Reviewed, UniProtKB/Swiss-Prot Q42592 (APXS_ARATH)

Names and origin

Protein names

Recommended name:
    L-ascorbate peroxidase S, chloroplastic/mitochondrial
    EC=1.11.1.11
Alternative name(s):
    Stromal ascorbate peroxidase
      Short name=sAPX
      Short name=AtAPx05

Gene names

Name:	APXS
Ordered Locus Names:	At4g08390
ORF Names:	T28D5.80

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	372 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	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 1 potassium or calcium ion per subunit By similarity.
Subcellular location	Mitochondrion. Plastid › chloroplast stromaPotential.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Transit peptide
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
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	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium 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
	Transit peptide	1 – ?		Chloroplast and mitochondrion Potential
	Chain	? – 372		L-ascorbate peroxidase S, chloroplastic/mitochondrial		PRO_0000261326
Sites
	Active site	133	1	Proton acceptor By similarity
	Metal binding	262	1	Iron (heme axial ligand) By similarity
	Metal binding	263	1	Potassium or calcium By similarity
	Metal binding	295	1	Potassium or calcium By similarity
	Metal binding	302	1	Potassium or calcium By similarity
	Site	129	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	11	1	G → V in CAA67425. Ref.1
	Sequence conflict	75	1	S → P in CAA67425. Ref.1
	Sequence conflict	81	1	Y → C in CAA67425. Ref.1
	Sequence conflict	371	1	V → I in CAA67425. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q42592-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: A5D94B9A20720B87	FASTA	372	40,407
	10 20 30 40 50 60 MAERVSLTLN GTLLSPPPTT TTTTMSSSLR STTAASLLLR SSSSSSRSTL TLSASSSLSF 70 80 90 100 110 120 VRSLVSSPRL SSSSSLSQKK YRIASVNRSF NSTTAATKSS SSDPDQLKNA REDIKELLST 130 140 150 160 170 180 KFCHPILVRL GWHDAGTYNK NIKEWPQRGG ANGSLRFDIE LKHAANAGLV NALNLIKDIK 190 200 210 220 230 240 EKYSGISYAD LFQLASATAI EEAGGPKIPM KYGRVDASGP EDCPEEGRLP DAGPPSPATH 250 260 270 280 290 300 LREVFYRMGL DDKDIVALSG AHTLGRSRPE RSGWGKPETK YTKEGPGAPG GQSWTPEWLK 310 320 330 340 350 360 FDNSYFKEIK EKRDEDLLVL PTDAAIFEDS SFKVYAEKYA ADQDAFFKDY AVAHAKLSNL 370 GAEFNPPEGI VI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase." Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G. Biochem. J. 326:305-310(1997) [PubMed: 9291097] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"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.
[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]	"Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants." Chew O., Whelan J., Millar A.H. J. Biol. Chem. 278:46869-46877(2003) [PubMed: 12954611] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X98925 mRNA. Translation: CAA67425.1. AL109819 Genomic DNA. Translation: CAB52561.1. AL161511 Genomic DNA. Translation: CAB77964.1. AY056319 mRNA. Translation: AAL07168.1. AY114065 mRNA. Translation: AAM45113.1.
PIR	T14193.
RefSeq	NP_192579.1. NP_974520.1.
UniGene	At.22866
3D structure databases
HSSP	HSSP built from PDB template 1IYN based on UniProtKB Q8LNY5.
SMR	Q42592. Positions 100-369.
ModBase	Search...
Proteomic databases
ProMEX	Q42592.
Genome annotation databases
GeneID	826396.
GenomeReviews	Gene locus AT4G08390 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.18492.
Organism-specific databases
GeneFarm	1956. 146.
TAIR	At4g08390.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APXS_ARATH

Accession

Primary (citable) accession number: Q42592
Secondary accession number(s): Q9STM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	November 25, 2008
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)