Reviewed, UniProtKB/Swiss-Prot P49012 (LIG2_PHACH)

Names and origin

Protein names

Recommended name:
    Ligninase LG2
    EC=1.11.1.14
Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase

Gene names

Name:	GLG2
Synonyms:	LIP2

Organism

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

Taxonomic identifier

5306 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	371 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	1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H(2)O(2) = 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H(2)O.
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	Lignin degradation
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Cleavage on pair of basic residues Glycoprotein Hydroxylation Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW diarylpropane peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro iron 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

Propeptide

22 – 28

7

PRO_0000023762

Chain

29 – 371

343

Ligninase LG2

PRO_0000023763

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

Modified residue

199

1

3-hydroxytryptophan

Glycosylation

285

1

N-linked (GlcNAc...) Potential

Disulfide bond

31 ↔ 43

Disulfide bond

42 ↔ 313

Disulfide bond

62 ↔ 148

Disulfide bond

277 ↔ 345

Secondary structure

1

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371

Helix Strand Turn

Details...

Helix

40 – 43

4

Helix

44 – 55

12

Turn

58 – 60

3

Helix

64 – 77

14

Helix

82 – 85

4

Beta strand

87 – 89

3

Beta strand

94 – 97

4

Helix

98 – 101

4

Helix

103 – 106

4

Helix

110 – 112

3

Helix

115 – 129

15

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

255 – 258

4

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)
	P49012-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F6AAB123EDC92123	FASTA	371	39,329
	10 20 30 40 50 60 MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD DIQANMFHGG 70 80 90 100 110 120 QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM IFDTIETAFH PNIGLDEVVA 130 140 150 160 170 180 MQKPFVQKHG VTPGDFIAFA GAVALSNCPG APQMNFFTGR KPATQPAPDG LVPEPFHTVD 190 200 210 220 230 240 QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG 250 260 270 280 290 300 TLFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL 310 320 330 340 350 360 TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF PSLVTLPGPA 370 TSVARIPPHK A

References

[1]	"Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme." Ritch T.G. Jr., Nipper V.J., Akileswaran L., Smith A.J., Pribnow D.G., Gold M.H. Gene 107:119-126(1991) [PubMed: 1743510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-48. Strain: ATCC 201542 / OGC101.
[2]	"Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporium." Ritch T.G. Jr., Gold M.H. Gene 118:73-80(1992) [PubMed: 1511887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 201542 / OGC101.
[3]	"Crystallographic refinement of lignin peroxidase at 2 A." Poulos T.L., Edwards S.L., Wariishi H., Gold M.H. J. Biol. Chem. 268:4429-4440(1993) [PubMed: 8440725] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]	"The crystal structure of lignin peroxidase at 1.70-A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle." Choinowski T., Blodig W., Winterhalter K.H., Piontek K. J. Mol. Biol. 286:809-827(1999) [PubMed: 10024453] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), HYDROXYLATION AT TRP-199. Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M74229 mRNA. Translation: AAA33735.1.
M92644 Genomic DNA. Translation: AAA33738.1.

PIR

JC1268.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LGA	X-ray	2.03	A/B	29-371	[»]
1LLP	X-ray	1.70	A	29-371	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

2409. PcLiPE_OGC101.

Family and domain databases

InterPro

IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
[Graphical view]

Pfam

PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00462. LIGNINASE.
PR00458. PEROXIDASE.

PROSITE

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

ProtoNet

Search...

Other Resources

LinkHub

P49012.

Entry information

Entry name

LIG2_PHACH

Accession

Primary (citable) accession number: P49012

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)