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Protein

Phenol hydroxylase P1 protein

Gene

dmpL

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein predictedi

Functioni

Catabolizes phenol, and some of its methylated derivatives. P1 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

GO - Molecular functioni

  1. phenol 2-monooxygenase activity Source: UniProtKB

GO - Biological processi

  1. aerobic phenol-containing compound catabolic process Source: UniProtKB
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-12795.
UniPathwayiUPA00728.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenol hydroxylase P1 protein (EC:1.14.13.7)
Alternative name(s):
Phenol 2-monooxygenase P1 component
Gene namesi
Name:dmpL
Synonyms:pheA2
Encoded oniPlasmid pVI1500 Publication
OrganismiPseudomonas sp. (strain CF600)
Taxonomic identifieri79676 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Subcellular locationi

GO - Cellular componenti

  1. extrachromosomal circular DNA Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Phenol hydroxylase P1 proteinPRO_0000079942Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP19730.
SMRiP19730. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFiPIRSF000040. MMOH_comp. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.

Sequencei

Sequence statusi: Complete.

P19730-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVEIKTNTV DPIRQTYGNL QRRFGDKPAS RYQEASYDIE AVTNFHYRPL
60 70 80 90 100
WDPQHELHDP TRTAIRMTDW HKVTDPRQFY YGAYVQTRAR MQEATEHAYG
110 120 130 140 150
FCEKRELLSR LPAELQAKLL RCLVPLRHAE LGANMNNSSI AGDSIAATVT
160 170 180 190 200
QMHIYQAMDR LGMGQYLSRI GLLLDGGTGE ALDQAKAYWL DDPIWQGLRR
210 220 230 240 250
YVEDSFVIRD WFELGLAQNL VLDGLLQPLM YQRFDQWLTE NGGSDVAMLT
260 270 280 290 300
EFMRDWYGES TRWVDAMFKT VLAENDANRE QVQAWLEVWE PRAYEALLPL
310 320 330
AEEATGIAAL DEVRSAFATR LQKIGLKSRE E
Length:331
Mass (Da):38,208
Last modified:February 1, 1991 - v1
Checksum:i8042F5723BE3A5E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60276 Genomic DNA. Translation: AAA25940.1.
D28864 Genomic DNA. Translation: BAA06015.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60276 Genomic DNA. Translation: AAA25940.1.
D28864 Genomic DNA. Translation: BAA06015.1.

3D structure databases

ProteinModelPortaliP19730.
SMRiP19730. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00728.
BioCyciMetaCyc:MONOMER-12795.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFiPIRSF000040. MMOH_comp. 1 hit.
SUPFAMiSSF47240. SSF47240. 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.

Entry informationi

Entry nameiDMPL_PSEUF
AccessioniPrimary (citable) accession number: P19730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 66 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

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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 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.