Reviewed, UniProtKB/Swiss-Prot Q9LHB9 (PER32_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 32
      Short name=Atperox P32
    EC=1.11.1.7
Alternative name(s):
    PRXR3
    ATP16a

Gene names

Name:	PER32
Synonyms:	P32
Ordered Locus Names:	At3g32980
ORF Names:	T15D2.7, T15D2.9

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	352 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 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. Exhibits a Ca2+-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
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 Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
Tissue specificity	Strongly expressed in roots. Ref.9 Ref.10
Induction	Late induced by infection with an incompatible bacterial plant pathogen. Ref.11
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 Vacuole
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
Cellular component	cell wall Inferred from direct assay. Source: TAIR extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay. Source: TAIR vacuole 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 – 29	29	Potential
	Chain	30 – 352	323	Peroxidase 32		PRO_0000023698
Sites
	Active site	71	1	Proton acceptor
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	77	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1 By similarity
	Metal binding	81	1	Calcium 1 By similarity
	Metal binding	199	1	Iron (heme axial ligand) By similarity
	Metal binding	200	1	Calcium 2 By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Metal binding	254	1	Calcium 2 By similarity
	Metal binding	259	1	Calcium 2 By similarity
	Binding site	168	1	Substrate; via carbonyl oxygen By similarity
	Site	67	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	30	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Glycosylation	227	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Glycosylation	284	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 120		By similarity
	Disulfide bond	73 ↔ 78		By similarity
	Disulfide bond	126 ↔ 330		By similarity
	Disulfide bond	206 ↔ 238		By similarity
Experimental info
	Sequence conflict	24	1	S → L Ref.1
	Sequence conflict	24	1	S → L Ref.2
	Sequence conflict	24	1	S → L Ref.3
	Sequence conflict	24	1	S → L Ref.6
	Sequence conflict	145	1	S → Y in AAM64838. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9LHB9-1 [UniParc]. Last modified February 5, 2008. Version 3. Checksum: 765696B3869BA1DB	FASTA	352	38,847
	10 20 30 40 50 60 MNFSYSSLST WTTLMTLGCL LLHSSISSAQ LTPTFYDNTC PSVFTIVRDT IVNELRSDPR 70 80 90 100 110 120 IAASILRLHF HDCFVNGCDA SILLDNTTSF RTEKDAAPNA NSARGFPVID RMKAAVETAC 130 140 150 160 170 180 PRTVSCADIL TIAAQQAVNL AGGPSWRVPL GRRDSLQAFF ALANTNLPAP FFTLPQLKAS 190 200 210 220 230 240 FQNVGLDRPS DLVALSGGHT FGKNQCQFIM DRLYNFSNTG LPDPTLNTTY LQTLRGQCPR 250 260 270 280 290 300 NGNQTVLVDF DLRTPTVFDN KYYVNLKELK GLIQTDQELF SSPNATDTIP LVREYADGTQ 310 320 330 340 350 KFFNAFVEAM NRMGNITPLT GTQGQIRQNC RVVNSNSLLH DVVEIVDFVS SM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases." Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P. Plant Gene Register PGR96-066 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases." Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Structure of the gene encoding Arabidopsis thaliana PRXR3 peroxidase." Tognolli M., Greppin H., Simon P. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Structural analysis of Arabidopsis thaliana chromosome 3. III." Nakamura Y. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"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.
[6]	"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].
[7]	"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.
[8]	"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana." Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C. J. Plant Physiol. 159:1165-1171(2002) Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[9]	"Towards Arabidopsis genome analysis: monitoring expression profiles of 1400 genes using cDNA microarrays." Ruan Y., Gilmore J., Conner T. Plant J. 15:821-833(1998) [PubMed: 9807821] [Abstract] Cited for: TISSUE SPECIFICITY. Strain: cv. Columbia.
[10]	"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array." Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X. Plant Physiol. Biochem. 39:221-242(2001) Cited for: TISSUE SPECIFICITY. Strain: cv. Columbia.
[11]	"Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays." Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D. J. Biol. Chem. 277:10555-10561(2002) [PubMed: 11748215] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[12]	"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	X98315 mRNA. Translation: CAA66959.1. X98777 mRNA. Translation: CAA67313.1. AJ133036 Genomic DNA. Translation: CAB37193.1. AP002054 Genomic DNA. Translation: BAB02631.1. AY080608 mRNA. Translation: AAL86292.1. AY133730 mRNA. Translation: AAM91664.1. AY087285 mRNA. Translation: AAM64838.1.
IPI	IPI00518620.
RefSeq	NP_850652.1.
UniGene	At.47588 At.67710 At.71576
3D structure databases
HSSP	HSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMR	Q9LHB9. Positions 30-334.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9LHB9. 1 interaction.
Protein family/group databases
PeroxiBase	198. AtPrx32.
Proteomic databases
PRIDE	Q9LHB9.
Genome annotation databases
GeneID	823067.
GenomeReviews	Gene locus AT3G32980 in contig BA000014_GR.
KEGG	ath:AT3G32980.
Organism-specific databases
GeneFarm	1859. 61.
TAIR	At3g32980.
Phylogenomic databases
OMA	Q9LHB9. AVETACP.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9LHB9.
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

PER32_ARATH

Accession

Primary (citable) accession number: Q9LHB9
Secondary accession number(s): Q43732, Q6K1J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	February 5, 2008
Last modified:	June 16, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)