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Protein

Phenol hydroxylase P2 protein

Gene

dmpM

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi: phenol degradation

This protein is involved in the pathway phenol degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenol degradation and in Aromatic compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, Iron, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12796.
UniPathwayiUPA00728.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenol hydroxylase P2 protein (EC:1.14.13.7)
Alternative name(s):
Phenol 2-monooxygenase P2 component
Gene namesi
Name:dmpM
Synonyms:pheA3
Encoded oniPlasmid pVI1500 Publication
OrganismiPseudomonas sp. (strain CF600)
Taxonomic identifieri79676 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9090Phenol hydroxylase P2 proteinPRO_0000079943Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
90
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi14 – 2512Combined sources
Beta strandi26 – 283Combined sources
Beta strandi43 – 486Combined sources
Helixi50 – 589Combined sources
Helixi60 – 623Combined sources
Helixi63 – 686Combined sources
Beta strandi69 – 724Combined sources
Beta strandi84 – 885Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQINMR-A1-90[»]
ProteinModelPortaliP19731.
SMRiP19731. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19731.

Family & Domainsi

Family and domain databases

Gene3Di3.90.56.10. 1 hit.
InterProiIPR003454. mOase_MmoB_DmpM.
[Graphical view]
PfamiPF02406. MmoB_DmpM. 1 hit.
[Graphical view]
ProDomiPD004249. mOase_MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56029. SSF56029. 1 hit.

Sequencei

Sequence statusi: Complete.

P19731-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLVYIAFQ DNDNARYVVE AIIQDNPHAV VQHHPAMIRI EAEKRLEIRR
60 70 80 90
ETVEENLGRA WDVQEMLVDV ITIGGNVDED DDRFVLEWKN
Length:90
Mass (Da):10,491
Last modified:February 1, 1991 - v1
Checksum:i32B3A5FB72664AED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60276 Genomic DNA. Translation: AAA25941.1.
D28864 Genomic DNA. Translation: BAA06016.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60276 Genomic DNA. Translation: AAA25941.1.
D28864 Genomic DNA. Translation: BAA06016.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQINMR-A1-90[»]
ProteinModelPortaliP19731.
SMRiP19731. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00728.
BioCyciMetaCyc:MONOMER-12796.

Miscellaneous databases

EvolutionaryTraceiP19731.

Family and domain databases

Gene3Di3.90.56.10. 1 hit.
InterProiIPR003454. mOase_MmoB_DmpM.
[Graphical view]
PfamiPF02406. MmoB_DmpM. 1 hit.
[Graphical view]
ProDomiPD004249. mOase_MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56029. SSF56029. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiDMPM_PSEUF
AccessioniPrimary (citable) accession number: P19731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: December 9, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.