Reviewed, UniProtKB/Swiss-Prot O23237 (PER49_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 49
      Short name=Atperox P49
    EC=1.11.1.7
Alternative name(s):
    ATP31

Gene names

Name:	PER49
Synonyms:	DIDI 6G-3B, P49
Ordered Locus Names:	At4g36430
ORF Names:	C7A10.930, AP22.54

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	331 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 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 By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	SecretedBy 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
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
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
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 – 22	22	Potential
	Chain	23 – 331	309	Peroxidase 49		PRO_0000023714
Sites
	Active site	70	1	Proton acceptor By similarity
	Metal binding	71	1	Calcium 1 By similarity
	Metal binding	74	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	76	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	78	1	Calcium 1 By similarity
	Metal binding	80	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	66	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Disulfide bond	39 ↔ 119		By similarity
	Disulfide bond	72 ↔ 77		By similarity
	Disulfide bond	125 ↔ 326		By similarity
	Disulfide bond	204 ↔ 236		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O23237-1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: E9C0130D77406624	FASTA	331	36,164
	10 20 30 40 50 60 MARLTSFLLL LSLICFVPLC LCDKSYGGKL FPGYYAHSCP QVNEIVRSVV AKAVARETRM 70 80 90 100 110 120 AASLLRLHFH DCFVQGCDGS LLLDSSGRVA TEKNSNPNSK SARGFDVVDQ IKAELEKQCP 130 140 150 160 170 180 GTVSCADVLT LAARDSSVLT GGPSWVVPLG RRDSRSASLS QSNNNIPAPN NTFQTILSKF 190 200 210 220 230 240 NRQGLDITDL VALSGSHTIG FSRCTSFRQR LYNQSGNGSP DMTLEQSFAA NLRQRCPKSG 250 260 270 280 290 300 GDQILSVLDI ISAASFDNSY FKNLIENKGL LNSDQVLFSS NEKSRELVKK YAEDQGEFFE 310 320 330 QFAESMIKMG NISPLTGSSG EIRKNCRKIN S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis thaliana genes expressed in the early compatible interaction with root-knot nematodes." Vercauteren I., van der Schueren E., Van Montagu M., Gheysen G. Mol. Plant Microbe Interact. 14:288-299(2001) [PubMed: 11277426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Root.
[2]	"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. Tissue: Root.
[3]	"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.
[4]	"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.
[5]	"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	AJ286345 mRNA. Translation: CAB71009.1. AF452384 mRNA. Translation: AAL40848.1. Z99708 Genomic DNA. Translation: CAB16848.1. AL161589 Genomic DNA. Translation: CAB80309.1. AY074296 mRNA. Translation: AAL66993.1. AY117238 mRNA. Translation: AAM51313.1.
PIR	A85430.
RefSeq	NP_195361.1.
UniGene	At.4607
3D structure databases
HSSP	HSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBase	Search...
Protein family/group databases
PeroxiBase	215. AtPrx49.
Genome annotation databases
GeneID	829795.
GenomeReviews	Gene locus AT4G36430 in contig CT486007_GR.
KEGG	ath:AT4G36430.
NMPDR	fig|3702.1.peg.21738.
Organism-specific databases
GeneFarm	1881. 61.
TAIR	At4g36430.
Gene expression databases
ArrayExpress	O23237.
GermOnline	AT4G36430. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. [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

PER49_ARATH

Accession

Primary (citable) accession number: O23237

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	May 1, 1999
Last modified:	November 25, 2008
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)