Reviewed, UniProtKB/Swiss-Prot Q02567 (PEM1_PHACH)

Names and origin

Protein names

Recommended name:
    Peroxidase manganese-dependent 1
    EC=1.11.1.13
Alternative name(s):
    Peroxidase manganese-dependent I
    Manganese peroxidase isozyme 1
      Short name=MnP-1
      Short name=MnP1

Gene names

Name:

MNP1

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	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted.
Induction	During wound-healing and by factors which induce suberization.
Sequence similarities	Belongs to the peroxidase family. Ligninase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide Lignin degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Manganese Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
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
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 378

357

Peroxidase manganese-dependent 1

PRO_0000023778

Sites

Active site

67

1

Proton acceptor

Metal binding

56

1

Manganese

Metal binding

60

1

Manganese

Metal binding

68

1

Calcium 1

Metal binding

83

1

Calcium 1; via carbonyl oxygen

Metal binding

85

1

Calcium 1

Metal binding

87

1

Calcium 1

Metal binding

194

1

Iron (heme axial ligand)

Metal binding

195

1

Calcium 2

Metal binding

200

1

Manganese

Metal binding

212

1

Calcium 2

Metal binding

214

1

Calcium 2

Metal binding

217

1

Calcium 2; via carbonyl oxygen

Metal binding

219

1

Calcium 2

Site

63

1

Transition state stabilizer

Amino acid modifications

Glycosylation

97

1

N-linked (GlcNAc...) Potential

Glycosylation

152

1

N-linked (GlcNAc...)

Glycosylation

238

1

N-linked (GlcNAc...) Potential

Disulfide bond

24 ↔ 36

Disulfide bond

35 ↔ 310

Disulfide bond

54 ↔ 138

Disulfide bond

274 ↔ 340

Disulfide bond

362 ↔ 369

Experimental info

Sequence conflict

75

1

S → L in AAA33742. Ref.2

Secondary structure

1

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378

Helix Strand Turn

Details...

Helix

33 – 37

5

Helix

38 – 48

11

Turn

49 – 52

4

Beta strand

53 – 55

3

Helix

56 – 70

15

Turn

74 – 76

3

Helix

78 – 80

3

Beta 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

Beta strand

198 – 203

6

Beta 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

Beta strand

307 – 309

3

Helix

311 – 313

3

Helix

333 – 335

3

Sequences

	Sequence		Length	Mass (Da)
	Q02567-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 17A9A8F642441F27	FASTA	378	39,557
	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

References

[1]	"Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium." Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H. Gene 93:119-124(1990) [PubMed: 2227420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 201542 / OGC101.
[2]	"Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium." Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H. J. Biol. Chem. 264:5036-5040(1989) [PubMed: 2925681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41. Strain: ATCC 201542 / OGC101.
[3]	"Characterization of manganese(II) binding site mutants of manganese peroxidase." Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M., Gold M.H. Biochemistry 35:8986-8994(1996) [PubMed: 8688436] [Abstract] Cited for: METAL-BINDING.
[4]	"The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution." Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L. J. Biol. Chem. 269:32759-32767(1994) [PubMed: 7806497] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
[5]	"Crystal structures of substrate binding site mutants of manganese peroxidase." Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L. J. Biol. Chem. 272:17574-17580(1997) [PubMed: 9211904] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M60672 Genomic DNA. Translation: AAA33744.1.
M77513 Genomic DNA. Translation: AAA33743.1.
J04624 mRNA. Translation: AAA33742.1.

PIR

A33271. JN0092.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MN1	X-ray	2.00	A	22-378	[»]
1MN2	X-ray	2.00	A	22-378	[»]
1MNP	X-ray	2.00	A	22-378	[»]
1YYD	X-ray	1.45	A	22-378	[»]
1YYG	X-ray	1.60	A	22-378	[»]
1YZP	X-ray	1.60	A	22-378	[»]
1YZR	X-ray	1.60	A	22-378	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3866. PcMnP01_OGC101.

Family and domain databases

InterPro

IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
[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...

Other Resources

LinkHub

Q02567.

Entry information

Entry name

PEM1_PHACH

Accession

Primary (citable) accession number: Q02567
Secondary accession number(s): Q01788

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)