ID   3HBH_KLEOX              Reviewed;         397 AA.
AC   Q5EXK1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=3-hydroxybenzoate 6-hydroxylase;
DE            EC=1.14.13.24;
GN   Name=mhbM;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-169.
RC   STRAIN=M5a1;
RX   PubMed=15782938; DOI=10.1016/j.micres.2004.09.003;
RA   Liu D.Q., Liu H., Gao X.L., Leak D.J., Zhou N.Y.;
RT   "Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-
RT   hydroxylase from Klebsiella pneumoniae M5a1.";
RL   Microbiol. Res. 160:53-59(2005).
RN   [2]
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, INDUCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RC   STRAIN=M5a1;
RX   PubMed=7729672; DOI=10.1111/j.1574-6968.1995.tb07431.x;
RA   Suarez M., Ferrer E., Garrido-Pertierra A., Martin M.;
RT   "Purification and characterization of the 3-hydroxybenzoate-6-hydroxylase
RT   from Klebsiella pneumoniae.";
RL   FEMS Microbiol. Lett. 126:283-290(1995).
CC   -!- FUNCTION: Catalyzes the NAD- or NADP-dependent conversion of 3-
CC       hydroxybenzoate to gentisate. NAD and NADP function equally well.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxybenzoate + H(+) + NADH + O2 = 2,5-dihydroxybenzoate +
CC         H2O + NAD(+); Xref=Rhea:RHEA:22692, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16193,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58044;
CC         EC=1.14.13.24; Evidence={ECO:0000269|PubMed:7729672};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:7729672};
CC   -!- ACTIVITY REGULATION: Inhibited by copper, mercury and iron ions.
CC       {ECO:0000269|PubMed:7729672}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=70 uM for NADH {ECO:0000269|PubMed:7729672};
CC         KM=70 uM for NADPH {ECO:0000269|PubMed:7729672};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:7729672};
CC       Temperature dependence:
CC         Optimum temperature is 25-30 degrees Celsius.
CC         {ECO:0000269|PubMed:7729672};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7729672}.
CC   -!- INDUCTION: By 3-hydroxybenzoate and 2,5-dihydroxybenzoate.
CC       {ECO:0000269|PubMed:7729672}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AY648560; AAW63416.1; -; Genomic_DNA.
DR   RefSeq; WP_024359203.1; NZ_QDDU01000005.1.
DR   AlphaFoldDB; Q5EXK1; -.
DR   SMR; Q5EXK1; -.
DR   STRING; 571.MC52_27515; -.
DR   GeneID; 64336519; -.
DR   PATRIC; fig|571.110.peg.4032; -.
DR   eggNOG; COG0654; Bacteria.
DR   OrthoDB; 504558at2; -.
DR   BRENDA; 1.14.13.24; 2811.
DR   GO; GO:0018669; F:3-hydroxybenzoate 6-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NAD;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..397
FT                   /note="3-hydroxybenzoate 6-hydroxylase"
FT                   /id="PRO_0000382698"
FT   MUTAGEN         169
FT                   /note="R->E: No activity."
FT                   /evidence="ECO:0000269|PubMed:15782938"
SQ   SEQUENCE   397 AA;  43887 MW;  86411484F680D9FE CRC64;
     MAKVMRAIIV GGGIGGAATA LSLARQGIKV MLLEKAHEIG EIGAGIQLGP NAFSALDSLG
     VGEVARQRAV FTDHITMMDA VNGEEVVHIE TGQAFRDHFG GPYAVIHRVD IHATVWEAAL
     THPAVEYRTS TQVVDIRQTA DDVTVFDDKG NSWTADILIG CDGGKSVVRQ SLLGDSPRVT
     GHVVYRAVVD AADMPDDLRI NAPVLWAGPH CHLVHYPLRG GKQYNLVVTF HSRQQEEWGV
     RDGSKEEVLS YFKGIHPRPR QMLDKPTSWR RWSTADREPV EKWGNDRITL VGDAAHPVAQ
     YMAQGACMAL EDAVTLGKAL AQCDGDAARA FALYESVRIP RTARIVWSTR EMGRVYHAAG
     VERQVRNLLW KGKTQSEFYR GIEWLYGWKE DNCLEAR