Reviewed, UniProtKB/Swiss-Prot Q9LDA4 (PER38_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 38
      Short name=Atperox P38
    EC=1.11.1.7

Gene names

Name:	PER38
Synonyms:	P38
Ordered Locus Names:	At4g08780
ORF Names:	T32A17.90

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	346 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	SecretedProbable. VacuoleProbable. 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	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-KW vacuole Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding 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 – 22	22	Potential
	Chain	23 – 346	324	Peroxidase 38		PRO_0000023704
Sites
	Active site	64	1	Proton acceptor By similarity
	Metal binding	65	1	Calcium 1 By similarity
	Metal binding	68	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	70	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	74	1	Calcium 1 By similarity
	Metal binding	192	1	Iron (heme axial ligand) By similarity
	Metal binding	193	1	Calcium 2 By similarity
	Metal binding	244	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	60	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	23	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Disulfide bond	33 ↔ 113		By similarity
	Disulfide bond	66 ↔ 71		By similarity
	Disulfide bond	119 ↔ 323		By similarity
	Disulfide bond	199 ↔ 231		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LDA4-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: D5CD5762D9C03392	FASTA	346	38,086
	10 20 30 40 50 60 MHSSLIKLGF LLLLLQVSLS HAQLSPSFYD KTCPQVFDIV TNTIVNALRS DPRIAASILR 70 80 90 100 110 120 LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAIE KACPRTVSCA 130 140 150 160 170 180 DMLAIAAKES IVLAGGPSWM VPNGRRDSLR GFMDLANDNL PGPSSTLKQL KDRFKNVGLD 190 200 210 220 230 240 RSSDLVALSG GHTFGKSQCQ FIMDRLYNFG ETGLPDPTLD KSYLATLRKQ CPRNGNQSVL 250 260 270 280 290 300 VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDAAD TLPLVRAYAD GQGTFFDAFV 310 320 330 340 KAIIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVDDAL EFASFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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	AL161512 Genomic DNA. Translation: CAB78003.1. AL161813 Genomic DNA. Translation: CAB82114.1.
PIR	C85088.
RefSeq	NP_192618.1.
UniGene	At.54214
3D structure databases
HSSP	HSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMR	Q9LDA4. Positions 23-327.
ModBase	Search...
Protein family/group databases
PeroxiBase	204. AtPrx38.
Genome annotation databases
GeneID	826448.
GenomeReviews	Gene locus AT4G08780 in contig CT486007_GR.
KEGG	ath:AT4G08780.
NMPDR	fig|3702.1.peg.18531.
Organism-specific databases
GeneFarm	1867. 61.
TAIR	At4g08780.
Gene expression databases
ArrayExpress	Q9LDA4.
GermOnline	AT4G08780. 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]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

PER38_ARATH

Accession

Primary (citable) accession number: Q9LDA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	October 1, 2000
Last modified:	November 4, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)