Reviewed, UniProtKB/Swiss-Prot Q9SZE7 (PER51_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 51
      Short name=Atperox P51
    EC=1.11.1.7
Alternative name(s):
    ATP37

Gene names

Name:	PER51
Synonyms:	P51
Ordered Locus Names:	At4g37530
ORF Names:	F19F18.20, F6G17.2

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	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted By similarity.
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
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	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 response to salt stress Inferred from expression pattern. Source: TAIR
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...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SZE7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 329	304	Peroxidase 51		PRO_0000023716
Sites
	Active site	67	1	Proton acceptor By similarity
	Metal binding	68	1	Calcium 1 By similarity
	Metal binding	71	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	73	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	75	1	Calcium 1 By similarity
	Metal binding	77	1	Calcium 1 By similarity
	Metal binding	197	1	Iron (heme axial ligand) By similarity
	Metal binding	198	1	Calcium 2 By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Metal binding	257	1	Calcium 2 By similarity
	Binding site	167	1	Substrate; via carbonyl oxygen By similarity
	Site	63	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	26	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Disulfide bond	36 ↔ 119		By similarity
	Disulfide bond	69 ↔ 74		By similarity
	Disulfide bond	125 ↔ 325		By similarity
	Disulfide bond	204 ↔ 236		By similarity
Experimental info
	Sequence conflict	31	1	F → L in AAL49862. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: DF4D71BB1503F145	FASTA	329	35,989
	10 20 30 40 50 60 MVVMNKTNLL LLILSLFLAI NLSSAQLRGD FYAGTCPNVE QIVRNAVQKK IQQTFTTIPA 70 80 90 100 110 120 TLRLYFHDCF VNGCDASVMI ASTNTNKAEK DHEDNLSLAG DGFDTVIKAK EAVDAVPNCR 130 140 150 160 170 180 NKVSCADILT MATRDVVNLA GGPQYAVELG RRDGLSSSAS SVTGKLPKPT FDLNQLNALF 190 200 210 220 230 240 AENGLSPNDM IALSGAHTLG FAHCTKVFNR LYNFNKTNNV DPTINKDYVT ELKASCPQNI 250 260 270 280 290 300 DPRVAINMDP NTPRQFDNVY YKNLQQGKGL FTSDQVLFTD SRSKPTVDLW ANNGQLFNQA 310 320 FISSMIKLGR VGVKTGSNGN IRRDCGAFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana." Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L. Eur. J. Biochem. 269:6063-6081(2002) [PubMed: 12473102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [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]	"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	AF469928 mRNA. Translation: AAL79842.1. AL035605 Genomic DNA. Translation: CAB38292.1. AL161591 Genomic DNA. Translation: CAB80418.1. AL035601 Genomic DNA. No translation available. AY070459 mRNA. Translation: AAL49862.1. AY150515 mRNA. Translation: AAN13031.1.
IPI	IPI00540304.
PIR	T04710.
RefSeq	NP_195469.1.
UniGene	At.68229
3D structure databases
HSSP	HSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBase	Search...
Protein family/group databases
PeroxiBase	217. AtPrx51.
Proteomic databases
PRIDE	Q9SZE7.
Genome annotation databases
GeneID	829908.
GenomeReviews	Gene locus AT4G37530 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.21864.
Organism-specific databases
GeneFarm	1883. 61.
TAIR	At4g37530.
Phylogenomic databases
OMA	Q9SZE7. INMDPNT.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9SZE7.
GermOnline	AT4G37530. Arabidopsis thaliana.
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. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER51_ARATH

Accession

Primary (citable) accession number: Q9SZE7
Secondary accession number(s): Q8VYK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)