P28313 (PER_ARTRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Peroxidase EC=1.11.1.7
Organism	Arthromyces ramosus
Taxonomic identifier	5451 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Tricholomataceae › Arthromyces

Protein attributes

Sequence length	364 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 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 – 364

344

Peroxidase

PRO_0000023666

Sites

Active site

76

1

Proton acceptor

Metal binding

77

1

Calcium 1

Metal binding

95

1

Calcium 1; via carbonyl oxygen

Metal binding

97

1

Calcium 1

Metal binding

99

1

Calcium 1

Metal binding

204

1

Iron (heme axial ligand)

Metal binding

205

1

Calcium 2

Metal binding

222

1

Calcium 2

Metal binding

224

1

Calcium 2

Metal binding

227

1

Calcium 2; via carbonyl oxygen

Metal binding

229

1

Calcium 2

Site

72

1

Transition state stabilizer

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid

Glycosylation

163

1

N-linked (GlcNAc...) (high mannose) Ref.2

Disulfide bond

32 ↔ 44

Disulfide bond

43 ↔ 313

Disulfide bond

63 ↔ 149

Disulfide bond

277 ↔ 342

Secondary structure

1

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364

Helix Strand Turn

Details...

Beta strand

37 – 39

3

Helix

41 – 43

3

Helix

44 – 55

12

Turn

56 – 61

6

Helix

65 – 78

14

Helix

83 – 87

5

Beta strand

95 – 98

4

Helix

99 – 102

4

Helix

104 – 107

4

Helix

111 – 113

3

Helix

117 – 130

14

Helix

134 – 147

14

Helix

180 – 190

11

Helix

194 – 200

7

Helix

201 – 205

5

Beta strand

208 – 212

5

Beta strand

219 – 223

5

Helix

231 – 236

6

Beta strand

245 – 247

3

Beta strand

255 – 257

3

Helix

264 – 271

8

Turn

273 – 275

3

Helix

276 – 281

6

Turn

282 – 284

3

Helix

286 – 300

15

Turn

301 – 304

4

Helix

307 – 309

3

Beta strand

310 – 312

3

Helix

314 – 316

3

Helix

335 – 337

3

Sequences

	Sequence		Length	Mass (Da)
	P28313 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 08C3BB42B9695D88	FASTA	364	37,746
	10 20 30 40 50 60 MKLSLFSTFA AVIIGALALP QGPGGGGGSV TCPGGQSTSN SQCCVWFDVL DDLQTNFYQG 70 80 90 100 110 120 SKCESPVRKI LRIVFHDAIG FSPALTAAGQ FGGGGADGSI IAHSNIELAF PANGGLTDTI 130 140 150 160 170 180 EALRAVGINH GVSFGDLIQF ATAVGMSNCP GSPRLEFLTG RSNSSQPSPP SLIPGPGNTV 190 200 210 220 230 240 TAILDRMGDA GFSPDEVVDL LAAHSLASQE GLNSAIFRSP LDSTPQVFDT QFYIETLLKG 250 260 270 280 290 300 TTQPGPSLGF AEELSPFPGE FRMRSDALLA RDSRTACRWQ SMTSSNEVMG QRYRAAMAKM 310 320 330 340 350 360 SVLGFDRNAL TDCSDVIPSA VSNNAAPVIP GGLTVDDIEV SCPSEPFPEI ATASGPLPSL APAP

References

[1]	"Cloning, sequencing, and heterologous expression of a gene coding for Arthromyces ramosus peroxidase." Sawai-Hatanaka H., Ashikari T., Tanaka Y., Asada Y., Nakayama T., Minakata H., Kunishima N., Fukuyama K., Yamada H., Shibano Y., Amachi T. Biosci. Biotechnol. Biochem. 59:1221-1228(1995) [PubMed: 7670182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 1576150] [Abstract] Cited for: PROTEIN SEQUENCE OF 162-186, GLYCOSYLATION AT ASN-163.
[3]	"Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9-A resolution. Structural comparisons with the lignin and cytochrome c peroxidases." Kunishima N., Fukuyama K., Matsubara H., Hatanaka H., Shibano Y., Amachi T. J. Mol. Biol. 235:331-344(1994) [PubMed: 8289254] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[4]	"Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6-A resolution." Itakura H., Oda Y., Fukuyama K. FEBS Lett. 412:107-110(1997) [PubMed: 9257700] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[5]	"Binding of salicylhydroxamic acid and several aromatic donor molecules to Arthromyces ramosus peroxidase, investigated by X-ray crystallography, optical difference spectroscopy, NMR relaxation, molecular dynamics, and kinetics." Tsukamoto K., Itakura H., Sato K., Fukuyama K., Miura S., Takahashi S., Ikezawa H., Hosoya T. Biochemistry 38:12558-12568(1999) [PubMed: 10504224] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 36-350.
[6]	"Direct binding of hydroxylamine to the heme iron of Arthromyces ramosus peroxidase. Substrate analogue that inhibits compound I formation in a competetive manner." Wariishi H., Nonaka D., Johjima T., Nakamura N., Naruta Y., Kubo S., Fukuyama K. J. Biol. Chem. 275:32919-32924(2000) [PubMed: 10915789] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-364.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D63792 mRNA. Translation: BAA09861.1.

PIR

S22221.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ARP	X-ray	1.90	A	21-364	[»]
1ARU	X-ray	1.60	A	21-364	[»]
1ARV	X-ray	1.60	A	21-364	[»]
1ARW	X-ray	1.60	A	21-364	[»]
1ARX	X-ray	1.90	A	21-364	[»]
1ARY	X-ray	1.90	A	21-364	[»]
1C8I	X-ray	2.00	A	21-364	[»]
1CK6	X-ray	1.90	A	21-364	[»]
1GZA	X-ray	2.06	A	21-364	[»]
1GZB	X-ray	1.80	A	21-364	[»]
1HSR	X-ray	1.60	A	21-364	[»]
2E39	X-ray	1.30	A	21-364	[»]
2E3A	X-ray	1.30	A	21-364	[»]
2E3B	X-ray	1.30	A	21-364	[»]

ProteinModelPortal

P28313.

SMR

P28313. Positions 29-364.

ModBase

Search...

Protein family/group databases

PeroxiBase

2404. ArCII.

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...

Entry information

Entry name

PER_ARTRA

Accession

Primary (citable) accession number: P28313

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 1, 1996
Last modified:	October 19, 2011
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program