Reviewed, UniProtKB/Swiss-Prot P22195 (PER1_ARAHY)

Names and origin

Protein names

Recommended name:
    Cationic peroxidase 1
    EC=1.11.1.7
Alternative name(s):
    PNPC1

Gene names

Name:

PNC1

Organism

Arachis hypogaea (Peanut)

Taxonomic identifier

3818 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Dalbergieae › Arachis

Protein attributes

Sequence length	316 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	Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase 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
Gene Ontology (GO)
Biological process	hydrogen peroxide 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-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 22

22

Potential

Chain

23 – 316

294

Cationic peroxidase 1

PRO_0000023746

Sites

Active site

64

1

Proton acceptor

Metal binding

65

1

Calcium 1

Metal binding

68

1

Calcium 1; via carbonyl oxygen

Metal binding

70

1

Calcium 1; via carbonyl oxygen

Metal binding

72

1

Calcium 1

Metal binding

74

1

Calcium 1

Metal binding

191

1

Iron (heme axial ligand)

Metal binding

192

1

Calcium 2

Metal binding

236

1

Calcium 2

Metal binding

239

1

Calcium 2

Metal binding

242

1

Calcium 2; via carbonyl oxygen

Metal binding

244

1

Calcium 2

Site

60

1

Transition state stabilizer

Amino acid modifications

Modified residue

23

1

Pyrrolidone carboxylic acid

Glycosylation

82

1

N-linked (GlcNAc...)

Glycosylation

166

1

N-linked (GlcNAc...)

CAR_000185

Disulfide bond

33 ↔ 113

Disulfide bond

66 ↔ 71

Disulfide bond

119 ↔ 312

Disulfide bond

198 ↔ 223

Secondary structure

1

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316

Helix Strand Turn

Details...

Turn

26 – 32

7

Helix

36 – 50

15

Helix

53 – 66

14

Turn

67 – 69

3

Beta strand

70 – 73

4

Helix

74 – 76

3

Turn

90 – 95

6

Helix

99 – 112

14

Turn

114 – 116

3

Helix

119 – 133

15

Helix

153 – 159

7

Helix

167 – 175

9

Turn

176 – 178

3

Helix

181 – 188

8

Helix

189 – 192

4

Beta strand

195 – 197

3

Helix

198 – 207

10

Beta strand

209 – 211

3

Helix

213 – 220

8

Beta strand

225 – 227

3

Beta strand

232 – 235

4

Beta strand

237 – 239

3

Helix

246 – 252

7

Helix

259 – 263

5

Beta strand

265 – 268

4

Helix

271 – 279

9

Helix

281 – 295

15

Beta strand

305 – 307

3

Sequences

	Sequence		Length	Mass (Da)
	P22195-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 2CC271F8E8B8C9F0	FASTA	316	33,518
	10 20 30 40 50 60 MALPISKVDF LIFMCLIGLG SAQLSSNFYA TKCPNALSTI KSAVNSAVAK EARMGASLLR 70 80 90 100 110 120 LHFHDCFVQG CDASVLLDDT SNFTGEKTAG PNANSIRGFE VIDTIKSQVE SLCPGVVSCA 130 140 150 160 170 180 DILAVAARDS VVALGGASWN VLLGRRDSTT ASLSSANSDL PAPFFNLSGL ISAFSNKGFT 190 200 210 220 230 240 TKELVTLSGA HTIGQAQCTA FRTRIYNESN IDPTYAKSLQ ANCPSVGGDT NLSPFDVTTP 250 260 270 280 290 300 NKFDNAYYIN LRNKKGLLHS DQQLFNGVST DSQVTAYSNN AATFNTDFGN AMIKMGNLSP 310 LTGTSGQIRT NCRKTN

References

[1]	"Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells." Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M., Dang Ha D.B., Esnault R. Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(1990) [PubMed: 2247460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Esnault R. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 47.
[3]	"The crystal structure of peanut peroxidase." Schuller D.J., Ban N., van Huystee R.B., McPherson A., Poulos T.L. Structure 4:311-321(1996) [PubMed: 8805539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M37636 mRNA. Translation: AAB06183.1.

PIR

A38265.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SCH	X-ray	2.56	A/B	24-316	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

102. AhPrx04.

PTM databases

GlycoSuiteDB

P22195.

Enzyme and pathway databases

BRENDA

1.11.1.7. 569.

Family and domain databases

InterPro

IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Pfam

PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

PER1_ARAHY

Accession

Primary (citable) accession number: P22195

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 15, 1999
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)