NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-45, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISULFIDE BONDS.
STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767;
PubMed=2760033 [NCBI, ExPASy, EBI, Israel, Japan]
Pease E.A., Andrawis A., Tien M.;
"Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from cDNA sequence.";
J. Biol. Chem. 264:13531-13535(1989).

[2]

PROTEIN SEQUENCE OF 25-44.
PubMed=1592808 [NCBI, ExPASy, EBI, Israel, Japan]
Pease E.A., Tien M.;
"Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium.";
J. Bacteriol. 174:3532-3540(1992).

Comments

FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.
CATALYTIC ACTIVITY: 2 Mn²⁺ + 2 H⁺ + H₂O₂ = 2 Mn³⁺ + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
COFACTOR: Binds 2 calcium ions per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted.
INDUCTION: During wound-healing and by factors which induce suberization.
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

J04980; AAA33746.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32630; A32630.

3D structure databases

HSSP

Q02567; 1MN1. [HSSP ENTRY / PDB]

SMR

P19136; 25-382.

ModBase

P19136.

Protein family/group databases

PeroxiBase

2383; PcMnP02_ATCC24725.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016689;	Molecular function: manganese peroxidase activity (inferred from electronic annotation from EC).
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).

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 382`	`358`	`Peroxidase manganese-dependent H4.`	`PRO_0000023780`
`ACT_SITE`	`70 70`		`Proton acceptor (By similarity).`
`METAL`	`59 59`		`Manganese (By similarity).`
`METAL`	`63 63`		`Manganese (By similarity).`
`METAL`	`71 71`		`Calcium 1 (By similarity).`
`METAL`	`86 86`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`88 88`		`Calcium 1 (By similarity).`
`METAL`	`90 90`		`Calcium 1 (By similarity).`
`METAL`	`197 197`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`198 198`		`Calcium 2 (By similarity).`
`METAL`	`203 203`		`Manganese (By similarity).`
`METAL`	`215 215`		`Calcium 2 (By similarity).`
`METAL`	`217 217`		`Calcium 2 (By similarity).`
`METAL`	`220 220`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`222 222`		`Calcium 2 (By similarity).`
`SITE`	`66 66`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`100 100`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`155 155`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`241 241`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`27 39`
`DISULFID`	`38 313`
`DISULFID`	`57 141`
`DISULFID`	`277 344`
`DISULFID`	`366 373`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 40115 Da [This is the MW of the unprocessed precursor]

CRC64: 75E2A6B762867E3D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFGSLLAFV ALAAITRAAP TAESAVCPDG TRVTNAACCA FIPLAQDLQE TLFQGDCGED 

        70         80         90        100        110        120 
AHEVIRLTFH DAIAISQSLG PQAGGGADGS MLHFPTIEPN FSANSGIDDS VNNLLPFMQK 

       130        140        150        160        170        180 
HDTISAADLV QFAGAVALSN CPGAPRLEFM AGRPNTTIPA VEGLIPEPQD SVTKILQRFE 

       190        200        210        220        230        240 
DAGNFSPFEV VSLLASHTVA RADKVDETID AAPFDSTPFT FDTQVFLEVL LKGTGFPGSN 

       250        260        270        280        290        300 
NNTGEVMSPL PLGSGSDTGE MRLQSDFALA RDERTACFWQ SFVNEQEFMA ASFKAAMAKL 

       310        320        330        340        350        360 
AILGHSRSSL IDCSDVVPVP KPAVNKPATF PATKGPKDLD TLTCKALKFP TLTSDPGATE 

       370        380 
TLIPHCSNGG MSCPGVQFDG PA

P19136 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