ID   3HBH2_PSEAC             Reviewed;         320 AA.
AC   Q0QFQ1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=3-hydroxybenzoate 6-hydroxylase 2;
DE            EC=1.14.13.24;
DE   AltName: Full=Inducible 3-hydroxybenzoate 6-hydroxylase;
GN   Name=hbzD;
OS   Pseudomonas alcaligenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=43263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 9867 / P25X;
RX   PubMed=17720458; DOI=10.1016/j.resmic.2007.06.003;
RA   Yeo C.C., Tan C.L., Gao X., Zhao B., Poh C.L.;
RT   "Characterization of hbzE-encoded gentisate 1,2-dioxygenase from
RT   Pseudomonas alcaligenes NCIMB 9867.";
RL   Res. Microbiol. 158:608-616(2007).
RN   [2]
RP   INDUCTION.
RC   STRAIN=NCIMB 9867 / P25X;
RX   PubMed=16267294; DOI=10.1128/jb.187.22.7696-7702.2005;
RA   Gao X., Tan C.L., Yeo C.C., Poh C.L.;
RT   "Molecular and biochemical characterization of the xlnD-encoded 3-
RT   hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol
RT   via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867.";
RL   J. Bacteriol. 187:7696-7702(2005).
CC   -!- FUNCTION: Catalyzes the conversion of 3-hydroxybenzoate to gentisate.
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- INDUCTION: By 3-hydroxybenzoate. {ECO:0000269|PubMed:16267294}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ394580; ABD64514.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0QFQ1; -.
DR   SMR; Q0QFQ1; -.
DR   PRIDE; Q0QFQ1; -.
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   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..320
FT                   /note="3-hydroxybenzoate 6-hydroxylase 2"
FT                   /id="PRO_0000382701"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   320 AA;  36421 MW;  61FC1101E046B0C3 CRC64;
     MRSTNTRSAR SRPTKRSVNA SATPTQSFHR VDAHLSLLEG AEETGWVEFK TNTRVERIEQ
     DADSVTVYDQ NGNAYRGVAL IGADGVRSVV RQTYVNDQPR VTGHVVYRAV VDKDEFPQDL
     RWNASSLWVG PKCHLVHYPL RGGEQYNIVV TFQSRQQEEW GVTEGSKEEV ESYFQDICPK
     ARQLIGLPKS WKRWATADRE PIPQWTFGRT TLLGDAAHPT TQYMAQGACM ALEDAVTLGE
     ALRVHGNDWG KALDLYQRSR ITRTARIVLS GREMGRLYHA QGVERLVRNS LWKGRTTEQF
     YDAIQWLYGW NVDNCLSESI