Reviewed, UniProtKB/Swiss-Prot Q9LHA7 (PER31_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 31
      Short name=Atperox P31
    EC=1.11.1.7
Alternative name(s):
    ATP41

Gene names

Name:	PER31
Synonyms:	P31
Ordered Locus Names:	At3g28200
ORF Names:	T19D11.1, T19D11.4

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	316 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
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond 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-SubCell plant-type cell wall Inferred from direct assay. Source: TAIR
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 316	297	Peroxidase 31		PRO_0000023697
Sites
	Active site	61	1	Proton acceptor
	Metal binding	62	1	Calcium 1 By similarity
	Metal binding	67	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	69	1	Calcium 1 By similarity
	Metal binding	71	1	Calcium 1 By similarity
	Metal binding	189	1	Iron (heme axial ligand) By similarity
	Metal binding	190	1	Calcium 2 By similarity
	Metal binding	236	1	Calcium 2 By similarity
	Metal binding	239	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Binding site	159	1	Substrate; via carbonyl oxygen By similarity
	Site	57	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Disulfide bond	30 ↔ 111		By similarity
	Disulfide bond	63 ↔ 68		By similarity
	Disulfide bond	117 ↔ 312		By similarity
	Disulfide bond	196 ↔ 222		By similarity
Experimental info
	Sequence conflict	143	1	R → H in AAK59478. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9LHA7-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8B0A974FC8144523	FASTA	316	35,303
	10 20 30 40 50 60 MASLKSLFLL FLFFFTAQSR LTTNFYSKTC PRFLDIIRDT ITNKQITNPT TAAAVIRLFF 70 80 90 100 110 120 HDCFPNGCDA SVLISSTAFN TAERDSSINL SLPGDGFDVI VRAKTALELA CPNTVSCSDI 130 140 150 160 170 180 ISVATRDLLI TVGGPYYDVF LGRRDSRTSK SSLLTDLLPL PSTPISKIIQ QFESKGFTVQ 190 200 210 220 230 240 EMVALSGAHS IGFSHCKEFV GRVGRNNTGY NPRFAVALKK ACANYPKDPT ISVFNDIMTP 250 260 270 280 290 300 NKFDNMYYQN LKKGLGLLES DHGLYSDPRT RYFVDLYAKN QDLFFKDFAK AMQKLSLFGI 310 QTGRRGEIRR RCDAIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed: 10907853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"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	AP002056 Genomic DNA. Translation: BAB02637.1. AY034973 mRNA. Translation: AAK59478.1. AY150382 mRNA. Translation: AAN12927.1.
IPI	IPI00521145.
RefSeq	NP_189460.1.
UniGene	At.13955 At.22736
3D structure databases
HSSP	HSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBase	Search...
Protein family/group databases
PeroxiBase	197. AtPrx31.
Proteomic databases
PRIDE	Q9LHA7.
Genome annotation databases
GeneID	822446.
GenomeReviews	Gene locus AT3G28200 in contig BA000014_GR.
KEGG	ath:AT3G28200.
NMPDR	fig|3702.1.peg.15114.
Organism-specific databases
GeneFarm	1858. 61.
TAIR	At3g28200.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9LHA7.
GermOnline	AT3G28200. 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. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER31_ARATH

Accession

Primary (citable) accession number: Q9LHA7
Secondary accession number(s): Q94CB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)