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P19731 (DMPM_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenol hydroxylase P2 protein

EC=1.14.13.7
Alternative name(s):
Phenol 2-monooxygenase P2 component
Gene names
Name:dmpM
Synonyms:pheA3
Encoded onPlasmid pVI150
OrganismPseudomonas sp. (strain CF600)
Taxonomic identifier79676 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length90 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catabolizes phenol, and some of its methylated derivatives. P2 is required for growth on phenol, and for in vitro phenol hydroxylase activity.

Catalytic activity

Phenol + NADPH + O2 = catechol + NADP+ + H2O.

Cofactor

FAD.

Fe2+.

Pathway

Aromatic compound metabolism; phenol degradation.

Subunit structure

The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandFAD
Flavoprotein
Iron
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphenol 2-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9090Phenol hydroxylase P2 protein
PRO_0000079943

Secondary structure

................ 90
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19731 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 32B3A5FB72664AED

FASTA9010,491
        10         20         30         40         50         60 
MSSLVYIAFQ DNDNARYVVE AIIQDNPHAV VQHHPAMIRI EAEKRLEIRR ETVEENLGRA 

        70         80         90 
WDVQEMLVDV ITIGGNVDED DDRFVLEWKN 

« Hide

References

[1]"Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600."
Nordlund I., Powlowski J., Shingler V.
J. Bacteriol. 172:6826-6833(1990) [PubMed: 2254258] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M.
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BH.
[3]"Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy."
Qian H., Edlund U., Powlowski J., Shingler V., Sethson I.
Biochemistry 36:495-504(1997) [PubMed: 9012665] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60276 Genomic DNA. Translation: AAA25941.1.
D28864 Genomic DNA. Translation: BAA06016.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQINMR-A1-90[»]
ProteinModelPortalP19731.
SMRP19731. Positions 1-90.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12796.

Family and domain databases

InterProIPR003454. mOase_MmoB_DmpM.
[Graphical view]
Gene3DG3DSA:3.90.56.10. mOase_MmoB_DmpM. 1 hit.
PfamPF02406. MmoB_DmpM. 1 hit.
[Graphical view]
ProDomPD004249. mOase_MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56029. MmoB_DmpM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDMPM_PSEUF
AccessionPrimary (citable) accession number: P19731
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 28, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references