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P06181

- LIG8_PHACH

UniProt

P06181 - LIG8_PHACH

Protein

Ligninase H8

Gene

LPOA

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    (3,4-dimethoxyphenyl)methanol + H2O2 = 3,4-dimethoxybenzaldehyde + 2 H2O.

    Cofactori

    Binds 2 calcium ions per subunit.
    Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei71 – 711Transition state stabilizer
    Active sitei75 – 751Proton acceptor
    Metal bindingi76 – 761Calcium 1
    Metal bindingi94 – 941Calcium 1; via carbonyl oxygen
    Metal bindingi96 – 961Calcium 1
    Metal bindingi98 – 981Calcium 1
    Metal bindingi204 – 2041Iron (heme axial ligand)
    Metal bindingi205 – 2051Calcium 2
    Metal bindingi222 – 2221Calcium 2
    Metal bindingi224 – 2241Calcium 2
    Metal bindingi227 – 2271Calcium 2; via carbonyl oxygen
    Metal bindingi229 – 2291Calcium 2

    GO - Molecular functioni

    1. diarylpropane peroxidase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW
    2. lignin catabolic process Source: UniProtKB-UniPathway

    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. 4722.
    UniPathwayiUPA00892.

    Protein family/group databases

    mycoCLAPiLPO2H_PHACH.
    PeroxiBasei2412. PcLiP01_RP78.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ligninase H8 (EC:1.11.1.14)
    Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase
    Gene namesi
    Name:LPOA
    OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
    Taxonomic identifieri5306 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 2871 PublicationPRO_0000023760
    Chaini29 – 372344Ligninase H8PRO_0000023761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 43
    Disulfide bondi42 ↔ 313
    Disulfide bondi62 ↔ 148
    Disulfide bondi277 ↔ 345
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis

    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

    1
    372
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 394
    Helixi40 – 445
    Helixi45 – 5511
    Turni58 – 603
    Helixi64 – 7714
    Helixi82 – 865
    Beta strandi94 – 974
    Helixi98 – 1014
    Helixi103 – 1064
    Helixi110 – 1123
    Turni113 – 1153
    Helixi116 – 12914
    Helixi133 – 14614
    Helixi179 – 19012
    Helixi194 – 2007
    Helixi201 – 2066
    Beta strandi208 – 2136
    Beta strandi219 – 2235
    Helixi231 – 2355
    Beta strandi244 – 2474
    Beta strandi255 – 2573
    Helixi264 – 2696
    Turni273 – 2753
    Helixi276 – 2816
    Turni282 – 2843
    Helixi286 – 30116
    Turni302 – 3043
    Helixi307 – 3093
    Beta strandi310 – 3123
    Helixi314 – 3163
    Beta strandi325 – 3273
    Helixi338 – 3403
    Beta strandi346 – 3483
    Beta strandi357 – 3593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B80X-ray1.73A/B22-372[»]
    1B82X-ray1.80A/B22-372[»]
    1B85X-ray1.85A/B22-372[»]
    ProteinModelPortaliP06181.
    SMRiP06181. Positions 24-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06181.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250742.

    Family and domain databases

    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF11895. DUF3415. 1 hit.
    PF00141. peroxidase. 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

    MAFKQLFAAI SLALLLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD    50
    DIQQNLFHGG QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM 100
    IFDDIETAFH PNIGLDEIVK LQKPFVQKHG VTPGDFIAFA GRVALSNCPG 150
    APQMNFFTGR APATQPAPDG LVPEPFHTVD QIINRVNDAG EFDELELVWM 200
    LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG TAFPGSGGNQ 250
    GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL 300
    TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF 350
    PTLTTLPGPE TSVQRIPPPP GA 372
    Length:372
    Mass (Da):39,686
    Last modified:April 1, 1988 - v1
    Checksum:iE6ABA9FD48428FCC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151L → S.
    Natural varianti142 – 1421R → A.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37701 Genomic DNA. Translation: AAA33740.1. Sequence problems.
    Y00262 mRNA. Translation: CAA68373.1. Sequence problems.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37701 Genomic DNA. Translation: AAA33740.1 . Sequence problems.
    Y00262 mRNA. Translation: CAA68373.1 . Sequence problems.
    M21913 mRNA. No translation available.
    M27401 Genomic DNA. Translation: AAA53109.1 .
    M27884 Genomic DNA. Translation: AAB00798.1 .
    PIRi A27817.
    A32322.
    A43638.
    B32322.
    JT0402.
    PS0010.
    S01028.
    S08202.
    S69246.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B80 X-ray 1.73 A/B 22-372 [» ]
    1B82 X-ray 1.80 A/B 22-372 [» ]
    1B85 X-ray 1.85 A/B 22-372 [» ]
    ProteinModelPortali P06181.
    SMRi P06181. Positions 24-372.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi LPO2H_PHACH.
    PeroxiBasei 2412. PcLiP01_RP78.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG250742.

    Enzyme and pathway databases

    UniPathwayi UPA00892 .
    BioCyci MetaCyc:MONOMER-14338.
    BRENDAi 1.11.1.14. 4722.

    Miscellaneous databases

    EvolutionaryTracei P06181.

    Family and domain databases

    InterProi IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view ]
    Pfami PF11895. DUF3415. 1 hit.
    PF00141. peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium."
      Tien M., Tu C.-P.D.
      Nature 326:520-523(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
    2. Erratum
      Tien M., Tu C.-P.D.
      Nature 328:742-742(1987)
      Cited for: SEQUENCE REVISION.
    3. "Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase gene."
      Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M., Leisola M., Teeri T., Knowles J.K.C., Fiechter A.
      Gene 70:127-137(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    4. "Nucleotide sequence of a ligninase gene from Phanerochaete chrysosporium."
      Smith T.L., Schalch H., Gaskell J., Covert S., Cullan D.
      Nucleic Acids Res. 16:1219-1219(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    5. "Characterization of two lignin peroxidase clones from Phanerochaete chrysosporium."
      Andrawis A., Pease E.A., Kuan I., Holzbaur E., Tien M.
      Biochem. Biophys. Res. Commun. 162:673-680(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium."
      Holzbaur E.L.F., Tien M.
      Biochem. Biophys. Res. Commun. 155:626-633(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1.
    7. "Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes."
      Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M., Smit J.D.G., Leisola M.S.A.
      Eur. J. Biochem. 187:515-520(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-58.
      Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
    8. "Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase."
      Tien M., Kirk T.K.
      Proc. Natl. Acad. Sci. U.S.A. 81:2280-2284(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    10. "Autocatalytic formation of a hydroxy group at C beta of Trp171 in lignin peroxidase."
      Blodig W., Doyle W.A., Smith A.T., Winterhalter K.H., Choinowski T., Piontek K.
      Biochemistry 37:8832-8838(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
      Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.

    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: October 1, 2014
    This is version 114 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

    External Data

    Dasty 3