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Protein

Ligninase B

Gene

LIPB

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.1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+PROSITE-ProRule annotationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation

Kineticsi

  1. KM=85 µM for H2O21 Publication
  2. KM=83 µM for (3,4-dimethoxyphenyl)methanol1 Publication

    pH dependencei

    Optimum pH is 2.3.1 Publication

    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 stabilizerPROSITE-ProRule annotation1
    Active sitei75Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi76Calcium 1PROSITE-ProRule annotation1
    Metal bindingi94Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi96Calcium 1PROSITE-ProRule annotation1
    Metal bindingi98Calcium 1PROSITE-ProRule annotation1
    Metal bindingi204Iron (heme axial ligand)PROSITE-ProRule annotation1
    Metal bindingi205Calcium 2PROSITE-ProRule annotation1
    Metal bindingi222Calcium 2PROSITE-ProRule annotation1
    Metal bindingi224Calcium 2PROSITE-ProRule annotation1
    Metal bindingi227Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi229Calcium 2PROSITE-ProRule annotation1

    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

    UniPathwayiUPA00892.

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ligninase B (EC:1.11.1.141 Publication)
    Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase
    Gene namesi
    Name:LIPB
    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_000002377422 – 281 Publication7
    ChainiPRO_000002377529 – 372Ligninase BAdd BLAST344

    Amino acid modifications

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

    Keywords - PTMi

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

    Structurei

    3D structure databases

    ProteinModelPortaliP31838.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    P31838-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAFKQLFAAI SLALSLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD
    60 70 80 90 100
    DIQQNLFHGG QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM
    110 120 130 140 150
    IFDDIETAFH PNIGLDEIVK LQKPFVQKHG VTPGAFIAFA GAVALSNCPG
    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):39,530
    Last modified:July 1, 1993 - v1
    Checksum:iE0DD2CF40425D9D5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X54257 Genomic DNA. Translation: CAA38178.1.
    PIRiA32322.
    B32322.
    PS0010.
    S13564. OPJGBP.
    S69246.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X54257 Genomic DNA. Translation: CAA38178.1.
    PIRiA32322.
    B32322.
    PS0010.
    S13564. OPJGBP.
    S69246.

    3D structure databases

    ProteinModelPortaliP31838.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410II1B. Eukaryota.
    ENOG410ZS1R. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00892.

    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 nameiLIGB_PHACH
    AccessioniPrimary (citable) accession number: P31838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: November 30, 2016
    This is version 92 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.