P06181 (LIG8_PHACH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ligninase H8
EC=1.11.1.14

Alternative name(s):
Diarylpropane peroxidase
Lignin peroxidase

Gene names

Name:

LPOA

Organism

Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)

Taxonomic identifier

5306 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetes incertae sedis › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
Catalytic activity	(3,4-dimethoxyphenyl)methanol + H2O2 = 3,4-dimethoxybenzaldehyde + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Pathway	Secondary metabolite metabolism; lignin degradation.
Developmental stage	Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.
Sequence similarities	Belongs to the peroxidase family. Ligninase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide Lignin degradation
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	diarylpropane peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 28

7

PRO_0000023760

Chain

29 – 372

344

Ligninase H8

PRO_0000023761

Sites

Active site

75

1

Proton acceptor

Metal binding

76

1

Calcium 1

Metal binding

94

1

Calcium 1; via carbonyl oxygen

Metal binding

96

1

Calcium 1

Metal binding

98

1

Calcium 1

Metal binding

204

1

Iron (heme axial ligand)

Metal binding

205

1

Calcium 2

Metal binding

222

1

Calcium 2

Metal binding

224

1

Calcium 2

Metal binding

227

1

Calcium 2; via carbonyl oxygen

Metal binding

229

1

Calcium 2

Site

71

1

Transition state stabilizer

Amino acid modifications

Glycosylation

285

1

N-linked (GlcNAc...) Potential

Disulfide bond

31 ↔ 43

Disulfide bond

42 ↔ 313

Disulfide bond

62 ↔ 148

Disulfide bond

277 ↔ 345

Natural variations

Natural variant

15

1

L → S.

Natural variant

142

1

R → A.

Secondary structure

1

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372

Helix Strand Turn

Details...

Beta strand

36 – 39

4

Helix

40 – 44

5

Helix

45 – 55

11

Turn

58 – 60

3

Helix

64 – 77

14

Helix

82 – 86

5

Beta strand

94 – 97

4

Helix

98 – 101

4

Helix

103 – 106

4

Helix

110 – 112

3

Turn

113 – 115

3

Helix

116 – 129

14

Helix

133 – 146

14

Helix

179 – 190

12

Helix

194 – 200

7

Helix

201 – 206

6

Beta strand

208 – 213

6

Beta strand

219 – 223

5

Helix

231 – 235

5

Beta strand

244 – 247

4

Beta strand

255 – 257

3

Helix

264 – 269

6

Turn

273 – 275

3

Helix

276 – 281

6

Turn

282 – 284

3

Helix

286 – 301

16

Turn

302 – 304

3

Helix

307 – 309

3

Beta strand

310 – 312

3

Helix

314 – 316

3

Beta strand

325 – 327

3

Helix

338 – 340

3

Beta strand

346 – 348

3

Beta strand

357 – 359

3

Sequences

	Sequence		Length	Mass (Da)
	P06181 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: E6ABA9FD48428FCC	FASTA	372	39,686
	10 20 30 40 50 60 MAFKQLFAAI SLALLLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD DIQQNLFHGG 70 80 90 100 110 120 QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK 130 140 150 160 170 180 LQKPFVQKHG VTPGDFIAFA GRVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD 190 200 210 220 230 240 QIINRVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG 250 260 270 280 290 300 TAFPGSGGNQ GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL 310 320 330 340 350 360 TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF PTLTTLPGPE 370 TSVQRIPPPP GA

References

[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]	"Crystal structure of lignin peroxidase." Edwards S.L., Raag R., Wariishi H., Gold M.H., Poulos T.L. Proc. Natl. Acad. Sci. U.S.A. 90:750-754(1993) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A27817.
A32322.
A43638.
B32322.
JT0402.
PS0010.
S01028.
S08202.
S69246.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B80	X-ray	1.73	A/B	24-372	[»]
1B82	X-ray	1.80	A/B	22-372	[»]
1B85	X-ray	1.85	A/B	22-372	[»]

ProteinModelPortal

P06181.

SMR

P06181. Positions 24-372.

ModBase

Search...

Protein family/group databases

mycoCLAP

LPOH_PHACH.

PeroxiBase

2412. PcLiP01_RP78.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

NOG250742.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14338.

BRENDA

1.11.1.14. 4722.

UniPathway

UPA00892.

Family and domain databases

InterPro

IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Pfam

PF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00462. LIGNINASE.
PR00458. PEROXIDASE.

SUPFAM

SSF48113. Peroxidase_super. 1 hit.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06181.

Entry information

Entry name

LIG8_PHACH

Accession

Primary (citable) accession number: P06181

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	April 1, 1988
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program