Reviewed, UniProtKB/Swiss-Prot P11543 (LIG5_PHACH)

Names and origin

Protein names

Recommended name:
    Ligninase LG5
    EC=1.11.1.14
Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase

Gene names

Name:	GLG5
Synonyms:	LIP6

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 transcript 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 By similarity.
Pathway	Secondary metabolite metabolism; lignin degradation.
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 Glycoprotein Zymogen
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-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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	Potential
	Propeptide	22 – 27	6	Potential		PRO_0000023768
	Chain	28 – 371	344	Ligninase LG5		PRO_0000023769
Sites
	Active site	74	1	Proton acceptor By similarity
	Metal binding	75	1	Calcium 1 By similarity
	Metal binding	92	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	94	1	Calcium 1 By similarity
	Metal binding	96	1	Calcium 1 By similarity
	Metal binding	202	1	Iron (heme axial ligand) By similarity
	Metal binding	203	1	Calcium 2 By similarity
	Metal binding	220	1	Calcium 2 By similarity
	Metal binding	222	1	Calcium 2 By similarity
	Metal binding	225	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	227	1	Calcium 2 By similarity
	Site	70	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	283	1	N-linked (GlcNAc...) Potential
	Disulfide bond	30 ↔ 42		By similarity
	Disulfide bond	41 ↔ 311		By similarity
	Disulfide bond	61 ↔ 146		By similarity
	Disulfide bond	275 ↔ 344		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11543-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: F0AE30C69D7EF5C2	FASTA	371	39,418
	10 20 30 40 50 60 MAFKKLLAVL TAALSLRAAQ GAAVEKRATC SNGKVVPAAS CCTWFNVLSD IQENLFNGGQ 70 80 90 100 110 120 CGAEAHESIR LVFHDAIAIS PAMEPQASSV RGADGSIMIF DEIETNFHPN IGLDEIVRLQ 130 140 150 160 170 180 KPFVQKHGVT PGDFIAFAGA VALSNCPGAP QMNFFTGRAP ATQPAPDGLV PEPFHSVDQI 190 200 210 220 230 240 IDRVFDAGEF DELELVWMLS AHSVAAANDI DPNIQGLPFD STPGIFDSQF FVETQLAGTG 250 260 270 280 290 300 FTGGSNNQGE VSSPLPGEMR LQSDFLIARD ARTACEWQSF VNNQSKLVSD FQFIFLALTQ 310 320 330 340 350 360 LGQDPDAMTD CSAVIPISKP APNNTPGFSF FPPGMTMDDV EQACAETPFP TLSTLPGPAT 370 SVARIPPPPG A

References

[1]	"Analysis of nucleotide sequences of two ligninase cDNAs from a white-rot filamentous fungus, Phanerochaete chrysosporium." de Boer H.A., Zhang Y.Z., Collins C., Reddy C.A. Gene 60:93-102(1987) [PubMed: 3440521] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic organization of lignin peroxidase genes of Phanerochaete chrysosporium." Gaskell J., Dieperink E., Cullen D. Nucleic Acids Res. 19:599-603(1991) [PubMed: 2011531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[3]	"Cloning of several lignin peroxidase (LIP)-encoding genes: sequence analysis of the LIP6 gene from the white-rot basidiomycete, Phanerochaete chrysosporium." Zhang Y.Z., Reddy C.A., Rasooly A. Gene 97:191-198(1991) [PubMed: 1999283] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M18794 mRNA. Translation: AAA33734.1. X55343 Genomic DNA. Translation: CAA39033.1. M63496 Genomic DNA. Translation: AAA33739.1.
PIR	OPJGG5. JN0117.
3D structure databases
HSSP	HSSP built from PDB template 1B85 based on UniProtKB P06181.
SMR	P11543. Positions 24-371.
ModBase	Search...
Protein family/group databases
PeroxiBase	2411. PcLiPC.
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...

Entry information

Entry name

LIG5_PHACH

Accession

Primary (citable) accession number: P11543

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)