P28314 (PER_COPCI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxidase
EC=1.11.1.7

Gene names

Name:

CIP1

Organism

Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)

Taxonomic identifier

5346 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Psathyrellaceae › Coprinopsis

Protein attributes

Sequence length	363 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)

Catalytic activity	2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peroxidase family. Ligninase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 363

343

Peroxidase

PRO_0000023667

Sites

Active site

75

1

Proton acceptor

Metal binding

76

1

Calcium 1

Metal binding

94

1

Calcium 1; via carbonyl oxygen

Metal binding

96

1

Calcium 1

Metal binding

98

1

Calcium 1

Metal binding

203

1

Iron (heme axial ligand)

Metal binding

204

1

Calcium 2

Metal binding

221

1

Calcium 2

Metal binding

223

1

Calcium 2

Metal binding

226

1

Calcium 2; via carbonyl oxygen

Metal binding

228

1

Calcium 2

Site

71

1

Transition state stabilizer

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid

Glycosylation

162

1

N-linked (GlcNAc...) (high mannose) Ref.4

Glycosylation

358

1

O-linked (Man...) Ref.4

Disulfide bond

31 ↔ 43

Disulfide bond

42 ↔ 312

Disulfide bond

62 ↔ 148

Disulfide bond

276 ↔ 341

Natural variations

Natural variant

99

1

I → V.

Experimental info

Sequence conflict

119

1

V → I in CAA50060. Ref.2

Secondary structure

1

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363

Helix Strand Turn

Details...

Beta strand

36 – 39

4

Helix

40 – 42

3

Helix

45 – 54

10

Turn

55 – 60

6

Helix

64 – 77

14

Helix

82 – 86

5

Beta strand

94 – 96

3

Helix

98 – 101

4

Helix

103 – 106

4

Helix

110 – 112

3

Helix

116 – 129

14

Helix

133 – 146

14

Helix

179 – 189

11

Helix

193 – 199

7

Helix

200 – 205

6

Beta strand

207 – 211

5

Helix

213 – 215

3

Beta strand

218 – 222

5

Helix

230 – 235

6

Beta strand

244 – 246

3

Beta strand

254 – 256

3

Helix

263 – 270

8

Turn

272 – 274

3

Helix

275 – 280

6

Helix

285 – 300

16

Turn

301 – 303

3

Helix

306 – 308

3

Beta strand

309 – 311

3

Helix

313 – 315

3

Helix

334 – 336

3

Beta strand

342 – 344

3

Sequences

	Sequence		Length	Mass (Da)
	P28314 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: E56EB53B963C3DB5	FASTA	363	37,640
	10 20 30 40 50 60 MKLSLLSTFA AVIIGALALP QGPGGGGSVT CPGGQSTSNS QCCVWFDVLD DLQTNFYQGS 70 80 90 100 110 120 KCESPVRKIL RIVFHDAIGF SPALTAAGQF GGGGADGSII AHSNIELAFP ANGGLTDTVE 130 140 150 160 170 180 ALRAVGINHG VSFGDLIQFA TAVGMSNCPG SPRLEFLTGR SNSSQPSPPS LIPGPGNTVT 190 200 210 220 230 240 AILDRMGDAG FSPDEVVDLL AAHSLASQEG LNSAIFRSPL DSTPQVFDTQ FYIETLLKGT 250 260 270 280 290 300 TQPGPSLGFA EELSPFPGEF RMRSDALLAR DSRTACRWQS MTSSNEVMGQ RYRAAMAKMS 310 320 330 340 350 360 VLGFDRNALT DCSDVIPSAV SNNAAPVIPG GLTVDDIEVS CPSEPFPEIA TASGPLPSLA PAP

References

[1]	"Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence encoding Coprinus cinereus peroxidase. A new family of fungal peroxidases." Baunsgaard L., Dalboege H., Houen G., Rasmussen E.M., Welinder K.G. Eur. J. Biochem. 213:605-611(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: NBRC 8371.
[2]	Dalboege H. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NBRC 8371.
[3]	"Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus." Kjalke M., Andersen M.B., Schneider P., Christensen B., Schuelein M., Welinder K.G. Biochim. Biophys. Acta 1120:248-256(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 161-185.
[4]	"Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6-A resolution." Petersen J.F.W., Kadziola A., Larsen S. FEBS Lett. 339:291-296(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), GLYCOSYLATION AT ASN-162 AND SER-358.
[5]	"Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase." Houborg K., Harris P., Petersen J., Rowland P., Poulsen J.-C.N., Schneider P., Vind J., Larsen S. Acta Crystallogr. D 59:989-996(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS).
[6]	"The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability." Houborg K., Harris P., Poulsen J.-C.N., Schneider P., Svendsen A., Larsen S. Acta Crystallogr. D 59:997-1003(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT.
[7]	"The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H-NMR spectroscopy and comparison with the wild-type enzyme." Veitch N.C., Gao Y., Welinder K.G. Biochemistry 35:14370-14380(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT ASN-265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X69457 mRNA. Translation: CAA49216.1.
X70789 Genomic DNA. Translation: CAA50060.1.

PIR

S31780.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H3J	X-ray	2.00	A/B	22-363	[»]
1LY8	X-ray	2.05	A/B	21-363	[»]
1LY9	X-ray	2.00	A/B	21-363	[»]
1LYC	X-ray	1.57	A/B	21-363	[»]
1LYK	X-ray	2.00	A/B	21-363	[»]

ProteinModelPortal

P28314.

SMR

P28314. Positions 28-363.

ModBase

Search...

Protein family/group databases

mycoCLAP

PRXA_COPCI.

PeroxiBase

2403. CcinCIIBA.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Pfam

PF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00462. LIGNINASE.
PR00458. PEROXIDASE.

SUPFAM

SSF48113. Peroxidase_super. 1 hit.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P28314.

Entry information

Entry name

PER_COPCI

Accession

Primary (citable) accession number: P28314
Secondary accession number(s): P28315, Q12575

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program