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Protein

Ligninase A

Gene

LIPA

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=140 µM for H2O21 Publication
  2. KM=200 µM for (3,4-dimethoxyphenyl)methanol1 Publication

    pH dependencei

    Optimum pH is 2.5.1 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

    BioCyciMetaCyc:MONOMER-14336.
    UniPathwayiUPA00892.

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    PeroxiBasei2413. PcLiP02_RP78.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ligninase A (EC:1.11.1.141 Publication)
    Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase
    Gene namesi
    Name:LIPA
    Synonyms:LPOB
    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_000002377222 – 281 Publication7
    ChainiPRO_000002377329 – 372Ligninase AAdd 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

    Proteomic databases

    PRIDEiP31837.

    Structurei

    3D structure databases

    ProteinModelPortaliP31837.
    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.

    P31837-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAFKQLVAAI SLALSLTTAN AAVVKEKRAT CSNGATVGDA SCCAWFDVLD
    60 70 80 90 100
    DIQQNLFQGG QCGAEAHESI RLVFHDAIAI SPAMEAQGKF GGGGADGSIM
    110 120 130 140 150
    IFDDIEPNFH PNIGLDEIIN LQKPFVQKHG VTPGAFIAFA GAVALSNCPG
    160 170 180 190 200
    APQMNFFTGR APATQPAPDG LVPEPFHTVD QIIARVNDAG EFDELELVWM
    210 220 230 240 250
    LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG ILFPGSGGNQ
    260 270 280 290 300
    GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL
    310 320 330 340 350
    TQLGQDPNAM TDCSDVIPIS KPIPGNLPFS FFPPGKSMKD VEQACAETPF
    360 370
    PSLVTLPGPA TSVARIPPPP GA
    Length:372
    Mass (Da):39,394
    Last modified:July 1, 1993 - v1
    Checksum:i04CE4598D6D6F09B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti135A → D in AAA33741 (PubMed:2373364).Curated1
    Sequence conflicti161A → R in AAA33741 (PubMed:2373364).Curated1
    Sequence conflicti298L → H in AAA33741 (PubMed:2373364).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X54257 Genomic DNA. Translation: CAA38177.1.
    M37701 Genomic DNA. Translation: AAA33741.1.
    PIRiJH0156.
    PS0011.
    S13563. OPJGAP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X54257 Genomic DNA. Translation: CAA38177.1.
    M37701 Genomic DNA. Translation: AAA33741.1.
    PIRiJH0156.
    PS0011.
    S13563. OPJGAP.

    3D structure databases

    ProteinModelPortaliP31837.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    PeroxiBasei2413. PcLiP02_RP78.

    Proteomic databases

    PRIDEiP31837.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410II1B. Eukaryota.
    ENOG410ZS1R. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00892.
    BioCyciMetaCyc:MONOMER-14336.

    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 nameiLIGA_PHACH
    AccessioniPrimary (citable) accession number: P31837
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: November 30, 2016
    This is version 96 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.