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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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O.2 Publications
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O.2 Publications

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

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

    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
    Sitei71Transition state stabilizer1
    Active sitei75Proton acceptor1
    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

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide, Lignin degradation

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14338.
    BRENDAi1.11.1.14. 1380.
    UniPathwayiUPA00892.

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    mycoCLAPiLPO2H_PHACH.
    PeroxiBasei2412. PcLiP01_RP78.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ligninase H8 (EC:1.11.1.142 Publications)
    Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase1 Publication
    Gene namesi
    Name:LPOA
    OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
    Taxonomic identifieri5306 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Sequence analysisAdd BLAST21
    PropeptideiPRO_000002376022 – 281 Publication7
    ChainiPRO_000002376129 – 372Ligninase H8Add BLAST344

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi31 ↔ 43
    Disulfide bondi42 ↔ 313
    Disulfide bondi62 ↔ 148
    Disulfide bondi277 ↔ 345
    Glycosylationi285N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

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

    Expressioni

    Developmental stagei

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

    Structurei

    Secondary structure

    1372
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi36 – 39Combined sources4
    Helixi40 – 44Combined sources5
    Helixi45 – 55Combined sources11
    Turni58 – 60Combined sources3
    Helixi64 – 77Combined sources14
    Helixi82 – 86Combined sources5
    Beta strandi94 – 97Combined sources4
    Helixi98 – 101Combined sources4
    Helixi103 – 106Combined sources4
    Helixi110 – 112Combined sources3
    Turni113 – 115Combined sources3
    Helixi116 – 129Combined sources14
    Helixi133 – 146Combined sources14
    Helixi179 – 190Combined sources12
    Helixi194 – 200Combined sources7
    Helixi201 – 206Combined sources6
    Beta strandi208 – 213Combined sources6
    Beta strandi219 – 223Combined sources5
    Helixi231 – 235Combined sources5
    Beta strandi244 – 247Combined sources4
    Beta strandi255 – 257Combined sources3
    Helixi264 – 269Combined sources6
    Turni273 – 275Combined sources3
    Helixi276 – 281Combined sources6
    Turni282 – 284Combined sources3
    Helixi286 – 301Combined sources16
    Turni302 – 304Combined sources3
    Helixi307 – 309Combined sources3
    Beta strandi310 – 312Combined sources3
    Helixi314 – 316Combined sources3
    Beta strandi325 – 327Combined sources3
    Helixi338 – 340Combined sources3
    Beta strandi346 – 348Combined sources3
    Beta strandi357 – 359Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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...

    Miscellaneous databases

    EvolutionaryTraceiP06181.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG410II1B. Eukaryota.
    ENOG410ZS1R. LUCA.

    Family and domain databases

    CDDicd00692. ligninase. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 1 hit.
    PF11895. Peroxidase_ext. 1 hit.
    [Graphical view]
    PRINTSiPR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:iE6ABA9FD48428FCC
    GO

    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
    Natural varianti15L → S.1
    Natural varianti142R → A.1

    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.

    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:
    PDBei
    RCSB PDBi
    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.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410II1B. Eukaryota.
    ENOG410ZS1R. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00892.
    BioCyciMetaCyc:MONOMER-14338.
    BRENDAi1.11.1.14. 1380.

    Miscellaneous databases

    EvolutionaryTraceiP06181.

    Family and domain databases

    CDDicd00692. ligninase. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 1 hit.
    PF11895. Peroxidase_ext. 1 hit.
    [Graphical view]
    PRINTSiPR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLIG8_PHACH
    AccessioniPrimary (citable) accession number: P06181
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: April 1, 1988
    Last modified: November 30, 2016
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.