Reviewed, UniProtKB/Swiss-Prot Q9FG34 (PER54_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 54
      Short name=Atperox P54
    EC=1.11.1.7
Alternative name(s):
    ATP29a

Gene names

Name:	PER54
Synonyms:	P54
Ordered Locus Names:	At5g06730
ORF Names:	MPH15.9

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	358 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 Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: TAIR vacuole 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 358	327	Peroxidase 54		PRO_0000023719
Sites
	Active site	73	1	Proton acceptor By similarity
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	77	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	81	1	Calcium 1 By similarity
	Metal binding	83	1	Calcium 1 By similarity
	Metal binding	200	1	Iron (heme axial ligand) By similarity
	Metal binding	201	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Metal binding	255	1	Calcium 2 By similarity
	Metal binding	260	1	Calcium 2 By similarity
	Binding site	170	1	Substrate; via carbonyl oxygen By similarity
	Site	69	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	32	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	34	1	N-linked (GlcNAc...) Potential
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	298	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 122		By similarity
	Disulfide bond	75 ↔ 80		By similarity
	Disulfide bond	128 ↔ 330		By similarity
	Disulfide bond	207 ↔ 239		By similarity
Experimental info
	Sequence conflict	21	1	I → V in AAM66044. Ref.4
	Sequence conflict	28	1	T → A in AAM66044. Ref.4
	Sequence conflict	189	1	K → N in AAM66044. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9FG34-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F9841562BAC5106B	FASTA	358	37,290
	10 20 30 40 50 60 MAVTSSSSTC DGFFIISLIV IVSSLFGTSS AQLNATFYSG TCPNASAIVR STIQQALQSD 70 80 90 100 110 120 ARIGGSLIRL HFHDCFVNGC DGSLLLDDTS SIQSEKNAPA NANSTRGFNV VDSIKTALEN 130 140 150 160 170 180 ACPGIVSCSD ILALASEASV SLAGGPSWTV LLGRRDGLTA NLSGANSSLP SPFEGLNNIT 190 200 210 220 230 240 SKFVAVGLKT TDVVSLSGAH TFGRGQCVTF NNRLFNFNGT GNPDPTLNST LLSSLQQLCP 250 260 270 280 290 300 QNGSNTGITN LDLSTPDAFD NNYFTNLQSN NGLLQSDQEL FSNTGSATVP IVNSFASNQT 310 320 330 340 350 LFFEAFVQSM IKMGNISPLT GSSGEIRQDC KVVNGQSSAT EAGDIQLQSD GPVSVADM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]	"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].
[5]	"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 212-358. Strain: cv. Columbia. Tissue: Root.
[6]	"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	AP002032 Genomic DNA. Translation: BAB09807.1. AK118827 mRNA. Translation: BAC43417.1. BT008584 mRNA. Translation: AAP40411.1. AY088509 mRNA. Translation: AAM66044.1. Y11794 mRNA. Translation: CAA72490.1.
IPI	IPI00528868.
RefSeq	NP_196291.1.
UniGene	At.90
3D structure databases
HSSP	HSSP built from PDB template 1PA2 based on UniProtKB Q42578.
SMR	Q9FG34. Positions 32-335.
ModBase	Search...
Protein family/group databases
PeroxiBase	220. AtPrx54.
Proteomic databases
PRIDE	Q9FG34.
Genome annotation databases
GeneID	830562.
GenomeReviews	Gene locus AT5G06730 in contig BA000015_GR.
KEGG	ath:AT5G06730.
NMPDR	fig|3702.1.peg.22804.
Organism-specific databases
GeneFarm	1908. 61.
TAIR	At5g06730.
Phylogenomic databases
OMA	Q9FG34. HRSDARI.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9FG34.
GermOnline	AT5G06730. 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

PER54_ARATH

Accession

Primary (citable) accession number: Q9FG34
Secondary accession number(s): P93729

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	March 1, 2001
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)