ID   HBQR_BURSP              Reviewed;         183 AA.
AC   D3KVM6;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=2-hydroxy-1,4-benzoquinone reductase {ECO:0000305};
DE            EC=1.6.5.7 {ECO:0000269|PubMed:20480210};
DE   AltName: Full=Benzoquinone reductase {ECO:0000303|PubMed:20480210};
DE   AltName: Full=Hydroxybenzoquinone reductase {ECO:0000305};
OS   Burkholderia sp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=36773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=AK-5;
RX   PubMed=20480210; DOI=10.1007/s10532-010-9369-5;
RA   Takenaka S., Koshiya J., Okugawa S., Takata A., Murakami S., Aoki K.;
RT   "Fe-superoxide dismutase and 2-hydroxy-1,4-benzoquinone reductase preclude
RT   the auto-oxidation step in 4-aminophenol metabolism by Burkholderia sp.
RT   strain AK-5.";
RL   Biodegradation 22:1-11(2011).
CC   -!- FUNCTION: Involved in the metabolism of 4-aminophenol. Catalyzes the
CC       reduction of the auto-oxidation product 2-hydroxy-1,4-benzoquinone back
CC       to hydroxyquinol. Has a broad substrate specificity toward
CC       benzoquinones, converting them to the corresponding 1,4-benzenediols.
CC       {ECO:0000269|PubMed:20480210}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-1,4-benzoquinone + 2 H(+) + NADH = benzene-1,2,4-
CC         triol + NAD(+); Xref=Rhea:RHEA:12428, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16971, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58474; EC=1.6.5.7;
CC         Evidence={ECO:0000269|PubMed:20480210};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P0AGE6};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.12 mM for 2-hydroxy-1,4-benzoquinone
CC         {ECO:0000269|PubMed:20480210};
CC         KM=0.031 mM for 2-methoxy-1,4-benzoquinone
CC         {ECO:0000269|PubMed:20480210};
CC         KM=0.048 mM for 2-methyl-1,4-benzoquinone
CC         {ECO:0000269|PubMed:20480210};
CC         KM=0.035 mM for 1,4-benzoquinone {ECO:0000269|PubMed:20480210};
CC         Vmax=0.10 umol/min/mg enzyme with 2-hydroxy-1,4-benzoquinone as
CC         substrate {ECO:0000269|PubMed:20480210};
CC         Vmax=0.56 umol/min/mg enzyme with 2-methoxy-1,4-benzoquinone as
CC         substrate {ECO:0000269|PubMed:20480210};
CC         Vmax=0.79 umol/min/mg enzyme with 2-methyl-1,4-benzoquinone as
CC         substrate {ECO:0000269|PubMed:20480210};
CC         Vmax=0.83 umol/min/mg enzyme with 1,4-benzoquinone as substrate
CC         {ECO:0000269|PubMed:20480210};
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:20480210};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20480210}.
CC   -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR   EMBL; AB518003; BAI77485.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3KVM6; -.
DR   SMR; D3KVM6; -.
DR   BioCyc; MetaCyc:MON-17535; -.
DR   GO; GO:0050625; F:2-hydroxy-1,4-benzoquinone reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN           1..183
FT                   /note="2-hydroxy-1,4-benzoquinone reductase"
FT                   /id="PRO_0000441890"
FT   BINDING         11..18
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT   BINDING         77..80
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT   BINDING         113
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGE6"
SQ   SEQUENCE   183 AA;  20211 MW;  829ED881A50C3F12 CRC64;
     MALKIAVVVG SLRRDSFNKQ LAHALASLAP SDFSFDFVDI GGLPLYSQDY DSDFPEVARA
     FKQQIADADG LLIVTPEYNR SMPGVLKNAL DWASRPWGQS VWGGKPGAII GTSVGAIGTA
     IAQSHLRGVC AYLDIVLMNQ PEMYIKHDES RIDANGNIVS EDTRKYLQTF MDKYAAWVRD
     RRV