Reviewed, UniProtKB/Swiss-Prot P31837 (LIGA_PHACH)

Names and origin

Protein names

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

Gene names

Name:	LIPA
Synonyms:	LPOB

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	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 + H2O2 = 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. 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 Disulfide bond 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
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	Potential		PRO_0000023772
	Chain	29 – 372	344	Ligninase A		PRO_0000023773
Sites
	Active site	75	1	Proton acceptor By similarity
	Metal binding	76	1	Calcium 1 By similarity
	Metal binding	94	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	96	1	Calcium 1 By similarity
	Metal binding	98	1	Calcium 1 By similarity
	Metal binding	204	1	Iron (heme axial ligand) By similarity
	Metal binding	205	1	Calcium 2 By similarity
	Metal binding	222	1	Calcium 2 By similarity
	Metal binding	224	1	Calcium 2 By similarity
	Metal binding	227	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	229	1	Calcium 2 By similarity
	Site	71	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 43		By similarity
	Disulfide bond	42 ↔ 313		By similarity
	Disulfide bond	62 ↔ 148		By similarity
	Disulfide bond	277 ↔ 345		By similarity
Experimental info
	Sequence conflict	135	1	A → D in AAA33741. Ref.2
	Sequence conflict	161	1	A → R in AAA33741. Ref.2
	Sequence conflict	298	1	L → H in AAA33741. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31837-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 04CE4598D6D6F09B	FASTA	372	39,394
	10 20 30 40 50 60 MAFKQLVAAI SLALSLTTAN AAVVKEKRAT CSNGATVGDA SCCAWFDVLD DIQQNLFQGG 70 80 90 100 110 120 QCGAEAHESI RLVFHDAIAI SPAMEAQGKF GGGGADGSIM IFDDIEPNFH PNIGLDEIIN 130 140 150 160 170 180 LQKPFVQKHG VTPGAFIAFA GAVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD 190 200 210 220 230 240 QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG 250 260 270 280 290 300 ILFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL 310 320 330 340 350 360 TQLGQDPNAM TDCSDVIPIS KPIPGNLPFS FFPPGKSMKD VEQACAETPF PSLVTLPGPA 370 TSVARIPPPP GA

References

[1]	"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.
[2]	"Characterization of lignin peroxidase-encoding genes from lignin-degrading basidiomycetes." Huoponen K., Ollikka P., Kaelin M., Walther I., Maentsaelae P., Reiser J. Gene 89:145-150(1990) [PubMed: 2373364] [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	X54257 Genomic DNA. Translation: CAA38177.1. M37701 Genomic DNA. Translation: AAA33741.1.
PIR	JH0156. PS0011. OPJGAP. S13563.
3D structure databases
HSSP	HSSP built from PDB template 1LLP based on UniProtKB P49012.
SMR	P31837. Positions 24-372.
ModBase	Search...
Protein family/group databases
PeroxiBase	2413. PcLiPB.
Enzyme and pathway databases
BRENDA	1.11.1.14. 16698.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR001621. Ligninase. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [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

LIGA_PHACH

Accession

Primary (citable) accession number: P31837

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 5, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)