DMPM_PSEUF
ID DMPM_PSEUF Reviewed; 90 AA.
AC P19731;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phenol 2-monooxygenase, stimulatory component DmpM {ECO:0000305};
DE EC=1.14.13.244 {ECO:0000269|PubMed:2254259};
DE AltName: Full=Phenol 2-monooxygenase P2 component;
DE AltName: Full=Phenol hydroxylase P2 protein;
GN Name=dmpM {ECO:0000303|PubMed:2254258}; Synonyms=pheA3;
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, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=CF600;
RX PubMed=10451366; DOI=10.1021/bi990835q;
RA Cadieux E., Powlowski J.;
RT "Characterization of active and inactive forms of the phenol hydroxylase
RT stimulatory protein DmpM.";
RL Biochemistry 38:10714-10722(1999).
RN [5]
RP FUNCTION.
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).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=9012665; DOI=10.1021/bi9619233;
RA Qian H., Edlund U., Powlowski J., Shingler V., Sethson I.;
RT "Solution structure of phenol hydroxylase protein component P2 determined
RT by NMR spectroscopy.";
RL Biochemistry 36:495-504(1997).
CC -!- FUNCTION: Part of a multicomponent enzyme which catalyzes the
CC degradation of phenol and some of its methylated derivatives
CC (PubMed:2254259). DmpM is a regulatory subunit that stimulates the
CC phenol hydroxylase activity of the complex (PubMed:10451366,
CC PubMed:12186554). The steady-state rate of phenol hydroxylase turnover
CC is dependent on the DmpM concentration, with a maximum observed rate at
CC about 1.5 DmpM per oxygenase monomer. Higher concentrations of DmpM
CC inhibit phenol hydroxylase activity (PubMed:12186554). May act by
CC altering the redox potential of the oxygenase (PubMed:12186554).
CC Required for growth on phenol and for in vitro phenol hydroxylase
CC activity (PubMed:2254258, PubMed:2254259).
CC {ECO:0000269|PubMed:10451366, ECO:0000269|PubMed:12186554,
CC ECO:0000269|PubMed:2254258, 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 -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC {ECO:0000269|PubMed:2254258}.
CC -!- SUBUNIT: Active as a monomer (PubMed:10451366). Formation of dimers
CC inactivates the protein (PubMed:10451366). The multicomponent enzyme
CC phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2
CC component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5
CC component) (PubMed:2254259). {ECO:0000269|PubMed:10451366,
CC ECO:0000269|PubMed:2254259}.
CC -!- MASS SPECTROMETRY: Mass=10361; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10451366};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on phenol.
CC {ECO:0000269|PubMed:2254258}.
CC -!- SIMILARITY: Belongs to the TmoD/XamoD family. {ECO:0000305}.
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DR EMBL; M60276; AAA25941.1; -; Genomic_DNA.
DR EMBL; D28864; BAA06016.1; -; Genomic_DNA.
DR PDB; 1HQI; NMR; -; A=1-90.
DR PDBsum; 1HQI; -.
DR AlphaFoldDB; P19731; -.
DR SMR; P19731; -.
DR BioCyc; MetaCyc:MON-12796; -.
DR BRENDA; 1.14.13.244; 16277.
DR UniPathway; UPA00728; -.
DR EvolutionaryTrace; P19731; -.
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; 3.90.56.10; -; 1.
DR InterPro; IPR003454; MOase_MmoB_DmpM.
DR InterPro; IPR036889; mOase_MmoB_DmpM_sf.
DR Pfam; PF02406; MmoB_DmpM; 1.
DR SUPFAM; SSF56029; SSF56029; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Monooxygenase; NAD;
KW Oxidoreductase; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10451366"
FT CHAIN 2..90
FT /note="Phenol 2-monooxygenase, stimulatory component DmpM"
FT /id="PRO_0000079943"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1HQI"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1HQI"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1HQI"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1HQI"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:1HQI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1HQI"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1HQI"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1HQI"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1HQI"
SQ SEQUENCE 90 AA; 10491 MW; 32B3A5FB72664AED CRC64;
MSSLVYIAFQ DNDNARYVVE AIIQDNPHAV VQHHPAMIRI EAEKRLEIRR ETVEENLGRA
WDVQEMLVDV ITIGGNVDED DDRFVLEWKN
