Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06181

- LIG8_PHACH

UniProt

P06181 - LIG8_PHACH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme bNote: Binds 1 heme b (iron(II)-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
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. 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 – 394Combined sources
Helixi40 – 445Combined sources
Helixi45 – 5511Combined sources
Turni58 – 603Combined sources
Helixi64 – 7714Combined sources
Helixi82 – 865Combined sources
Beta strandi94 – 974Combined sources
Helixi98 – 1014Combined sources
Helixi103 – 1064Combined sources
Helixi110 – 1123Combined sources
Turni113 – 1153Combined sources
Helixi116 – 12914Combined sources
Helixi133 – 14614Combined sources
Helixi179 – 19012Combined sources
Helixi194 – 2007Combined sources
Helixi201 – 2066Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi219 – 2235Combined sources
Helixi231 – 2355Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi255 – 2573Combined sources
Helixi264 – 2696Combined sources
Turni273 – 2753Combined sources
Helixi276 – 2816Combined sources
Turni282 – 2843Combined sources
Helixi286 – 30116Combined sources
Turni302 – 3043Combined sources
Helixi307 – 3093Combined sources
Beta strandi310 – 3123Combined sources
Helixi314 – 3163Combined sources
Beta strandi325 – 3273Combined sources
Helixi338 – 3403Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi357 – 3593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 115 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