ID   3HBH_POLNA              Reviewed;         400 AA.
AC   Q3S4B7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=3-hydroxybenzoate 6-hydroxylase;
DE            EC=1.14.13.24;
GN   Name=nagX; OrderedLocusNames=Pnap_3144;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16461653; DOI=10.1128/aem.72.2.1086-1095.2006;
RA   Jeon C.O., Park M., Ro H.-S., Park W., Madsen E.L.;
RT   "The naphthalene catabolic (nag) genes of Polaromonas naphthalenivorans
RT   CJ2: evolutionary implications for two gene clusters and novel regulatory
RT   control.";
RL   Appl. Environ. Microbiol. 72:1086-1095(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
RN   [3]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND COFACTOR.
RX   PubMed=17586666; DOI=10.1128/aem.00782-07;
RA   Park M., Jeon Y., Jang H.H., Ro H.-S., Park W., Madsen E.L., Jeon C.O.;
RT   "Molecular and biochemical characterization of 3-hydroxybenzoate 6-
RT   hydroxylase from Polaromonas naphthalenivorans CJ2.";
RL   Appl. Environ. Microbiol. 73:5146-5152(2007).
CC   -!- FUNCTION: Catalyzes the NAD- or NADP-dependent conversion of 3-
CC       hydroxybenzoate to gentisate. The affinity of the enzyme toward NAD is
CC       twice as high as for NADP.
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:17586666};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:17586666};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=64.9 uM for 3-hydroxybenzoate {ECO:0000269|PubMed:17586666};
CC         KM=493 uM for NADH {ECO:0000269|PubMed:17586666};
CC         KM=860 uM for NADPH {ECO:0000269|PubMed:17586666};
CC       pH dependence:
CC         Optimum pH is 8.4. {ECO:0000269|PubMed:17586666};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:17586666};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17586666}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ167475; AAZ93401.1; -; Genomic_DNA.
DR   EMBL; CP000529; ABM38442.1; -; Genomic_DNA.
DR   RefSeq; WP_011802513.1; NC_008781.1.
DR   AlphaFoldDB; Q3S4B7; -.
DR   SMR; Q3S4B7; -.
DR   STRING; 365044.Pnap_3144; -.
DR   EnsemblBacteria; ABM38442; ABM38442; Pnap_3144.
DR   KEGG; pna:Pnap_3144; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_19_3_4; -.
DR   OMA; YKHMVGH; -.
DR   OrthoDB; 504558at2; -.
DR   SABIO-RK; Q3S4B7; -.
DR   Proteomes; UP000000644; Chromosome.
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; Reference proteome.
FT   CHAIN           1..400
FT                   /note="3-hydroxybenzoate 6-hydroxylase"
FT                   /id="PRO_0000382699"
SQ   SEQUENCE   400 AA;  44111 MW;  DAE1C5B6FAF04F7E CRC64;
     MSDNPADLPV LVAGGGIGGL AAALALVRRG FSVKVLEQAP EIGEIGAGIQ LGPNAFHAFD
     ALGIGEKARG RAVYTDEMVM HDAIDGSLVG RIPTGEAFRQ RFGNPYAVIH RVDVHLSLLE
     GAQETGKVEF LTSTRALRIE QDEGSVTVYD QHGNAHKGIA LIGADGVKSV VREQFVGDAA
     RVTGHVVYRA VVDKKDFPES LQWNAASIWV GPNCHLVHYP LRGGEQYNVV VTFHSRQPEQ
     WGVTEGSKEE VQSYFQGICP QARQLIDLPK TWKRWATADR EPIGQWSFGR VTLLGDAAHP
     TTQYMAQGAC MAMEDGVTLG EALRVNNNDF PKAFELYQRS RVARTARIVL SSREMGRIYH
     AQGVERLVRN DLWKGRTPER FYDAMEWLYG WNVGNCLAKD