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Protein

Peroxidase 37

Gene

PER37

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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
Sitei60 – 601Transition state stabilizerPROSITE-ProRule annotation
Active sitei64 – 641Proton acceptorPROSITE-ProRule annotation
Metal bindingi65 – 651Calcium 1PROSITE-ProRule annotation
Metal bindingi68 – 681Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi70 – 701Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi72 – 721Calcium 1PROSITE-ProRule annotation
Metal bindingi74 – 741Calcium 1PROSITE-ProRule annotation
Binding sitei161 – 1611Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi192 – 1921Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi193 – 1931Calcium 2PROSITE-ProRule annotation
Metal bindingi244 – 2441Calcium 2PROSITE-ProRule annotation
Metal bindingi247 – 2471Calcium 2PROSITE-ProRule annotation
Metal bindingi252 – 2521Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • negative regulation of growth Source: TAIR
  • response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G08770-MONOMER.

Protein family/group databases

PeroxiBasei203. AtPrx37.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 37 (EC:1.11.1.7)
Short name:
Atperox P37
Alternative name(s):
ATP38
Gene namesi
Name:PER37
Synonyms:P37
Ordered Locus Names:At4g08770
ORF Names:T32A17.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G08770.

Subcellular locationi

  • Secreted Curated
  • Vacuole Curated

  • Note: Carboxy-terminal extension appears to target the protein to vacuoles.

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 346324Peroxidase 37PRO_0000023703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acidPROSITE-ProRule annotationBy similarity
Disulfide bondi33 ↔ 113PROSITE-ProRule annotation
Disulfide bondi66 ↔ 71PROSITE-ProRule annotation
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi119 ↔ 323PROSITE-ProRule annotation
Disulfide bondi199 ↔ 231PROSITE-ProRule annotation
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence analysis
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ9LDN9.
PRIDEiQ9LDN9.

Expressioni

Gene expression databases

GenevisibleiQ9LDN9. AT.

Interactioni

Protein-protein interaction databases

BioGridi11746. 2 interactions.
STRINGi3702.AT4G08770.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LDN9.
SMRiQ9LDN9. Positions 23-327.
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

eggNOGiENOG410JAWC. Eukaryota.
ENOG41119N5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9LDN9.
KOiK00430.
OMAiWHSSITI.
PhylomeDBiQ9LDN9.

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.

Q9LDN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSSLIKLGF LLLLIQVSLS HAQLSPSFYD KTCPQVFDIA TTTIVNALRS
60 70 80 90 100
DPRIAASILR LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD
110 120 130 140 150
VIDKMKAAVE KACPKTVSCA DLLAIAAQES VVLAGGPSWR VPNGRRDSLR
160 170 180 190 200
GFMDLANDNL PAPFFTLNQL KDRFKNVGLD RASDLVALSG GHTFGKNQCQ
210 220 230 240 250
FIMDRLYNFS NTGLPDPTLD KSYLSTLRKQ CPRNGNQSVL VDFDLRTPTL
260 270 280 290 300
FDNKYYVNLK ENKGLIQSDQ ELFSSPDASD TLPLVREYAD GQGKFFDAFA
310 320 330 340
KAMIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVEDAL EFASSM
Length:346
Mass (Da):38,203
Last modified:October 1, 2000 - v1
Checksum:i744A4B8B618E15EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281F → L in AAM97030 (PubMed:14593172).Curated
Sequence conflicti28 – 281F → L in AAN15499 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452387 mRNA. Translation: AAL40851.1.
AL161512 Genomic DNA. Translation: CAB78002.1.
AL161813 Genomic DNA. Translation: CAB82113.1.
CP002687 Genomic DNA. Translation: AEE82676.1.
AY136364 mRNA. Translation: AAM97030.1.
BT000180 mRNA. Translation: AAN15499.1.
PIRiB85088.
RefSeqiNP_192617.1. NM_116947.2.
UniGeneiAt.4181.
At.54214.

Genome annotation databases

EnsemblPlantsiAT4G08770.1; AT4G08770.1; AT4G08770.
GeneIDi826447.
GrameneiAT4G08770.1; AT4G08770.1; AT4G08770.
KEGGiath:AT4G08770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452387 mRNA. Translation: AAL40851.1.
AL161512 Genomic DNA. Translation: CAB78002.1.
AL161813 Genomic DNA. Translation: CAB82113.1.
CP002687 Genomic DNA. Translation: AEE82676.1.
AY136364 mRNA. Translation: AAM97030.1.
BT000180 mRNA. Translation: AAN15499.1.
PIRiB85088.
RefSeqiNP_192617.1. NM_116947.2.
UniGeneiAt.4181.
At.54214.

3D structure databases

ProteinModelPortaliQ9LDN9.
SMRiQ9LDN9. Positions 23-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11746. 2 interactions.
STRINGi3702.AT4G08770.1.

Protein family/group databases

PeroxiBasei203. AtPrx37.

Proteomic databases

PaxDbiQ9LDN9.
PRIDEiQ9LDN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G08770.1; AT4G08770.1; AT4G08770.
GeneIDi826447.
GrameneiAT4G08770.1; AT4G08770.1; AT4G08770.
KEGGiath:AT4G08770.

Organism-specific databases

TAIRiAT4G08770.

Phylogenomic databases

eggNOGiENOG410JAWC. Eukaryota.
ENOG41119N5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9LDN9.
KOiK00430.
OMAiWHSSITI.
PhylomeDBiQ9LDN9.

Enzyme and pathway databases

BioCyciARA:AT4G08770-MONOMER.

Miscellaneous databases

PROiQ9LDN9.

Gene expression databases

GenevisibleiQ9LDN9. 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. "Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana."
    Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.
    Eur. J. Biochem. 269:6063-6081(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Root.
  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. "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 nameiPER37_ARATH
AccessioniPrimary (citable) accession number: Q9LDN9
Secondary accession number(s): Q8L7B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 122 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.