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Q96518 (PER16_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidase 16
Short name=Atperox P16
EC=1.11.1.7
Alternative name(s):
ATP22a
Gene names
Name:PER16
Synonyms:P16
Ordered Locus Names:At2g18980
ORF Names:F19F24.18
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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 By similarity.

Tissue specificity

Expressed in the whole plant, but preferentially in roots and leaves. Ref.6

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 323300Peroxidase 16
PRO_0000023682

Sites

Active site651Proton acceptor By similarity
Metal binding661Calcium 1 By similarity
Metal binding691Calcium 1; via carbonyl oxygen By similarity
Metal binding711Calcium 1; via carbonyl oxygen By similarity
Metal binding731Calcium 1 By similarity
Metal binding751Calcium 1 By similarity
Metal binding1911Iron (heme axial ligand) By similarity
Metal binding1921Calcium 2 By similarity
Metal binding2431Calcium 2 By similarity
Metal binding2461Calcium 2 By similarity
Metal binding2511Calcium 2 By similarity
Binding site1611Substrate; via carbonyl oxygen By similarity
Site611Transition state stabilizer By similarity

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid By similarity
Disulfide bond34 ↔ 113 By similarity
Disulfide bond67 ↔ 72 By similarity
Disulfide bond119 ↔ 319 By similarity
Disulfide bond198 ↔ 230 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96518 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: 43880AD393482989

FASTA32335,832
        10         20         30         40         50         60 
MKNQSSFSIV ALLLIFFSSS VFAQLQTNFY RKSCPNVETI VRNAVRQKFQ QTFVTAPATL 

        70         80         90        100        110        120 
RLFFHDCFVR GCDASILLAS PSEKDHPDDK SLAGDGFDTV AKAKQALDRD PNCRNKVSCA 

       130        140        150        160        170        180 
DILALATRDV VVLTGGPNYP VELGRRDGRL STVASVQHSL PQPSFKLDQL NTMFARHGLS 

       190        200        210        220        230        240 
QTDMIALSGA HTIGFAHCGK FSKRIYNFSP KRPIDPTLNI RYALQLRQMC PIRVDLRIAI 

       250        260        270        280        290        300 
NMDPTSPNTF DNAYFKNLQK GMGLFTSDQV LFSDERSRST VNSFASSEAT FRQAFISAIT 

       310        320 
KLGRVGVKTG NAGEIRRDCS RVN

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [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]"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]"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 (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-323.
Strain: cv. Columbia.
[5]"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: 9738941] [Abstract]
Cited for: CHARACTERIZATION.
Strain: cv. Columbia.
[6]"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.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC003673 Genomic DNA. Translation: AAC09031.1.
CP002685 Genomic DNA. Translation: AEC06835.1.
BT003082 mRNA. Translation: AAO23647.1.
Y08781 mRNA. Translation: CAA70034.1.
IPIIPI00527019.
PIRT01626.
RefSeqNP_179488.1. NM_127455.3.
UniGeneAt.86.

3D structure databases

ProteinModelPortalQ96518.
SMRQ96518. Positions 24-323.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96518.

Protein family/group databases

PeroxiBase97. AtPrx16.

Proteomic databases

PRIDEQ96518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G18980.1; AT2G18980.1; AT2G18980.
GeneID816415.
GenomeReviewsGene locus AT2G18980 in contig CT485783_GR.
KEGGath:AT2G18980.
NMPDRfig|3702.1.peg.8895.

Organism-specific databases

GeneFarm1840. 61.
TAIRAt2g18980.

Phylogenomic databases

GeneTreeEPGT00050000003677.
HOGENOMHBG597790.
InParanoidQ96518.
OMARIDPTLN.
PhylomeDBQ96518.
ProtClustDBCLSN2683069.

Gene expression databases

ArrayExpressQ96518.
GenevestigatorQ96518.
GermOnlineAT2G18980. Arabidopsis thaliana.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
KOK00430.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER16_ARATH
AccessionPrimary (citable) accession number: Q96518
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 1, 1998
Last modified: December 14, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents