitted (JUL-2006) to the PDB data bank.
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones. {ECO:0000255|HAMAP-
CC Rule:MF_01216}.
CC -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC cleavage of the azo bond in aromatic azo compounds to the corresponding
CC amines. Requires NADH, but not NADPH, as an electron donor for its
CC activity. The enzyme can also reduce a wide range of sulfonated azo
CC dyes. The substrate preference order is methyl Red > Orange II >
CC Ponceau BS > Ponceau S > Orange G > Amaranth.
CC {ECO:0000269|PubMed:15003265}.
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01216, ECO:0000269|PubMed:15003265};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC Evidence={ECO:0000269|PubMed:15003265};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:15003265};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for methyl red {ECO:0000269|PubMed:15003265};
CC KM=140 uM for NADH {ECO:0000269|PubMed:15003265};
CC Vmax=89.2 umol/min/mg enzyme toward methyl red
CC {ECO:0000269|PubMed:15003265};
CC Vmax=86.2 umol/min/mg enzyme toward NADH
CC {ECO:0000269|PubMed:15003265};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:15003265}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305}.
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DR EMBL; AY422207; AAR38851.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO82310.1; -; Genomic_DNA.
DR RefSeq; NP_816240.1; NC_004668.1.
DR RefSeq; WP_002367152.1; NZ_KE136528.1.
DR PDB; 2HPV; X-ray; 2.00 A; A/B/C/D=1-208.
DR PDBsum; 2HPV; -.
DR AlphaFoldDB; Q831B2; -.
DR SMR; Q831B2; -.
DR STRING; 226185.EF_2601; -.
DR EnsemblBacteria; AAO82310; AAO82310; EF_2601.
DR GeneID; 60894603; -.
DR KEGG; efa:EF2601; -.
DR PATRIC; fig|226185.45.peg.955; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_3_0_9; -.
DR OMA; AGITFKY; -.
DR BRENDA; 1.7.1.17; 2095.
DR BRENDA; 1.7.1.6; 2095.
DR SABIO-RK; Q831B2; -.
DR EvolutionaryTrace; Q831B2; -.
DR Proteomes; UP000001415; 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 Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..208
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_0000233263"
FT BINDING 10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV"
FT BINDING 104..107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV"
FT BINDING 148..153
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV"
FT BINDING 184
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2HPV"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 76..94
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:2HPV"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:2HPV"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2HPV"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2HPV"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:2HPV"
SQ SEQUENCE 208 AA; 23221 MW; BD7628B22213C651 CRC64;
MSKLLVVKAH PLTKEESRSV RALETFLASY RETNPSDEIE ILDVYAPETN MPEIDEELLS
AWGALRAGAA FETLSENQQQ KVARFNELTD QFLSADKVVI ANPMWNLNVP TRLKAWVDTI
NVAGKTFQYT AEGPKPLTSG KKALHIQSNG GFYEGKDFAS QYIKAILNFI GVDQVDGLFI
EGIDHFPDRA EELLNTAMTK ATEYGKTF
