UniProtKB - P15245 (PHHY_TRICU)
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>sp|P15245|PHHY_TRICU Phenol hydroxylase OS=Trichosporon cutaneum OX=5554 PE=1 SV=3 MTKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYNGQADGLQCR TLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRIPDTLPGISRYHQVVLHQGR IERHILDSIAEISDTRIKVERPLIPEKMEIDSSKAEDPEAYPVTMTLRYMSDHESTPLQF GHKTENSLFHSNLQTQEEEDANYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEM IGEQTDYIWGVLDAVPASNFPDIRSPCAIHSAESGSIMIIPRENNLVRFYVQLQARAEKG GRVDRTKFTPEVVIANAKKIFHPYTFDVQQLDWFTAYHIGQRVTEKFSKDERVFIAGDAC HTHSPKAGQGMNTSMMDTYNLGWKLGLVLTGRAKRDILKTYEEERHAFAQALIDFDHQFS RLFSGRPAKDVADEMGVSMDVFKEAFVKGNEFASGTAINYDENLVTDKKSSKQELAKNCV VGTRFKSQPVVRHSEGLWMHFGDRLVTDGRFRIIVFAGKATDATQMSRIKKFSAYLDSEN SVISLYTPKVSDRNSRIDVITIHSCHRDDIEMHDFPAPALHPKWQYDFIYADCDSWHHPH PKSYQAWGVDETKGAVVVVRPDGYTSLVTDLEGTAEIDRYFSGILVEPKEKSGAQTEADW TKSTAHelp videoAdd a publicationFeedback
Protein
Phenol hydroxylase
Gene
N/A
Organism
Trichosporon cutaneum (Yeast) (Oidium cutaneum)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).8 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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, FUNCTION, CATALYTIC ACTIVITY. - Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION. - Ref.5"Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ."
Moertberg M., Neujahr H.Y.
FEBS Lett. 242:75-78(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.6"Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase."
Taylor M.G., Massey V.
J. Biol. Chem. 266:8291-8301(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.7"A fermentor culture for production of recombinant phenol hydroxylase."
Waters S., Neujahr H.Y.
Protein Expr. Purif. 5:534-540(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics."
Peelen S., Rietjens I.M., Boersma M.G., Vervoort J.
Eur. J. Biochem. 227:284-291(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.9"Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met."
Xu D., Ballou D.P., Massey V.
Biochemistry 40:12369-12378(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-55; ARG-282 AND TYR-290. - Ref.10"Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain."
Gerginova M., Manasiev J., Shivarova N., Alexieva Z.
Z. Naturforsch. C 62:83-86(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- H+EC:1.14.13.7
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Manual assertion based on experiment ini
- Ref.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, FUNCTION, CATALYTIC ACTIVITY. - Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION. - Ref.5"Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ."
Moertberg M., Neujahr H.Y.
FEBS Lett. 242:75-78(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.6"Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase."
Taylor M.G., Massey V.
J. Biol. Chem. 266:8291-8301(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.7"A fermentor culture for production of recombinant phenol hydroxylase."
Waters S., Neujahr H.Y.
Protein Expr. Purif. 5:534-540(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics."
Peelen S., Rietjens I.M., Boersma M.G., Vervoort J.
Eur. J. Biochem. 227:284-291(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.9"Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met."
Xu D., Ballou D.P., Massey V.
Biochemistry 40:12369-12378(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-55; ARG-282 AND TYR-290. - Ref.10"Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain."
Gerginova M., Manasiev J., Shivarova N., Alexieva Z.
Z. Naturforsch. C 62:83-86(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.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, FUNCTION, CATALYTIC ACTIVITY. - Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION. - Ref.5"Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ."
Moertberg M., Neujahr H.Y.
FEBS Lett. 242:75-78(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.6"Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase."
Taylor M.G., Massey V.
J. Biol. Chem. 266:8291-8301(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.7"A fermentor culture for production of recombinant phenol hydroxylase."
Waters S., Neujahr H.Y.
Protein Expr. Purif. 5:534-540(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics."
Peelen S., Rietjens I.M., Boersma M.G., Vervoort J.
Eur. J. Biochem. 227:284-291(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.9"Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met."
Xu D., Ballou D.P., Massey V.
Biochemistry 40:12369-12378(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-55; ARG-282 AND TYR-290. - Ref.10"Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain."
Gerginova M., Manasiev J., Shivarova N., Alexieva Z.
Z. Naturforsch. C 62:83-86(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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=catechol- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
FAD
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Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION. - Ref.11"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 (2.40 ANGSTROMS) OF 2-665 IN COMPLEX WITH FAD AND PHENOL, SUBUNIT, COFACTOR. - Ref.12"High-resolution structure of phenol hydroxylase and correction of sequence errors."
Enroth C.
Acta Crystallogr. D 59:1597-1602(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD AND PHENOL, COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by excess phenol (PubMed:4146224). Heavy metals such AsCuSO4, AgNO3, or HgCl2 severely inhibit activity (PubMed:4146224).1 Publication
Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=18 µM for phenol1 Publication
Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION.
- KM=71 µM for NADPH1 Publication
Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION.
- KM=53 µM for O21 Publication
Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION.
pH dependencei
Optimum pH is 7.2-7.6.2 Publications
Manual assertion based on experiment ini
- Ref.4"Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum."
Neujahr H.Y., Gaal A.
Eur. J. Biochem. 35:386-400(1973) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION. - Ref.5"Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ."
Moertberg M., Neujahr H.Y.
FEBS Lett. 242:75-78(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Temperature dependencei
Optimum temperature is 30 degrees Celsius.1 Publication
Manual assertion based on experiment ini
- Ref.5"Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ."
Moertberg M., Neujahr H.Y.
FEBS Lett. 242:75-78(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: phenol degradation
This protein is involved in the pathway phenol degradation, which is part of Aromatic compound metabolism.1 PublicationManual assertion based on experiment ini
- Ref.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, FUNCTION, CATALYTIC ACTIVITY.
View all proteins of this organism that are known to be involved in the pathway phenol degradation and in Aromatic compound metabolism.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 55 | SubstrateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 118 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 290 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 290 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 358 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 18 – 19 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 2 | |
| Nucleotide bindingi | 43 – 45 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 3 | |
| Nucleotide bindingi | 51 – 56 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 6 | |
| Nucleotide bindingi | 368 – 372 | FADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 5 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- FAD binding Source: InterPro
- phenol 2-monooxygenase activity Source: UniProtKB-EC
GO - Biological processi
- phenol-containing compound catabolic process Source: UniProtKB-UniPathway
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Monooxygenase, Oxidoreductase |
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | FAD, Flavoprotein, NADP |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-14669 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00728 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Phenol hydroxylase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: PHHY1 Publication Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Trichosporon cutaneum (Yeast) (Oidium cutaneum) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 5554 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Trichosporonales › Trichosporonaceae › Cutaneotrichosporon |
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 55 | D → N: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 282 | R → M: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 290 | Y → F: Leads to a slightly higher redox potential but is reduced by NADPH much slower. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000214045 | 2 – 665 | Phenol hydroxylaseAdd BLAST | 664 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | P15245 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.11"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 (2.40 ANGSTROMS) OF 2-665 IN COMPLEX WITH FAD AND PHENOL, SUBUNIT, COFACTOR.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 4 – 14 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 18 – 33 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 39 – 42 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 44 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 59 – 66 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 67 – 69 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 71 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 83 – 89 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 95 – 104 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 118 – 133 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 142 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 152 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 163 – 169 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 172 – 174 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 186 – 188 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 192 – 200 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 214 – 224 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 231 – 236 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 241 – 257 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Turni | 261 – 264 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 265 – 270 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 272 – 274 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 276 – 281 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 287 – 293 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 305 – 307 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 310 – 321 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 327 – 343 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 347 – 349 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 350 – 352 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 353 – 355 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 357 – 359 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 370 – 389 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Helixi | 395 – 399 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 400 – 424 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
| Beta strandi | 429 – 432 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 435 – 437 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 439 – 453 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 473 – 475 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 489 – 492 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 493 – 496 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 497 – 500 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 501 – 504 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 511 – 518 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 523 – 537 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 542 – 546 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 555 – 565 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 572 – 574 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 577 – 580 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 587 – 591 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 596 – 598 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 603 – 607 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 611 – 613 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 615 – 619 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 623 – 629 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 634 – 642 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 649 – 651 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P15245 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P15245 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the PheA/TfdB FAD monooxygenase family.Curated
Phylogenomic databases
KEGG Orthology (KO) More...KOi | K03380 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.30.20, 1 hit 3.50.50.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002938 FAD-bd IPR036188 FAD/NAD-bd_sf IPR012941 Phe_hydrox_C_dim_dom IPR038220 PHOX_C_sf IPR036249 Thioredoxin-like_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01494 FAD_binding_3, 1 hit PF07976 Phe_hydrox_dim, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51905 SSF51905, 1 hit SSF52833 SSF52833, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P15245-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY
60 70 80 90 100
NGQADGLQCR TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR
110 120 130 140 150
IPDTLPGISR YHQVVLHQGR IERHILDSIA EISDTRIKVE RPLIPEKMEI
160 170 180 190 200
DSSKAEDPEA YPVTMTLRYM SDHESTPLQF GHKTENSLFH SNLQTQEEED
210 220 230 240 250
ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM IGEQTDYIWG
260 270 280 290 300
VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG
310 320 330 340 350
GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD
360 370 380 390 400
ERVFIAGDAC HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT
410 420 430 440 450
YEEERHAFAQ ALIDFDHQFS RLFSGRPAKD VADEMGVSMD VFKEAFVKGN
460 470 480 490 500
EFASGTAINY DENLVTDKKS SKQELAKNCV VGTRFKSQPV VRHSEGLWMH
510 520 530 540 550
FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN SVISLYTPKV
560 570 580 590 600
SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH
610 620 630 640 650
PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE
660
KSGAQTEADW TKSTA
Length:665
Mass (Da):75,162
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1401BE35D38BFB71
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L04488 mRNA Translation: AAA34202.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S07772 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:AAA34202 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P15245 | Phenol hydroxylase from Trichosporon Cutaneum | 665 | UniRef90_P15245 | |||
| UPI00001CE537 | 665 | |||||
| UPI0000111715 | 664 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P15245 | Phenol hydroxylase from Trichosporon Cutaneum | 665 | UniRef50_P15245 | |||
| Putative phenol 2-monooxygenase protein | 570 | |||||
| Putative phenol 2-monooxygenase protein | 600 | |||||
| UPI00001CE537 | 665 | |||||
| Phenol hydroxylase from Trichosporon Cutaneum | 707 | |||||
| +1 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L04488 mRNA Translation: AAA34202.1 |
| PIRi | S07772 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1FOH | X-ray | 2.40 | A/B/C/D | 2-665 | [»] | |
| 1PN0 | X-ray | 1.70 | A/B/C/D | 1-665 | [»] | |
| SMRi | P15245 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Proteomic databases
| PRIDEi | P15245 |
Genome annotation databases
| KEGGi | ag:AAA34202 |
Phylogenomic databases
| KOi | K03380 |
Enzyme and pathway databases
| UniPathwayi | UPA00728 |
| BioCyci | MetaCyc:MONOMER-14669 |
Miscellaneous databases
| EvolutionaryTracei | P15245 |
Family and domain databases
| Gene3Di | 3.40.30.20, 1 hit 3.50.50.60, 1 hit |
| InterProi | View protein in InterPro IPR002938 FAD-bd IPR036188 FAD/NAD-bd_sf IPR012941 Phe_hydrox_C_dim_dom IPR038220 PHOX_C_sf IPR036249 Thioredoxin-like_sf |
| Pfami | View protein in Pfam PF01494 FAD_binding_3, 1 hit PF07976 Phe_hydrox_dim, 1 hit |
| SUPFAMi | SSF51905 SSF51905, 1 hit SSF52833 SSF52833, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PHHY_TRICU | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P15245Primary (citable) accession number: P15245 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | September 18, 2019 | |
| This is version 118 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Fungal Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways
