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Protein

Ligninase H8

Gene

LPOA

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
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

Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.2 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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.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=130 µM for H2O21 Publication
  2. KM=116 µM for (3,4-dimethoxyphenyl)methanol1 Publication
  3. KM=30 µM for H2O21 Publication

    pH dependencei

    Optimum pH is 3.2 Publications

    <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: lignin degradation

    This protein is involved in the pathway lignin degradation, which is part of Secondary metabolite metabolism.
    View all proteins of this organism that are known to be involved in the pathway lignin degradation and in Secondary metabolite metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei71Transition state stabilizer1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei75Proton acceptor1
    <p>This subsection of the ‘Function’ 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 bindingi76Calcium 11
    Metal bindingi94Calcium 1; via carbonyl oxygen1
    Metal bindingi96Calcium 11
    Metal bindingi98Calcium 11
    Metal bindingi204Iron (heme axial ligand)1
    Metal bindingi205Calcium 21
    Metal bindingi222Calcium 21
    Metal bindingi224Calcium 21
    Metal bindingi227Calcium 2; via carbonyl oxygen1
    Metal bindingi229Calcium 21

    <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

    GO - Biological processi

    <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, Peroxidase
    Biological processHydrogen peroxide, Lignin degradation
    LigandCalcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-14338

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.11.1.14 1380

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

    More...
    UniPathwayi
    UPA00892

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    AA2 Auxiliary Activities 2

    mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

    More...
    mycoCLAPi
    LPO2H_PHACH

    PeroxiBase, a peroxidase database

    More...
    PeroxiBasei
    2412 PcLiP01_RP78

    <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:
    Ligninase H8 (EC:1.11.1.142 Publications)
    Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:LPOA
    <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>OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
    <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 identifieri5306 [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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002376022 – 281 Publication7
    <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_000002376129 – 372Ligninase H8Add BLAST344

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi31 ↔ 43
    Disulfide bondi42 ↔ 313
    Disulfide bondi62 ↔ 148
    Disulfide bondi277 ↔ 345
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P06181

    <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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.

    <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

    1372
    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
    P06181

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

    More...
    SMRi
    P06181

    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
    P06181

    <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 peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410II1B Eukaryota
    ENOG410ZS1R LUCA

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00692 ligninase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010255 Haem_peroxidase
    IPR002016 Haem_peroxidase_pln/fun/bac
    IPR001621 Ligninase
    IPR024589 Ligninase_C
    IPR019794 Peroxidases_AS
    IPR019793 Peroxidases_heam-ligand_BS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00141 peroxidase, 1 hit
    PF11895 Peroxidase_ext, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00462 LIGNINASE
    PR00458 PEROXIDASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48113 SSF48113, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00435 PEROXIDASE_1, 1 hit
    PS00436 PEROXIDASE_2, 1 hit
    PS50873 PEROXIDASE_4, 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.

    P06181-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAFKQLFAAI SLALLLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD
    60 70 80 90 100
    DIQQNLFHGG QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM
    110 120 130 140 150
    IFDDIETAFH PNIGLDEIVK LQKPFVQKHG VTPGDFIAFA GRVALSNCPG
    160 170 180 190 200
    APQMNFFTGR APATQPAPDG LVPEPFHTVD QIINRVNDAG EFDELELVWM
    210 220 230 240 250
    LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG TAFPGSGGNQ
    260 270 280 290 300
    GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL
    310 320 330 340 350
    TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF
    360 370
    PTLTTLPGPE TSVQRIPPPP GA
    Length:372
    Mass (Da):39,686
    Last modified:April 1, 1988 - v1
    <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:iE6ABA9FD48428FCC
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA33740 differs from that shown. Reason: Erroneous translation.Curated
    The sequence CAA68373 differs from that shown. Reason: Frameshift at position 351.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti15L → S. 1
    Natural varianti142R → A. 1

    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
    M37701 Genomic DNA Translation: AAA33740.1 Sequence problems.
    Y00262 mRNA Translation: CAA68373.1 Frameshift.
    M21913 mRNA No translation available.
    M27401 Genomic DNA Translation: AAA53109.1
    M27884 Genomic DNA Translation: AAB00798.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A27817
    A32322
    A43638
    B32322
    JT0402
    PS0010
    S01028
    S08202
    S69246

    <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
    M37701 Genomic DNA Translation: AAA33740.1 Sequence problems.
    Y00262 mRNA Translation: CAA68373.1 Frameshift.
    M21913 mRNA No translation available.
    M27401 Genomic DNA Translation: AAA53109.1
    M27884 Genomic DNA Translation: AAB00798.1
    PIRiA27817
    A32322
    A43638
    B32322
    JT0402
    PS0010
    S01028
    S08202
    S69246

    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
    1B80X-ray1.73A/B22-372[»]
    1B82X-ray1.80A/B22-372[»]
    1B85X-ray1.85A/B22-372[»]
    ProteinModelPortaliP06181
    SMRiP06181
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2 Auxiliary Activities 2
    mycoCLAPiLPO2H_PHACH
    PeroxiBasei2412 PcLiP01_RP78

    Proteomic databases

    PRIDEiP06181

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410II1B Eukaryota
    ENOG410ZS1R LUCA

    Enzyme and pathway databases

    UniPathwayi
    UPA00892

    BioCyciMetaCyc:MONOMER-14338
    BRENDAi1.11.1.14 1380

    Miscellaneous databases

    EvolutionaryTraceiP06181

    Family and domain databases

    CDDicd00692 ligninase, 1 hit
    InterProiView protein in InterPro
    IPR010255 Haem_peroxidase
    IPR002016 Haem_peroxidase_pln/fun/bac
    IPR001621 Ligninase
    IPR024589 Ligninase_C
    IPR019794 Peroxidases_AS
    IPR019793 Peroxidases_heam-ligand_BS
    PfamiView protein in Pfam
    PF00141 peroxidase, 1 hit
    PF11895 Peroxidase_ext, 1 hit
    PRINTSiPR00462 LIGNINASE
    PR00458 PEROXIDASE
    SUPFAMiSSF48113 SSF48113, 1 hit
    PROSITEiView protein in PROSITE
    PS00435 PEROXIDASE_1, 1 hit
    PS00436 PEROXIDASE_2, 1 hit
    PS50873 PEROXIDASE_4, 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 nameiLIG8_PHACH
    <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: P06181
    <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: January 1, 1988
    Last sequence update: April 1, 1988
    Last modified: December 5, 2018
    This is version 130 of the entry and version 1 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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