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UniProtKB - P15245 (PHHY_TRICU)

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>

<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>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

<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

FAD3 Publications

<p>This subsection of the ‘Function’ 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

<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

  1. KM=18 µM for phenol1 Publication
  2. KM=71 µM for NADPH1 Publication
  3. KM=53 µM for O21 Publication

    pH dependencei

    Optimum pH is 7.2-7.6.2 Publications

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    <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 Publication
    View all proteins of this organism that are known to be involved in the pathway phenol degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei55SubstrateCombined sources2 Publications1
    Binding sitei118FADCombined sources2 Publications1
    Binding sitei290FADCombined sources2 Publications1
    Binding sitei290SubstrateCombined sources2 Publications1
    Binding sitei358FADCombined sources1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi18 – 19FADCombined sources2 Publications2
    Nucleotide bindingi43 – 45FADCombined sources2 Publications3
    Nucleotide bindingi51 – 56FADCombined sources2 Publications6
    Nucleotide bindingi368 – 372FADCombined sources2 Publications5

    <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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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 functionMonooxygenase, Oxidoreductase
    Biological processAromatic hydrocarbons catabolism
    LigandFAD, 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 (EC:1.14.13.78 Publications)
    Short name:
    PHHY1 Publication
    <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>OrganismiTrichosporon 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 identifieri5554 [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 lineageiEukaryota › 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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Mutagenesisi55D → N: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication1
    Mutagenesisi282R → M: Leads to a significant slower initial step of the oxidative half-reaction. 1 Publication1
    Mutagenesisi290Y → F: Leads to a slightly higher redox potential but is reduced by NADPH much slower. 1 Publication1

    <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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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 methionineiRemoved1 Publication
    <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_00002140452 – 665Phenol hydroxylaseAdd BLAST664

    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 Publication

    <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

    1665
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P15245

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P15245

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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>.<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 basket
    « Hide
            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
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links 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

    <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
    PIRiS07772

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FOHX-ray2.40A/B/C/D2-665[»]
    1PN0X-ray1.70A/B/C/D1-665[»]
    ProteinModelPortaliP15245
    SMRiP15245
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP15245

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA34202

    Phylogenomic databases

    KOiK03380

    Enzyme and pathway databases

    UniPathwayi
    UPA00728

    BioCyciMetaCyc:MONOMER-14669

    Miscellaneous databases

    EvolutionaryTraceiP15245

    Family and domain databases

    Gene3Di3.40.30.20, 1 hit
    3.50.50.60, 1 hit
    InterProiView 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
    PfamiView protein in Pfam
    PF01494 FAD_binding_3, 1 hit
    PF07976 Phe_hydrox_dim, 1 hit
    SUPFAMiSSF51905 SSF51905, 1 hit
    SSF52833 SSF52833, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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 nameiPHHY_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 116 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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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 sequencing

    Documents

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