ID   TBUD_RALPI              Reviewed;         671 AA.
AC   Q01551;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phenol 2-monooxygenase;
DE            EC=1.14.13.7;
DE   AltName: Full=Phenol hydroxylase;
GN   Name=tbuD;
OS   Ralstonia pickettii (Burkholderia pickettii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-22.
RC   STRAIN=PKO1;
RX   PubMed=1400204; DOI=10.1128/jb.174.20.6518-6526.1992;
RA   Kukor J.J., Olsen R.H.;
RT   "Complete nucleotide sequence of tbuD, the gene encoding phenol/cresol
RT   hydroxylase from Pseudomonas pickettii PKO1, and functional analysis of the
RT   encoded enzyme.";
RL   J. Bacteriol. 174:6518-6526(1992).
CC   -!- FUNCTION: Hydroxylates phenol to catechol. Also acts on cresols.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+);
CC         Xref=Rhea:RHEA:17061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:18135,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.7;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; M98806; AAA25992.1; -; Genomic_DNA.
DR   PIR; A45730; A45730.
DR   AlphaFoldDB; Q01551; -.
DR   UniPathway; UPA00728; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Cytoplasm; Direct protein sequencing;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1400204"
FT   CHAIN           2..671
FT                   /note="Phenol 2-monooxygenase"
FT                   /id="PRO_0000214047"
FT   BINDING         10..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         295..305
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   671 AA;  72999 MW;  A7ADFB9286640195 CRC64;
     MTKYNEAYCD VLIVGAGPAG VMAAAHLLSY GTTARPHRVR IFDATKEVNG SDESTESLST
     DVIADALNSG ASGPEKDAAS TTEDLPMLVT TLQVSDVLHD TGDDTKIAYR ETATEQQVLL
     LADTTANTSS TMNPRSMCEA GCRFHQIYQG HCFPEYELDS ERLRSVDGRA QVLEDEHETG
     QLRLERLGRP EELLELDEEN SMSVVTNLKA APYKFLMKDV DENFPGELST SGGKTTSISA
     DESAIDAALH AVWDADDLGA AWHLDEASGL RAVDWNAAQW FKSGQPWTPD AAKSLQEGRV
     FLAGDARHRH PPLTGIGKNT SIADCYNLTW KLLGVLLGVA RADPARTYVA ERVYIRMRAA
     TDIAVDAEME SLAAKWITVQ LTLSRSWISS AKEAERWDAV LRDSAMSASK PMWTTSDMRA
     SFDAGLMGHG HAHDHVTPTI KEFASSSISR SISELASTSW WESRGWGNGG PFESLMEDAR
     WTGAVESNCR YAAYDRDAPV LHEHVAWVTR FTSRARTAVL EAAVGQAHVV DCWDVGLVEP
     ALDDLDSAGA GLHVAHHADQ WPAQLDEAVW PRESLSDWRI VTDTSATGEG YQTSPREAPG
     DYADLNADNA KAHFNGQFAG HKAYGDAAAA DGGGCHGRIL VGPAVRGRHL HREIPLGEEC
     QRAAQPLFKE V