P00433 (PER1A_ARMRU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxidase C1A
EC=1.11.1.7

Gene names

Name:	PRXC1A
Synonyms:	HPRC1

Organism

Armoracia rusticana (Horseradish) (Armoracia laphatifolia)

Taxonomic identifier

3704 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Cardamineae › Armoracia

Protein attributes

Sequence length	353 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	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.
Subunit structure	Monomer.
Subcellular location	Secreted Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted Vacuole
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 vacuole 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 – 30

30

Ref.2

Chain

31 – 338

308

Peroxidase C1A Ref.2

PRO_0000023739

Propeptide

339 – 353

15

PRO_0000023740

Sites

Active site

72

1

Proton acceptor

Metal binding

73

1

Calcium 1

Metal binding

76

1

Calcium 1; via carbonyl oxygen

Metal binding

78

1

Calcium 1; via carbonyl oxygen

Metal binding

80

1

Calcium 1

Metal binding

82

1

Calcium 1

Metal binding

94

1

Calcium 1

Metal binding

200

1

Iron (heme axial ligand)

Metal binding

201

1

Calcium 2

Metal binding

252

1

Calcium 2

Metal binding

255

1

Calcium 2

Metal binding

260

1

Calcium 2

Binding site

169

1

Substrate; via carbonyl oxygen

Site

68

1

Transition state stabilizer

Amino acid modifications

Modified residue

31

1

Pyrrolidone carboxylic acid Ref.2

Glycosylation

43

1

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

Glycosylation

87

1

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

Glycosylation

188

1

N-linked (GlcNAc...)

Glycosylation

216

1

N-linked (GlcNAc...)

Glycosylation

228

1

N-linked (GlcNAc...)

Glycosylation

244

1

N-linked (GlcNAc...)

Glycosylation

285

1

N-linked (GlcNAc...)

Glycosylation

298

1

N-linked (GlcNAc...)

Disulfide bond

41 ↔ 121

Ref.2

Disulfide bond

74 ↔ 79

Ref.2

Disulfide bond

127 ↔ 331

Disulfide bond

207 ↔ 239

Secondary structure

1

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353

Helix Strand Turn

Details...

Turn

34 – 40

7

Helix

44 – 58

15

Helix

62 – 74

13

Turn

75 – 77

3

Beta strand

78 – 81

4

Helix

82 – 84

3

Beta strand

89 – 91

3

Helix

94 – 96

3

Turn

98 – 103

6

Helix

107 – 120

14

Turn

122 – 124

3

Helix

127 – 141

15

Helix

161 – 167

7

Helix

175 – 184

10

Helix

190 – 197

8

Helix

198 – 201

4

Beta strand

204 – 206

3

Helix

207 – 210

4

Helix

211 – 215

5

Helix

217 – 219

3

Beta strand

220 – 222

3

Helix

229 – 238

10

Beta strand

248 – 251

4

Beta strand

253 – 255

3

Helix

262 – 268

7

Helix

275 – 282

8

Turn

284 – 288

5

Helix

289 – 298

10

Helix

300 – 314

15

Beta strand

324 – 326

3

Sequences

	Sequence		Length	Mass (Da)
	P00433 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: AC916C03C4A24D27	FASTA	353	38,825
	10 20 30 40 50 60 MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD TIVNELRSDP 70 80 90 100 110 120 RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVESA 130 140 150 160 170 180 CPRTVSCADL LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LDLANANLPA PFFTLPQLKD 190 200 210 220 230 240 SFRNVGLNRS SDLVALSGGH TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP 250 260 270 280 290 300 LNGNLSALVD FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST 310 320 330 340 350 QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV SSM

References

[1]	"Structure of the horseradish peroxidase isozyme C genes." Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K., Shinmyo A., Takano M., Yamada Y., Okada H. Eur. J. Biochem. 173:681-687(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)." Welinder K.G. FEBS Lett. 72:19-23(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-338.
[3]	"Crystal structure of horseradish peroxidase C at 2.15-A resolution." Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L. Nat. Struct. Biol. 4:1032-1038(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[4]	"Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography." Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., Gajhede M. Biochemistry 37:8054-8060(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	Meno K., White C.G., Smith A.T., Gajhede M. Submitted (DEC-1998) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37156 Genomic DNA. Translation: AAA33377.1.

PIR

OPRHC. S00625.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ATJ	X-ray	2.15	A/B/C/D/E/F	31-336	[»]
1GW2	X-ray	2.15	A	31-338	[»]
1GWO	X-ray	2.07	A	31-338	[»]
1GWT	X-ray	1.70	A	31-338	[»]
1GWU	X-ray	1.31	A	31-338	[»]
1GX2	X-ray	2.20	A/B	31-338	[»]
1H55	X-ray	1.61	A	31-338	[»]
1H57	X-ray	1.60	A	31-338	[»]
1H58	X-ray	1.70	A	31-338	[»]
1H5A	X-ray	1.60	A	31-338	[»]
1H5C	X-ray	1.62	A	31-338	[»]
1H5D	X-ray	1.60	A	31-338	[»]
1H5E	X-ray	1.60	A	31-338	[»]
1H5F	X-ray	1.60	A	31-338	[»]
1H5G	X-ray	1.57	A	31-338	[»]
1H5H	X-ray	1.60	A	31-338	[»]
1H5I	X-ray	1.60	A	31-338	[»]
1H5J	X-ray	1.60	A	31-338	[»]
1H5K	X-ray	1.60	A	31-338	[»]
1H5L	X-ray	1.60	A	31-338	[»]
1H5M	X-ray	1.57	A	31-338	[»]
1HCH	X-ray	1.57	A	31-336	[»]
1KZM	X-ray	2.00	A	31-338	[»]
1W4W	X-ray	1.55	A	31-353	[»]
1W4Y	X-ray	1.60	A	31-353	[»]
2ATJ	X-ray	2.00	A/B	31-337	[»]
2YLJ	X-ray	1.69	A	31-336	[»]
3ATJ	X-ray	2.20	A/B	31-338	[»]
4ATJ	X-ray	2.50	A/B	31-338	[»]
6ATJ	X-ray	2.00	A	31-338	[»]
7ATJ	X-ray	1.47	A	31-338	[»]

ProteinModelPortal

P00433.

SMR

P00433. Positions 31-337.

ModBase

Search...

Protein family/group databases

PeroxiBase

90. AruPrx01-1.

PTM databases

GlycoSuiteDB

P00433.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P00433.

Family and domain databases

InterPro

IPR010255. Haem_peroxidase.
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.

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

P00433.

Entry information

Entry name

PER1A_ARMRU

Accession

Primary (citable) accession number: P00433

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program