[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PRL 572; DOI=10.1016/0300-9084(92)90043-E; PubMed=1581393 [NCBI, ExPASy, EBI, Israel, Japan] Joensson L.J., Nyman P.O.; "Characterization of a lignin peroxidase gene from the white-rot fungus Trametes versicolor."; Biochimie 74:177-182(1992).
[2]	PROTEIN SEQUENCE OF 27-38. DOI=10.1016/0014-5793(89)81258-X; PubMed=2707445 [NCBI, ExPASy, EBI, Israel, Japan] Joensson L.J., Karlsson O., Lundquist K., Nyman P.O.; "Trametes versicolor ligninase: isozyme sequence homology and substrate specificity."; FEBS Lett. 247:143-146(1989).

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 2 calcium ions per subunit (By similarity).
PATHWAY: Secondary metabolite metabolism; lignin degradation .
DEVELOPMENTAL STAGE: Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.
SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M64993; AAA34049.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S32581; S32581.

3D structure databases

HSSP

P11542; 1QPA. [HSSP ENTRY / PDB]

ModBase

P20013.

Protein family/group databases

PeroxiBase

2420; TvLiP.

Family and domain databases

InterPro

IPR002016; Haem_peroxidase_pln/fun/bac.
IPR001621; Ligninase.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00462; LIGNINASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; FALSE_NEG.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`
`CHAIN`	`27 372`	`346`	`Ligninase C.`	`PRO_0000023777`
`ACT_SITE`	`74 74`		`Proton acceptor (By similarity).`
`METAL`	`75 75`		`Calcium 1 (By similarity).`
`METAL`	`93 93`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`95 95`		`Calcium 1 (By similarity).`
`METAL`	`97 97`		`Calcium 1 (By similarity).`
`METAL`	`205 205`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`206 206`		`Calcium 2 (By similarity).`
`METAL`	`223 223`		`Calcium 2 (By similarity).`
`METAL`	`225 225`		`Calcium 2 (By similarity).`
`METAL`	`228 228`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`230 230`		`Calcium 2 (By similarity).`
`SITE`	`70 70`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`129 129`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 39625 Da [This is the MW of the unprocessed precursor]

CRC64: 9F7A06AABAA9B25A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKSLLSFV SVIGALQGAN AALTRRVACP DGVNTATNAA CCQLFAVRED LQQNLFHGGL 

        70         80         90        100        110        120 
CTAEAHESLR LTFHDAIAIS PALEAQGIFG GGGADGSIAI FPEIETNFHP NIGLDEIIEL 

       130        140        150        160        170        180 
QKPFIARHNI SVADFIQFAG AIGASNCAGA PQLAAFVGRK DATQPAPDGL VPEPFHTPDQ 

       190        200        210        220        230        240 
IFDRLADASQ GEFDPILTVW LLTAHTVAAA NDVDPTKSGL PFDSTPELWD TQFFLETQLR 

       250        260        270        280        290        300 
GTSFPGSGGN QGEVESPLAG EMRLQSDHTI ARDSRTACEW QSFVDNQPKA QQMFQFVFHD 

       310        320        330        340        350        360 
LSIFGQDINT LVDCTEVVPI PADPQGHTHF PAGLSNADIE QACAETPFPT FPTDPGPKTA 

       370 
VAPVPKPPAA RK

P20013 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools