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UniProtKB - Q47914 (PCPD_SPHCR)

Entry version 121 (12 Aug 2020)
Sequence version 2 (01 Oct 2002)
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Protein

Tetrachlorobenzoquinone reductase

Gene

pcpD

Organism
Sphingobium chlorophenolicum
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

Involved in the degradation of the xenobiocide pentachlorophenol (PCP) (PubMed:19325743, PubMed:23676275). Catalyzes the reduction of tetrachlorobenzoquinone (TCBQ) to yield tetrachlorohydroquinone (TCHQ) (PubMed:19325743, PubMed:23676275). Also able to reduce 2,6-dichloroindophenol (DCIP) (PubMed:23676275).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

In vitro, activated by tetrachlorohydroquinone (TCHQ) at low concentrations and inhibited at high concentrations (above 200 µM). However, PcpD would only be stimulated by tetrachlorohydroquinone (TCHQ) under in vivo conditions due to the toxicity of tetrachlorohydroquinone (TCHQ). Competitively inhibited by pentachlorophenol (PCP) in a concentration-dependent manner. PcpD is regulated by tetrachlorohydroquinone (TCHQ) and pentachlorophenol (PCP) using a mechanism, which maintains tetrachlorobenzoquinone at a level that would neither significantly decrease the biodegradation of pentachlorophenol (PCP) nor cause cytotoxicity in cells.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

Kcat is 20.1 sec(-1) for NADH as substrate (with 90 µM cytochrome c). Kcat is 14.1 sec(-1) for 2,6-dichloroindophenol (DCIP) as substrate (with 100 µM NADH). Kcat is 9.1 sec(-1) for cytochrome c as substrate (with 100 µM NADH). Kcat is 3.7 sec(-1) for NADPH as substrate (with 90 µM cytochrome c).1 Publication
  1. KM=1.21 µM for NADPH (with 90 µM cytochrome c)1 Publication
  2. KM=11.5 µM for NADH (with 90 µM cytochrome c)1 Publication
  3. KM=17.6 µM for cytochrome c (with 100 µM NADH)1 Publication
  4. KM=38.3 µM for 2,6-dichloroindophenol (DCIP) (with 100 µM NADH)1 Publication

    pH dependencei

    Optimum pH is 7. It maintains more than 70% of its optimal activity even at pH 5.0. PcpD loses its activity quickly in basic solutions, retaining less than 20% of its optimal activity at pH 8.0.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pentachlorophenol degradation

    This protein is involved in the pathway pentachlorophenol degradation, which is part of Xenobiotic degradation.1 Publication1 Publication
    View all proteins of this organism that are known to be involved in the pathway pentachlorophenol degradation and in Xenobiotic degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi273Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi278Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi281Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
    Metal bindingi311Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionOxidoreductase
    Biological processAromatic hydrocarbons catabolism, Electron transport, Transport
    Ligand2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

    Enzyme and pathway databases

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00691

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Tetrachlorobenzoquinone reductase1 Publication (EC:1.1.1.4042 Publications)
    Short name:
    TCBQ reductase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:pcpD1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSphingobium chlorophenolicum
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri46429 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Sphingobium

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene show a significant sensitivity to pentachlorophenol (PCP) and 2,4,6-trichlorophenol (TriCP).1 Publication

    <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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004444441 – 324Tetrachlorobenzoquinone reductaseAdd BLAST324

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Constitutively expressed.1 Publication

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotrimer.

    2 Publications

    <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

    3D structure databases

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

    More...    SMRi    		Q47914

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 107FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST103
    Domaini238 – 3242Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST87

    <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 PDR/VanB family.Curated

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00207, fer2, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.10.20.30, 1 hit
    3.40.50.80, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR036010, 2Fe-2S_ferredoxin-like_sf
    IPR001041, 2Fe-2S_ferredoxin-type
    IPR006058, 2Fe2S_fd_BS
    IPR012675, Beta-grasp_dom_sf
    IPR017927, FAD-bd_FR_type
    IPR039261, FNR_nucleotide-bd
    IPR001433, OxRdtase_FAD/NAD-bd
    IPR000951, Ph_dOase_redase
    IPR017938, Riboflavin_synthase-like_b-brl

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00111, Fer2, 1 hit
    PF00175, NAD_binding_1, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00409, PHDIOXRDTASE

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52343, SSF52343, 1 hit
    SSF54292, SSF54292, 1 hit
    SSF63380, SSF63380, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00197, 2FE2S_FER_1, 1 hit
    PS51085, 2FE2S_FER_2, 1 hit
    PS51384, FAD_FR, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q47914-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTNPVSTIDM TVTQITRVAK DINSYELRPE PGVILPEFTA GAHIGVSLPN 
            60         70         80         90        100
    GIQRSYSLVN PQGERDRYVI TVNLDRNSRG GSRYLHEQLR VGQRLSIVPP 
           110        120        130        140        150
    ANNFALVETA PHSVLFAGGI GITPIWSMIQ RLRELGSTWE LHYACRGKDF 
           160        170        180        190        200
    VAYRQELEQA AAEAGARFHL HLDEEADGKF LDLAGPVAQA GQDSIFYCCG 
           210        220        230        240        250
    PEAMLQAYKA ATADLPSERV RFEHFGAALT GEPADDVFTV VLARRSGQEF 
           260        270        280        290        300
    TVEPGMTILE TLLQNGISRN YSCTQGVCGT CETKVLEGEP DHRDWVLSDE 
           310        320 
    KKASNSTMLI CCSLSKSPRL VLDI
    Length:324
    Mass (Da):35,598
    Last modified:October 1, 2002 - v2
    <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:i1FADB899AECC90AE
    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
    		U12290 Genomic DNA Translation: AAA68938.2

    <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
    		U12290 Genomic DNA Translation: AAA68938.2

    3D structure databases

    SMRiQ47914
    ModBaseiSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00691

    Family and domain databases

    CDDicd00207, fer2, 1 hit
    Gene3Di3.10.20.30, 1 hit
    3.40.50.80, 1 hit
    InterProiView protein in InterPro
    IPR036010, 2Fe-2S_ferredoxin-like_sf
    IPR001041, 2Fe-2S_ferredoxin-type
    IPR006058, 2Fe2S_fd_BS
    IPR012675, Beta-grasp_dom_sf
    IPR017927, FAD-bd_FR_type
    IPR039261, FNR_nucleotide-bd
    IPR001433, OxRdtase_FAD/NAD-bd
    IPR000951, Ph_dOase_redase
    IPR017938, Riboflavin_synthase-like_b-brl
    PfamiView protein in Pfam
    PF00111, Fer2, 1 hit
    PF00175, NAD_binding_1, 1 hit
    PRINTSiPR00409, PHDIOXRDTASE
    SUPFAMiSSF52343, SSF52343, 1 hit
    SSF54292, SSF54292, 1 hit
    SSF63380, SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS00197, 2FE2S_FER_1, 1 hit
    PS51085, 2FE2S_FER_2, 1 hit
    PS51384, FAD_FR, 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 nameiPCPD_SPHCR
    <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: Q47914
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2018
    Last sequence update: October 1, 2002
    Last modified: August 12, 2020
    This is version 121 of the entry and version 2 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 programProkaryotic 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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