ID   DMPO_PSEUF              Reviewed;         119 AA.
AC   P19733;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Phenol 2-monooxygenase, oxygenase component DmpO {ECO:0000305};
DE            EC=1.14.13.244 {ECO:0000269|PubMed:2254259};
DE   AltName: Full=Phenol 2-monooxygenase P4 component;
DE   AltName: Full=Phenol hydroxylase P4 protein;
GN   Name=dmpO {ECO:0000303|PubMed:2254258}; Synonyms=pheA5;
OS   Pseudomonas sp. (strain CF600).
OG   Plasmid pVI150.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=79676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=CF600;
RX   PubMed=2254258; DOI=10.1128/jb.172.12.6826-6833.1990;
RA   Nordlund I., Powlowski J., Shingler V.;
RT   "Complete nucleotide sequence and polypeptide analysis of multicomponent
RT   phenol hydroxylase from Pseudomonas sp. strain CF600.";
RL   J. Bacteriol. 172:6826-6833(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BH;
RA   Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=CF600;
RX   PubMed=2254259; DOI=10.1128/jb.172.12.6834-6840.1990;
RA   Powlowski J., Shingler V.;
RT   "In vitro analysis of polypeptide requirements of multicomponent phenol
RT   hydroxylase from Pseudomonas sp. strain CF600.";
RL   J. Bacteriol. 172:6834-6840(1990).
RN   [4]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC   STRAIN=CF600;
RX   PubMed=12186554; DOI=10.1021/bi025901u;
RA   Cadieux E., Vrajmasu V., Achim C., Powlowski J., Muenck E.;
RT   "Biochemical, Moessbauer, and EPR studies of the diiron cluster of phenol
RT   hydroxylase from Pseudomonas sp. strain CF 600.";
RL   Biochemistry 41:10680-10691(2002).
CC   -!- FUNCTION: Part of a multicomponent enzyme which catalyzes the
CC       degradation of phenol and some of its methylated derivatives
CC       (PubMed:2254259). DmpL, DmpN and DmpO form the oxygenase component of
CC       the complex (PubMed:12186554). Required for growth on phenol and for in
CC       vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
CC       {ECO:0000269|PubMed:12186554, ECO:0000269|PubMed:2254258,
CC       ECO:0000269|PubMed:2254259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + phenol = catechol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:57952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:18135,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.244;
CC         Evidence={ECO:0000269|PubMed:2254259};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57953;
CC         Evidence={ECO:0000269|PubMed:2254259};
CC   -!- ACTIVITY REGULATION: Requires DmpM for efficient turnover. The activity
CC       of DmpLNO oxygenase is inhibited by dithiothreitol (DTT) by a mechanism
CC       apparently involving H(2)O(2) generation.
CC       {ECO:0000269|PubMed:12186554}.
CC   -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC       {ECO:0000269|PubMed:2254258}.
CC   -!- SUBUNIT: The multicomponent enzyme phenol hydroxylase is formed by DmpL
CC       (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4
CC       component) and DmpP (P5 component) (PubMed:2254259). The oxygenase
CC       component is a dimer composed of three subunits, DmpL, DmpN and DmpO
CC       (DmpLNO) (PubMed:12186554). {ECO:0000269|PubMed:12186554,
CC       ECO:0000269|PubMed:2254259}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on phenol.
CC       {ECO:0000269|PubMed:2254258}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M60276; AAA25943.1; -; Genomic_DNA.
DR   EMBL; D28864; BAA06018.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19733; -.
DR   SMR; P19733; -.
DR   BioCyc; MetaCyc:MON-12798; -.
DR   BRENDA; 1.14.13.244; 16277.
DR   UniPathway; UPA00728; -.
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; 3.10.20.560; -; 1.
DR   InterPro; IPR006756; Phenol_hydroxylase.
DR   InterPro; IPR043010; Phenol_hydroxylase_sf.
DR   Pfam; PF04663; Phenol_monoox; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Monooxygenase; NAD; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..119
FT                   /note="Phenol 2-monooxygenase, oxygenase component DmpO"
FT                   /id="PRO_0000079946"
SQ   SEQUENCE   119 AA;  13207 MW;  AE0151A918638C49 CRC64;
     MTVNSIGEYT ATPRDVQANF NGMQLLYLYW EEHLMYCSAL AFLVAPGMPF AEFLEQVLKP
     AIHAHPDSAK IDFSQALWQL NDQPFTPDYA ASLEANGIDH KSMLRLNTPG LNGIQGSCS