ID   TFDB_CUPPJ              Reviewed;         598 AA.
AC   P27138; Q46M70;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=2,4-dichlorophenol 6-monooxygenase;
DE            EC=1.14.13.20;
DE   AltName: Full=2,4-dichlorophenol hydroxylase;
DE            Short=2,4-DCP hydroxylase;
GN   Name=tfdB; Synonyms=tfdBI; OrderedLocusNames=Reut_D6462;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=2185214; DOI=10.1128/jb.172.5.2351-2359.1990;
RA   Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.;
RT   "Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase
RT   and dichlorocatechol oxidative operons of plasmid pJP4.";
RL   J. Bacteriol. 172:2351-2359(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Transforms 2,4-dichlorophenol (2,4-DCP) into 3,5-
CC       dichlorocatechol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-dichlorophenol + H(+) + NADPH + O2 = 3,5-dichlorocatechol
CC         + H2O + NADP(+); Xref=Rhea:RHEA:20920, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15788,
CC         ChEBI:CHEBI:16738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.14.13.20;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Xenobiotic degradation; (2,4-dichlorophenoxy)acetate
CC       degradation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; M35097; AAA98266.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31035.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65760.1; -; Genomic_DNA.
DR   PIR; E35255; E35255.
DR   RefSeq; WP_011178382.1; NZ_AY365053.1.
DR   AlphaFoldDB; P27138; -.
DR   SMR; P27138; -.
DR   EnsemblBacteria; AAZ65760; AAZ65760; Reut_D6462.
DR   GeneID; 55536838; -.
DR   KEGG; reu:Reut_D6462; -.
DR   HOGENOM; CLU_009665_14_0_4; -.
DR   OMA; DSFDIGW; -.
DR   OrthoDB; 867226at2; -.
DR   BioCyc; MetaCyc:MON-14385; -.
DR   UniPathway; UPA00685; -.
DR   GO; GO:0018666; F:2,4-dichlorophenol 6-monooxygenase activity; NAS:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046300; P:2,4-dichlorophenoxyacetic acid catabolic process; NAS:UniProtKB.
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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NADP;
KW   Oxidoreductase; Plasmid.
FT   CHAIN           1..598
FT                   /note="2,4-dichlorophenol 6-monooxygenase"
FT                   /id="PRO_0000214049"
FT   BINDING         8..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         301..311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   598 AA;  65380 MW;  A1E552E5A34B832F CRC64;
     MALTIETDVL VVGTGPAGAS AGALLARYGV RTMLINKYNW TAPTPRAHIT NQRTMEILRD
     LGLEAEARLY AAPNDLMGEN TICASLAGEE FGRIRTWGTD VRRRADYDEC SPTSMCDLPQ
     NYLEPILVKS AALDGCKVRF DTEYLGHEQD ADGVSSRLRD RLNGEEFTVR SKYLIGADGA
     NSRVVSDLDL PLEGTMGKSG SINLLFEADL DRYVAHRPSV LYWVIQPGSD IGGLGIGVVR
     MVRPWNKWLA IWGYDVEQGP PEISESFARR IVHNLIGDDS VPLKIEGIST WTVNDMYATR
     LQQGRVFCAG DAVHRHPPTN GLGSNTSIQD SFNLAWKIAM VLNGTADESL LDTYTIERAP
     IAKQVVCRAN KSLEDFPPIA MALGLPQAKS ADEMKSNMAR RKEPGPEAQA QRTRLREAIA
     GTNYVYNAHG VEMNQRYDSP AIVADNSPDE VFRDVELYHQ ASTRPGAPMP HVWVYASGDG
     HRISTKDLCG KGNFTLFTGI GGAAWQDAAA AVSRQLGVAV TVRIIGPGQA YEDHYGDFAR
     ISEIIDTGAI LVRPDFHVAY RATSLPADAA GDLVSAMRRI LGRQSERSSA LRVTSRAI