Reviewed, UniProtKB/Swiss-Prot Q9LT91 (PER66_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 66
      Short name=Atperox P66
    EC=1.11.1.7
Alternative name(s):
    ATP27a

Gene names

Name:	PER66
Synonyms:	P66
Ordered Locus Names:	At5g51890
ORF Names:	MJM18.4

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	322 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.
Caution	Lacks one of the disulfide bridges highly conserved in the class III peroxidase family.

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
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 Traceable author statement. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 322	298	Peroxidase 66		PRO_0000023731
Sites
	Active site	66	1	Proton acceptor By similarity
	Metal binding	67	1	Calcium 1 By similarity
	Metal binding	72	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	76	1	Calcium 1 By similarity
	Metal binding	191	1	Iron (heme axial ligand) By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	245	1	Calcium 2 By similarity
	Metal binding	247	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Binding site	161	1	Substrate; via carbonyl oxygen By similarity
	Site	62	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	155	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 114		By similarity
	Disulfide bond	68 ↔ 73		By similarity
	Disulfide bond	198 ↔ 230		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LT91-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: DCCFC4C87A5EB31B	FASTA	322	35,560
	10 20 30 40 50 60 MAFSKGLIFA MIFAVLAIVK PSEAALDAHY YDQSCPAAEK IILETVRNAT LYDPKVPARL 70 80 90 100 110 120 LRMFFHDCFI RGCDASILLD STRSNQAEKD GPPNISVRSF YVIEDAKRKL EKACPRTVSC 130 140 150 160 170 180 ADVIAIAARD VVTLSGGPYW SVLKGRKDGT ISRANETRNL PPPTFNVSQL IQSFAARGLS 190 200 210 220 230 240 VKDMVTLSGG HTIGFSHCSS FESRLQNFSK FHDIDPSMNY AFAQTLKKKC PRTSNRGKNA 250 260 270 280 290 300 GTVLDSTSSV FDNVYYKQIL SGKGVFGSDQ ALLGDSRTKW IVETFAQDQK AFFREFAASM 310 320 VKLGNFGVKE TGQVRVNTRF VN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [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]	"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 (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-322. 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	AB025623 Genomic DNA. Translation: BAA97224.1. AY072121 mRNA. Translation: AAL59943.1. AY122968 mRNA. Translation: AAM67501.1. Y11792 mRNA. Translation: CAA72488.1.
IPI	IPI00521324.
RefSeq	NP_200002.3.
UniGene	At.25182
3D structure databases
HSSP	HSSP built from PDB template 1GX2 based on UniProtKB P00433.
ModBase	Search...
Protein family/group databases
PeroxiBase	232. AtPrx66.
Genome annotation databases
GeneID	835264.
GenomeReviews	Gene locus AT5G51890 in contig BA000015_GR.
KEGG	ath:AT5G51890.
NMPDR	fig|3702.1.peg.27063.
Organism-specific databases
GeneFarm	1925. 61.
TAIR	At5g51890.
Phylogenomic databases
OMA	Q9LT91. FFREFAA.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9LT91.
GermOnline	AT5G51890. 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

PER66_ARATH

Accession

Primary (citable) accession number: Q9LT91
Secondary accession number(s): P93727

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)