Reviewed, UniProtKB/Swiss-Prot Q39034 (PER59_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 59
      Short name=Atperox P59
    EC=1.11.1.7
Alternative name(s):
    Peroxidase N
    ATPN

Gene names

Name:	PER59
Synonyms:	P59
Ordered Locus Names:	At5g19890
ORF Names:	F28I16.40

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	328 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.
Catalytic activity	Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 2 calcium ions per subunit.
Subcellular location	SecretedBy similarity.
Tissue specificity	Slightly 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 – 28

28

Potential

Chain

29 – 328

300

Peroxidase 59

PRO_0000023724

Sites

Active site

70

1

Proton acceptor

Metal binding

71

1

Calcium 1

Metal binding

74

1

Calcium 1; via carbonyl oxygen

Metal binding

76

1

Calcium 1; via carbonyl oxygen

Metal binding

78

1

Calcium 1

Metal binding

80

1

Calcium 1

Metal binding

193

1

Iron (heme axial ligand)

Metal binding

194

1

Calcium 2

Metal binding

245

1

Calcium 2

Metal binding

248

1

Calcium 2

Metal binding

251

1

Calcium 2; via carbonyl oxygen

Metal binding

253

1

Calcium 2

Binding site

163

1

Substrate; via carbonyl oxygen

Site

66

1

Transition state stabilizer

Amino acid modifications

Modified residue

29

1

Pyrrolidone carboxylic acid By similarity

Glycosylation

182

1

N-linked (GlcNAc...) Potential

Glycosylation

209

1

N-linked (GlcNAc...) Potential

Glycosylation

239

1

N-linked (GlcNAc...) Potential

Glycosylation

281

1

N-linked (GlcNAc...) Potential

Glycosylation

310

1

N-linked (GlcNAc...) Potential

Disulfide bond

39 ↔ 116

Disulfide bond

72 ↔ 77

Disulfide bond

122 ↔ 323

Disulfide bond

200 ↔ 232

Experimental info

Sequence conflict

3

1

T → R in AAM65571. Ref.4

Sequence conflict

213

1

L → A Ref.1 Ref.4

Secondary structure

1

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328

Helix Strand Turn

Details...

Turn

32 – 38

7

Helix

42 – 56

15

Helix

60 – 72

13

Turn

73 – 75

3

Beta strand

76 – 79

4

Helix

80 – 82

3

Helix

89 – 91

3

Turn

93 – 98

6

Helix

102 – 115

14

Turn

117 – 119

3

Helix

122 – 135

14

Turn

136 – 138

3

Helix

156 – 159

4

Helix

169 – 177

9

Turn

178 – 180

3

Helix

183 – 190

8

Helix

191 – 194

4

Beta strand

195 – 199

5

Helix

200 – 202

3

Helix

204 – 206

3

Beta strand

210 – 214

5

Helix

222 – 231

10

Beta strand

241 – 247

7

Beta strand

249 – 251

3

Helix

255 – 261

7

Helix

268 – 275

8

Turn

277 – 283

7

Helix

284 – 292

9

Helix

294 – 308

15

Sequences

	Sequence		Length	Mass (Da)
	Q39034-1 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: DABD3854FB2D3B12	FASTA	328	35,023
	10 20 30 40 50 60 MKTQTKVMGG HVLLTVFTLC MLCSGVRAQL SPDIYAKSCP NLVQIVRKQV AIALKAEIRM 70 80 90 100 110 120 AASLIRLHFH DCFVNGCDAS LLLDGADSEK LAIPNINSAR GFEVIDTIKA AVENACPGVV 130 140 150 160 170 180 SCADILTLAA RDSVVLSGGP GWRVALGRKD GLVANQNSAN NLPSPFEPLD AIIAKFVAVN 190 200 210 220 230 240 LNITDVVALS GAHTFGQAKC AVFSNRLFNF TGLGNPDATL ETSLLSNLQT VCPLGGNSNI 250 260 270 280 290 300 TAPLDRSTTD TFDNNYFKNL LEGKGLLSSD QILFSSDLAV NTTKKLVEAY SRSQSLFFRD 310 320 FTCAMIRMGN ISNGASGEVR TNCRVINN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis and expression of two peroxidase encoding mRNAs from Arabidopsis thaliana." Oestergaard L., Welinder K.G. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] 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 thaliana peroxidase N: structure of a novel neutral peroxidase." Mirza O., Henriksen A., Oestergaard L., Welinder K.G., Gajhede M. Acta Crystallogr. D 56:372-375(2000) [PubMed: 10713531] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME, DISULFIDE BONDS. Strain: cv. Columbia.
[7]	"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

X98453 mRNA. Translation: CAA67092.1.
AF296836 Genomic DNA. No translation available.
AY123985 mRNA. Translation: AAM74498.1.
BT000582 mRNA. Translation: AAN18151.1.
AY088025 mRNA. Translation: AAM65571.1.

RefSeq

NP_568385.1.

UniGene

At.143

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QGJ	X-ray	1.90	A/B	29-328	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

225. AtPrx59.

Genome annotation databases

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