[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 201542 / OGC101; DOI=10.1016/0378-1119(90)90144-G; PubMed=2227420 [NCBI, ExPASy, EBI, Israel, Japan] Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H.; "Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium."; Gene 93:119-124(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-41. STRAIN=ATCC 201542 / OGC101; PubMed=2925681 [NCBI, ExPASy, EBI, Israel, Japan] Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H.; "Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium."; J. Biol. Chem. 264:5036-5040(1989).
[3]	METAL-BINDING. DOI=10.1021/bi960679c; PubMed=8688436 [NCBI, ExPASy, EBI, Israel, Japan] Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M., Gold M.H.; "Characterization of manganese(II) binding site mutants of manganese peroxidase."; Biochemistry 35:8986-8994(1996).
[4]	X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS). PubMed=7806497 [NCBI, ExPASy, EBI, Israel, Japan] Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.; "The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution."; J. Biol. Chem. 269:32759-32767(1994).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS. DOI=10.1074/jbc.272.28.17574; PubMed=9211904 [NCBI, ExPASy, EBI, Israel, Japan] Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.; "Crystal structures of substrate binding site mutants of manganese peroxidase."; J. Biol. Chem. 272:17574-17580(1997).

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 2 calcium ions per subunit.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
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

M60672; AAA33744.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M77513; AAA33743.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04624; AAA33742.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0092; A33271.

3D structure databases

PDB

1MN1; X-ray; 2.00 A; A=22-378.	[ExPASy / RCSB / EBI]
1MN2; X-ray; 2.00 A; A=22-378.	[ExPASy / RCSB / EBI]
1MNP; X-ray; 2.00 A; A=22-378.	[ExPASy / RCSB / EBI]
1YYD; X-ray; 1.45 A; A=22-378.	[ExPASy / RCSB / EBI]
1YYG; X-ray; 1.60 A; A=22-378.	[ExPASy / RCSB / EBI]
1YZP; X-ray; 1.60 A; A=22-378.	[ExPASy / RCSB / EBI]
1YZR; X-ray; 1.60 A; A=22-378.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MN1; -.
1MN2; -.
1MNP; -.
1YYD; -.
1YYG; -.
1YZP; -.
1YZR; -.

ModBase

Q02567.

Protein family/group databases

PeroxiBase

3866; PcMnP01_OGC101.

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: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: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

Q02567; -.

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

Keywords

3D-structure; 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 21`	`21`
`CHAIN`	`22 378`	`357`	`Peroxidase manganese-dependent 1.`	`PRO_0000023778`
`ACT_SITE`	`67 67`		`Proton acceptor.`
`METAL`	`56 56`		`Manganese.`
`METAL`	`60 60`		`Manganese.`
`METAL`	`68 68`		`Calcium 1.`
`METAL`	`83 83`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`85 85`		`Calcium 1.`
`METAL`	`87 87`		`Calcium 1.`
`METAL`	`194 194`		`Iron (heme axial ligand).`
`METAL`	`195 195`		`Calcium 2.`
`METAL`	`200 200`		`Manganese.`
`METAL`	`212 212`		`Calcium 2.`
`METAL`	`214 214`		`Calcium 2.`
`METAL`	`217 217`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`219 219`		`Calcium 2.`
`SITE`	`63 63`	`1`	`Transition state stabilizer.`
`CARBOHYD`	`97 97`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`152 152`		`N-linked (GlcNAc...).`
`CARBOHYD`	`238 238`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`24 36`
`DISULFID`	`35 310`
`DISULFID`	`54 138`
`DISULFID`	`274 340`
`DISULFID`	`362 369`
`CONFLICT`	`75 75`		`S -> L (in Ref. 2; AAA33742).`
`HELIX`	`33 37`	`5`
`HELIX`	`38 48`	`11`
`TURN`	`49 52`	`4`
`STRAND`	`53 55`	`3`
`HELIX`	`56 70`	`15`
`TURN`	`74 76`	`3`
`HELIX`	`78 80`	`3`
`STRAND`	`83 85`	`3`
`HELIX`	`87 90`	`4`
`TURN`	`92 94`	`3`
`HELIX`	`95 97`	`3`
`HELIX`	`99 101`	`3`
`TURN`	`102 104`	`3`
`HELIX`	`105 117`	`13`
`HELIX`	`123 136`	`14`
`HELIX`	`169 180`	`12`
`HELIX`	`184 190`	`7`
`HELIX`	`191 196`	`6`
`STRAND`	`198 203`	`6`
`STRAND`	`209 213`	`5`
`HELIX`	`221 226`	`6`
`HELIX`	`261 268`	`8`
`TURN`	`270 272`	`3`
`HELIX`	`273 278`	`6`
`TURN`	`279 281`	`3`
`HELIX`	`283 297`	`15`
`TURN`	`298 301`	`4`
`HELIX`	`304 306`	`3`
`STRAND`	`307 309`	`3`
`HELIX`	`311 313`	`3`
`HELIX`	`333 335`	`3`

Sequence information

Length: 378 AA [This is the length of the unprocessed precursor]

Molecular weight: 39557 Da [This is the MW of the unprocessed precursor]

CRC64: 17A9A8F642441F27 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKSLIAFV ALAAAVRAAP TAVCPDGTRV SHAACCAFIP LAQDLQETIF QNECGEDAHE 

        70         80         90        100        110        120 
VIRLTFHDAI AISRSQGPKA GGGADGSMLL FPTVEPNFSA NNGIDDSVNN LIPFMQKHNT 

       130        140        150        160        170        180 
ISAADLVQFA GAVALSNCPG APRLEFLAGR PNKTIAAVDG LIPEPQDSVT KILQRFEDAG 

       190        200        210        220        230        240 
GFTPFEVVSL LASHSVARAD KVDQTIDAAP FDSTPFTFDT QVFLEVLLKG VGFPGSANNT 

       250        260        270        280        290        300 
GEVASPLPLG SGSDTGEMRL QSDFALAHDP RTACIWQGFV NEQAFMAASF RAAMSKLAVL 

       310        320        330        340        350        360 
GHNRNSLIDC SDVVPVPKPA TGQPAMFPAS TGPQDLELSC PSERFPTLTT QPGASQSLIA 

       370 
HCPDGSMSCP GVQFNGPA

Q02567 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