NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767;
DOI=10.1093/nar/18.23.7173; PubMed=2129560 [NCBI, ExPASy, EBI, Israel, Japan]
Naidu P.S., Reddy C.A.;
"Nucleotide sequence of a new lignin peroxidase gene GLG3 from the white-rot fungus, Phanerochaete chrysosporium.";
Nucleic Acids Res. 18:7173-7173(1990).

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).
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

X51590; CAA35939.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32322; A32322.
B32322; B32322.
PS0010; PS0010.
S13723; OPJG3P.
S69246; S69246.

3D structure databases

HSSP

P06181; 1B80. [HSSP ENTRY / PDB]

SMR

P21764; 24-372.

ModBase

P21764.

Protein family/group databases

PeroxiBase

2482; PcLiPI.

Ontologies

GO:0016690;	Molecular function: diarylpropane peroxidase activity (inferred from electronic annotation from EC).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0046274;	Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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

ProtoNet

P21764.

Other

UniRef

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

Keywords

Cleavage on pair of basic residues; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 28`	`7`		`PRO_0000023764`
`CHAIN`	`29 372`	`344`	`Ligninase LG3.`	`PRO_0000023765`
`ACT_SITE`	`75 75`		`Proton acceptor (By similarity).`
`METAL`	`76 76`		`Calcium 1 (By similarity).`
`METAL`	`94 94`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`96 96`		`Calcium 1 (By similarity).`
`METAL`	`98 98`		`Calcium 1 (By similarity).`
`METAL`	`204 204`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`205 205`		`Calcium 2 (By similarity).`
`METAL`	`222 222`		`Calcium 2 (By similarity).`
`METAL`	`224 224`		`Calcium 2 (By similarity).`
`METAL`	`227 227`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`229 229`		`Calcium 2 (By similarity).`
`SITE`	`71 71`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`285 285`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 43`		`By similarity.`
`DISULFID`	`62 148`		`By similarity.`
`DISULFID`	`277 345`		`By similarity.`

Sequence information

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

Molecular weight: 39536 Da [This is the MW of the unprocessed precursor]

CRC64: DA0293178F4E2A4A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKQLFAAI SLALSLSAAN AAAVIEKRAT CSNGKTVGDA SSCAWFDVLD DIQQNLFHGG 

        70         80         90        100        110        120 
QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK 

       130        140        150        160        170        180 
LQKPFVQKHG CTPGDFIAFA GAVALSNCPG APQMNFFTGR APATQAAPDG 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

P21764 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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