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Protein

Peroxidase 45

Gene

PER45

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

Functioni

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 activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+PROSITE-ProRule annotationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei63 – 631Transition state stabilizerPROSITE-ProRule annotation
Active sitei67 – 671Proton acceptorPROSITE-ProRule annotation
Metal bindingi68 – 681Calcium 1PROSITE-ProRule annotation
Metal bindingi71 – 711Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi73 – 731Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi75 – 751Calcium 1PROSITE-ProRule annotation
Metal bindingi77 – 771Calcium 1PROSITE-ProRule annotation
Binding sitei163 – 1631Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi193 – 1931Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi194 – 1941Calcium 2PROSITE-ProRule annotation
Metal bindingi245 – 2451Calcium 2PROSITE-ProRule annotation
Metal bindingi248 – 2481Calcium 2PROSITE-ProRule annotation
Metal bindingi253 – 2531Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G30170-MONOMER.

Protein family/group databases

PeroxiBasei211. AtPrx45.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 45 (EC:1.11.1.7)
Short name:
Atperox P45
Alternative name(s):
ATP8a
Gene namesi
Name:PER45
Synonyms:P45
Ordered Locus Names:At4g30170
ORF Names:F9N11.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G30170.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 325300Peroxidase 45PRO_0000023711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 115PROSITE-ProRule annotation
Disulfide bondi69 ↔ 74PROSITE-ProRule annotation
Disulfide bondi121 ↔ 321PROSITE-ProRule annotation
Disulfide bondi200 ↔ 232PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ96522.
PRIDEiQ96522.

Expressioni

Tissue specificityi

Slightly expressed in roots.1 Publication

Inductioni

Up-regulated transiently by a cold treatment. Induced by methyl jasmonate, a plant defense-related signaling molecule.2 Publications

Gene expression databases

GenevisibleiQ96522. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G30170.1.

Structurei

3D structure databases

ProteinModelPortaliQ96522.
SMRiQ96522. Positions 26-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJYG. Eukaryota.
ENOG4111S7R. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ96522.
KOiK00430.
OMAiQLKQMCP.
PhylomeDBiQ96522.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
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.

Q96522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKNTSQTIF SNFFLLLLLS SCVSAQLRTG FYQNSCPNVE TIVRNAVRQK
60 70 80 90 100
FQQTFVTAPA TLRLFFHDCF VRGCDASIMI ASPSERDHPD DMSLAGDGFD
110 120 130 140 150
TVVKAKQAVD SNPNCRNKVS CADILALATR EVVVLTGGPS YPVELGRRDG
160 170 180 190 200
RISTKASVQS QLPQPEFNLN QLNGMFSRHG LSQTDMIALS GAHTIGFAHC
210 220 230 240 250
GKMSKRIYNF SPTTRIDPSI NRGYVVQLKQ MCPIGVDVRI AINMDPTSPR
260 270 280 290 300
TFDNAYFKNL QQGKGLFTSD QILFTDQRSR STVNSFANSE GAFRQAFITA
310 320
ITKLGRVGVL TGNAGEIRRD CSRVN
Length:325
Mass (Da):35,829
Last modified:February 1, 1997 - v1
Checksum:iF852C14BC2E846CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98855 mRNA. Translation: CAA67361.1.
AL109796 Genomic DNA. Translation: CAB52461.1.
AL161576 Genomic DNA. Translation: CAB81010.1.
CP002687 Genomic DNA. Translation: AEE85729.1.
AF370284 mRNA. Translation: AAK44099.1.
AY063051 mRNA. Translation: AAL34225.1.
AY085450 mRNA. Translation: AAM62676.1.
PIRiT14077.
RefSeqiNP_194746.1. NM_119163.2.
UniGeneiAt.24710.
At.67068.

Genome annotation databases

EnsemblPlantsiAT4G30170.1; AT4G30170.1; AT4G30170.
GeneIDi829140.
GrameneiAT4G30170.1; AT4G30170.1; AT4G30170.
KEGGiath:AT4G30170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98855 mRNA. Translation: CAA67361.1.
AL109796 Genomic DNA. Translation: CAB52461.1.
AL161576 Genomic DNA. Translation: CAB81010.1.
CP002687 Genomic DNA. Translation: AEE85729.1.
AF370284 mRNA. Translation: AAK44099.1.
AY063051 mRNA. Translation: AAL34225.1.
AY085450 mRNA. Translation: AAM62676.1.
PIRiT14077.
RefSeqiNP_194746.1. NM_119163.2.
UniGeneiAt.24710.
At.67068.

3D structure databases

ProteinModelPortaliQ96522.
SMRiQ96522. Positions 26-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G30170.1.

Protein family/group databases

PeroxiBasei211. AtPrx45.

Proteomic databases

PaxDbiQ96522.
PRIDEiQ96522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G30170.1; AT4G30170.1; AT4G30170.
GeneIDi829140.
GrameneiAT4G30170.1; AT4G30170.1; AT4G30170.
KEGGiath:AT4G30170.

Organism-specific databases

TAIRiAT4G30170.

Phylogenomic databases

eggNOGiENOG410IJYG. Eukaryota.
ENOG4111S7R. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ96522.
KOiK00430.
OMAiQLKQMCP.
PhylomeDBiQ96522.

Enzyme and pathway databases

BioCyciARA:AT4G30170-MONOMER.

Miscellaneous databases

PROiQ96522.

Gene expression databases

GenevisibleiQ96522. AT.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
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. "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 (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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. "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].
  6. "Computational analyses and annotations of the Arabidopsis peroxidase gene family."
    Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.
    FEBS Lett. 433:98-102(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: cv. Columbia.
  7. "Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array."
    Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.
    Plant Physiol. Biochem. 39:221-242(2001)
    Cited for: TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  8. "Coordinated plant defense responses in Arabidopsis revealed by microarray analysis."
    Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  9. "Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway."
    Fowler S., Thomashow M.F.
    Plant Cell 14:1675-1690(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  10. "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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
    Strain: cv. Columbia.

Entry informationi

Entry nameiPER45_ARATH
AccessioniPrimary (citable) accession number: Q96522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: February 1, 1997
Last modified: February 17, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

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.