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Reviewed, UniProtKB/Swiss-Prot Q9LDN9 (PER37_ARATH)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Peroxidase 37
      Short name=Atperox P37
    EC=1.11.1.7
Alternative name(s):
    ATP38
Gene names
Name: PER37
Synonyms: P37
Ordered Locus Names: At4g08770
ORF Names: T32A17.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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 activity

Donor + H2O2 = oxidized donor + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Subcellular location

Secreted Probable. Vacuole Probable. 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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 346324Peroxidase 37
PRO_0000023703

Sites

Active site641Proton acceptor By similarity
Metal binding651Calcium 1 By similarity
Metal binding681Calcium 1; via carbonyl oxygen By similarity
Metal binding701Calcium 1; via carbonyl oxygen By similarity
Metal binding721Calcium 1 By similarity
Metal binding741Calcium 1 By similarity
Metal binding1921Iron (heme axial ligand) By similarity
Metal binding1931Calcium 2 By similarity
Metal binding2441Calcium 2 By similarity
Metal binding2471Calcium 2 By similarity
Metal binding2521Calcium 2 By similarity
Binding site1611Substrate; via carbonyl oxygen By similarity
Site601Transition state stabilizer By similarity

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid By similarity
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 113 By similarity
Disulfide bond66 ↔ 71 By similarity
Disulfide bond119 ↔ 323 By similarity
Disulfide bond199 ↔ 231 By similarity

Experimental info

Sequence conflict281F → L in AAM97030. Ref.3
Sequence conflict281F → L in AAN15499. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q9LDN9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 744A4B8B618E15EE

FASTA34638,203
        10         20         30         40         50         60 
MHSSLIKLGF LLLLIQVSLS HAQLSPSFYD KTCPQVFDIA TTTIVNALRS DPRIAASILR 

        70         80         90        100        110        120 
LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAVE KACPKTVSCA 

       130        140        150        160        170        180 
DLLAIAAQES VVLAGGPSWR VPNGRRDSLR GFMDLANDNL PAPFFTLNQL KDRFKNVGLD 

       190        200        210        220        230        240 
RASDLVALSG GHTFGKNQCQ FIMDRLYNFS NTGLPDPTLD KSYLSTLRKQ CPRNGNQSVL 

       250        260        270        280        290        300 
VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDASD TLPLVREYAD GQGKFFDAFA 

       310        320        330        340 
KAMIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVEDAL EFASSM

« Hide

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References

« Hide 'large scale' references
[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: 12473102] [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. expand/collapse author list , 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. expand/collapse author list , 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]"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.

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Cross-references

Sequence databases

AF452387 mRNA. Translation: AAL40851.1.
AL161512 Genomic DNA. Translation: CAB78002.1.
AL161813 Genomic DNA. Translation: CAB82113.1.
AY136364 mRNA. Translation: AAM97030.1.
BT000180 mRNA. Translation: AAN15499.1.
IPIIPI00545315.
PIRB85088.
RefSeqNP_192617.1.
UniGeneAt.4181
At.54214

3D structure databases

HSSPHSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMRQ9LDN9. Positions 23-328.
ModBaseSearch...

Protein family/group databases

PeroxiBase203. AtPrx37.

Proteomic databases

PRIDEQ9LDN9.

Genome annotation databases

GeneID826447.
GenomeReviewsGene locus AT4G08770 in contig CT486007_GR.
KEGGath:AT4G08770.
NMPDRfig|3702.1.peg.18530.

Organism-specific databases

GeneFarm1864. 61.
TAIRAt4g08770.

Phylogenomic databases

OMAQ9LDN9. DIATTTI.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ9LDN9.
GermOnlineAT4G08770. Arabidopsis thaliana.

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePER37_ARATH
AccessionPrimary (citable) accession number: Q9LDN9
Secondary accession number(s): Q8L7B3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents