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P15245 (PH2M_TRICU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 2-monooxygenase

EC=1.14.13.7
Alternative name(s):
Phenol hydroxylase
OrganismTrichosporon cutaneum (Yeast) (Oidium cutaneum)
Taxonomic identifier5554 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesmitosporic TremellalesTrichosporon

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols.

Catalytic activity

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

Cofactor

FAD.

Enzyme regulation

Inhibited by excess phenol.

Pathway

Aromatic compound metabolism; phenol degradation.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the PheA/TfdB FAD monooxygenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processphenol-containing compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphenol 2-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 665664Phenol 2-monooxygenase
PRO_0000214045

Regions

Nucleotide binding10 – 4435FAD Potential
Nucleotide binding348 – 35811FAD Potential

Secondary structure

....................................................................................................... 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15245 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1401BE35D38BFB71

FASTA66575,162
        10         20         30         40         50         60 
MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY NGQADGLQCR 

        70         80         90        100        110        120 
TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR IPDTLPGISR YHQVVLHQGR 

       130        140        150        160        170        180 
IERHILDSIA EISDTRIKVE RPLIPEKMEI DSSKAEDPEA YPVTMTLRYM SDHESTPLQF 

       190        200        210        220        230        240 
GHKTENSLFH SNLQTQEEED ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM 

       250        260        270        280        290        300 
IGEQTDYIWG VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG 

       310        320        330        340        350        360 
GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD ERVFIAGDAC 

       370        380        390        400        410        420 
HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT YEEERHAFAQ ALIDFDHQFS 

       430        440        450        460        470        480 
RLFSGRPAKD VADEMGVSMD VFKEAFVKGN EFASGTAINY DENLVTDKKS SKQELAKNCV 

       490        500        510        520        530        540 
VGTRFKSQPV VRHSEGLWMH FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN 

       550        560        570        580        590        600 
SVISLYTPKV SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH 

       610        620        630        640        650        660 
PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE KSGAQTEADW 


TKSTA 

« Hide

References

[1]"Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli."
Kalin M., Neujahr H.Y., Weissmahr R.N., Sejlitz T., Johl R., Fiechter A., Reiser J.
J. Bacteriol. 174:7112-7120(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 46490.
[2]"Amino acid sequences around the pyridoxal-5'-phosphate-binding sites of phenol hydroxylase."
Sejlitz T., Wernstedt C., Engstroem A., Neujahr H.N.
Eur. J. Biochem. 187:225-228(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-64; 299-311 AND 352-377.
Strain: ATCC 46490.
[3]"The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis."
Enroth C., Neujahr H.Y., Schneider G., Lindqvist Y.
Structure 6:605-617(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Strain: ATCC 46490.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04488 mRNA. Translation: AAA34202.1.
PIRS07772.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOHX-ray2.40A/B/C/D2-665[»]
1PN0X-ray1.70A/B/C/D1-665[»]
ProteinModelPortalP15245.
SMRP15245. Positions 2-665.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14669.
UniPathwayUPA00728.

Family and domain databases

InterProIPR002938. mOase_FAD-bd.
IPR012941. Phe_hydrox_C_dim.
IPR003042. Rng_hydrolase-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF01494. FAD_binding_3. 1 hit.
PF07976. Phe_hydrox_dim. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
SUPFAMSSF52833. SSF52833. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP15245.

Entry information

Entry namePH2M_TRICU
AccessionPrimary (citable) accession number: P15245
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways