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Protein

L-ascorbate peroxidase 5, peroxisomal

Gene

APX5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in hydrogen peroxide removal.By similarity

Catalytic activityi

2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O.

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei35 – 351Transition state stabilizerPROSITE-ProRule annotation
Active sitei39 – 391Proton acceptorPROSITE-ProRule annotation
Metal bindingi158 – 1581Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi159 – 1591Potassium or calciumBy similarity
Metal bindingi175 – 1751Potassium or calciumBy similarity
Metal bindingi182 – 1821Potassium or calciumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, Potassium

Enzyme and pathway databases

BioCyciARA:AT4G35970-MONOMER.

Protein family/group databases

PeroxiBasei1887. AtAPx04.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ascorbate peroxidase 5, peroxisomal (EC:1.11.1.11)
Short name:
AtAPx04
Gene namesi
Name:APX5
Ordered Locus Names:At4g35970
ORF Names:F4B14_240, T19K4.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35970.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei251 – 27121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 279L-ascorbate peroxidase 5, peroxisomalPRO_0000261324
Transit peptidei1 – ?PeroxisomeSequence analysis

Proteomic databases

PaxDbiQ7XZP5.
PRIDEiQ7XZP5.

Expressioni

Gene expression databases

GenevisibleiQ7XZP5. AT.

Interactioni

Subunit structurei

Interacts with AKR2A and AKR2B.1 Publication

Protein-protein interaction databases

BioGridi15033. 2 interactions.
STRINGi3702.AT4G35970.1.

Structurei

3D structure databases

ProteinModelPortaliQ7XZP5.
SMRiQ7XZP5. Positions 5-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi272 – 2798AKR2A-binding sequence (ABS) required for peroxisome membrane targeting1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEWS. Eukaryota.
COG0376. LUCA.
HOGENOMiHOG000189824.
InParanoidiQ7XZP5.
KOiK00434.
OMAiVIFTICY.
PhylomeDBiQ7XZP5.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7XZP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNVDAEYL KEIEKTRRDL RALISSRNCA PIMLRLAWHD AGTYDAKKKT
60 70 80 90 100
GGANGSIRFK EELNRPHNKG LEKAVAFCEE VKAKHPRVSY ADLYQLAGVV
110 120 130 140 150
AVEVTGGPAI PFTPGRKDAD SADDGELPNP NEGASHLRTL FSRMGLLDRD
160 170 180 190 200
IVALSGGHTL GRAHKERSDF EGPWTQDPLK FDNSYFVELL KGETPGLLQL
210 220 230 240 250
KTDKALLDDP KFHPFVKLYA KDEDMFFKAY AISHKKLSEL GFNPPRRIPS
260 270
AVTQQTLGIA VAAAVVIFTI CYEASRRGK
Length:279
Mass (Da):30,895
Last modified:November 28, 2006 - v2
Checksum:i518836C729B1C745
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022373 Genomic DNA. Translation: CAA18491.1.
AL031986 Genomic DNA. Translation: CAA21483.1.
AL161588 Genomic DNA. Translation: CAB81506.1.
CP002687 Genomic DNA. Translation: AEE86596.1.
AK119023 mRNA. Translation: BAC43599.1.
BT006053 mRNA. Translation: AAP04038.1.
AF441714 mRNA. Translation: AAP72144.1.
PIRiT04707.
RefSeqiNP_195321.1. NM_119763.2.
UniGeneiAt.31367.

Genome annotation databases

EnsemblPlantsiAT4G35970.1; AT4G35970.1; AT4G35970.
GeneIDi829751.
GrameneiAT4G35970.1; AT4G35970.1; AT4G35970.
KEGGiath:AT4G35970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022373 Genomic DNA. Translation: CAA18491.1.
AL031986 Genomic DNA. Translation: CAA21483.1.
AL161588 Genomic DNA. Translation: CAB81506.1.
CP002687 Genomic DNA. Translation: AEE86596.1.
AK119023 mRNA. Translation: BAC43599.1.
BT006053 mRNA. Translation: AAP04038.1.
AF441714 mRNA. Translation: AAP72144.1.
PIRiT04707.
RefSeqiNP_195321.1. NM_119763.2.
UniGeneiAt.31367.

3D structure databases

ProteinModelPortaliQ7XZP5.
SMRiQ7XZP5. Positions 5-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15033. 2 interactions.
STRINGi3702.AT4G35970.1.

Protein family/group databases

PeroxiBasei1887. AtAPx04.

Proteomic databases

PaxDbiQ7XZP5.
PRIDEiQ7XZP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35970.1; AT4G35970.1; AT4G35970.
GeneIDi829751.
GrameneiAT4G35970.1; AT4G35970.1; AT4G35970.
KEGGiath:AT4G35970.

Organism-specific databases

TAIRiAT4G35970.

Phylogenomic databases

eggNOGiENOG410IEWS. Eukaryota.
COG0376. LUCA.
HOGENOMiHOG000189824.
InParanoidiQ7XZP5.
KOiK00434.
OMAiVIFTICY.
PhylomeDBiQ7XZP5.

Enzyme and pathway databases

BioCyciARA:AT4G35970-MONOMER.

Miscellaneous databases

PROiQ7XZP5.

Gene expression databases

GenevisibleiQ7XZP5. AT.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis."
    Panchuk I.I., Volkov R.A., Schoffl F.
    Plant Physiol. 129:838-853(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-279.
    Strain: cv. Columbia.
  6. "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis."
    Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.
    Plant Cell 22:811-831(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKR2A AND AKR2B.
    Strain: cv. C24 and cv. Columbia.
  7. "Is AKR2A an essential molecular chaperone for a class of membrane-bound proteins in plants?"
    Zhang H., Li X., Zhang Y., Kuppu S., Shen G.
    Plant Signal. Behav. 5:1520-1522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: AKR2A-BINDING SEQUENCE, REVIEW.

Entry informationi

Entry nameiAPX5_ARATH
AccessioniPrimary (citable) accession number: Q7XZP5
Secondary accession number(s): O65634
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: March 16, 2016
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one cation per subunit; probably K+, but might also be Ca2+.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.