Reviewed, UniProtKB/Swiss-Prot Q42578 (PER53_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 53
      Short name=Atperox P53
    EC=1.11.1.7
Alternative name(s):
    ATPA2

Gene names

Name:	PER53
Synonyms:	P53
Ordered Locus Names:	At5g06720
ORF Names:	MPH15.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	335 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 H(2)O(2), 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. Closely linked to lignin formation by showing monolignol substrate specificity.
Catalytic activity	Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	SecretedBy similarity.
Tissue specificity	Mainly expressed in roots.
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
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	Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome
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-KW
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 335

305

Peroxidase 53

PRO_0000023718

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

199

1

Iron (heme axial ligand) By similarity

Metal binding

200

1

Calcium 2

Metal binding

251

1

Calcium 2

Metal binding

254

1

Calcium 2

Metal binding

259

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

Glycosylation

33

1

N-linked (GlcNAc...) Potential

Glycosylation

43

1

N-linked (GlcNAc...) Potential

Glycosylation

165

1

N-linked (GlcNAc...) Potential

Glycosylation

177

1

N-linked (GlcNAc...) Potential

Glycosylation

215

1

N-linked (GlcNAc...) Potential

Glycosylation

227

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Glycosylation

297

1

N-linked (GlcNAc...) Potential

Disulfide bond

41 ↔ 121

By similarity

Disulfide bond

74 ↔ 79

By similarity

Disulfide bond

127 ↔ 329

By similarity

Disulfide bond

206 ↔ 238

By similarity

Experimental info

Sequence conflict

21

1

V → L in AAM65211. Ref.4

Sequence conflict

172

1

I → V in AAM65211. Ref.4

Sequence conflict

180

1

F → S in AAM65211. Ref.4

Sequence conflict

270

1

D → N in AAM65211. Ref.4

Secondary structure

1

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335

Helix Strand Turn

Details...

Turn

34 – 40

7

Helix

44 – 56

13

Helix

62 – 74

13

Turn

75 – 77

3

Beta strand

78 – 81

4

Helix

82 – 84

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

189 – 196

8

Helix

197 – 200

4

Beta strand

201 – 205

5

Helix

206 – 208

3

Helix

210 – 212

3

Helix

216 – 218

3

Beta strand

219 – 221

3

Helix

228 – 237

10

Beta strand

247 – 250

4

Beta strand

252 – 257

6

Helix

261 – 267

7

Helix

274 – 281

8

Helix

287 – 296

10

Helix

298 – 313

16

Beta strand

322 – 324

3

Sequences

	Sequence		Length	Mass (Da)
	Q42578-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 57E375B212F1BC6B	FASTA	335	34,989
	10 20 30 40 50 60 MAVTNLPTCD GLFIISLIVI VSSIFGTSSA QLNATFYSGT CPNASAIVRS TIQQALQSDT 70 80 90 100 110 120 RIGASLIRLH FHDCFVNGCD ASILLDDTGS IQSEKNAGPN VNSARGFNVV DNIKTALENA 130 140 150 160 170 180 CPGVVSCSDV LALASEASVS LAGGPSWTVL LGRRDSLTAN LAGANSSIPS PIESLSNITF 190 200 210 220 230 240 KFSAVGLNTN DLVALSGAHT FGRARCGVFN NRLFNFSGTG NPDPTLNSTL LSTLQQLCPQ 250 260 270 280 290 300 NGSASTITNL DLSTPDAFDN NYFANLQSND GLLQSDQELF STTGSSTIAI VTSFASNQTL 310 320 330 FFQAFAQSMI NMGNISPLTG SNGEIRLDCK KVNGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture." Oestergaard L., Abelskov A.K., Mattsson O., Welinder K.G. FEBS Lett. 398:243-247(1996) [PubMed: 8977116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Computational analyses and annotations of the Arabidopsis peroxidase gene family." Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G. FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract] Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[6]	"Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification." Oestergaard L., Teilum K., Mirza O., Mattsson O., Petersen M., Welinder K.G., Mundy J., Gajhede M., Henriksen A. Plant Mol. Biol. 44:231-243(2000) [PubMed: 11117266] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). Strain: cv. Columbia.
[7]	"Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2." Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M., Smulevich G., Welinder K.G. Biochemistry 40:11013-11021(2001) [PubMed: 11551197] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). Strain: cv. Columbia.
[8]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X99952 mRNA. Translation: CAA68212.1.
AP002032 Genomic DNA. Translation: BAB09806.1.
AY056186 mRNA. Translation: AAL07035.1.
AY096713 mRNA. Translation: AAM20347.1.
AY087674 mRNA. Translation: AAM65211.1.

RefSeq

NP_196290.1.

UniGene

At.93

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PA2	X-ray	1.45	A	31-335	[»]
1QO4	X-ray	3.00	A	31-335	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

219. AtPrx53.

Proteomic databases

PRIDE

Q42578.

Genome annotation databases

GeneID

830561.

GenomeReviews

Gene locus AT5G06720 in contig BA000015_GR.

KEGG

ath:AT5G06720.

NMPDR

fig|3702.1.peg.22803.

Organism-specific databases

GeneFarm

1907. 61.

TAIR

At5g06720.

Gene expression databases

ArrayExpress

Q42578.

GermOnline