Q9FG34 (PER54_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 95.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxidase 54 Short name=Atperox P54 EC=1.11.1.7 Alternative name(s): ATP29a | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Protein attributes
| Sequence length | 358 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Secreted Vacuole |
| Domain | Signal |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| PTM | Disulfide bond Glycoprotein Pyrrolidone carboxylic acid |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell vacuolar membraneInferred from direct assay. Source: TAIR |
| Molecular function | heme binding Inferred from electronic annotation. Source: InterPro peroxidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 31 | 31 | Potential | ||||||||
| Chain | 32 – 358 | 327 | Peroxidase 54 | PRO_0000023719 | |||||||
Sites | |||||||||||
| Active site | 73 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 74 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 77 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 79 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 81 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 83 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 200 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Metal binding | 201 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 252 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 255 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 260 | 1 | Calcium 2 By similarity | ||||||||
| Binding site | 170 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||||
| Site | 69 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 32 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||||
| Glycosylation | 34 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 44 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 103 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 161 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 166 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 178 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 218 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 228 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 242 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 298 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 42 ↔ 122 | By similarity | |||||||||
| Disulfide bond | 75 ↔ 80 | By similarity | |||||||||
| Disulfide bond | 128 ↔ 330 | By similarity | |||||||||
| Disulfide bond | 207 ↔ 239 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 21 | 1 | I → V in AAM66044. Ref.5 | ||||||||
| Sequence conflict | 28 | 1 | T → A in AAM66044. Ref.5 | ||||||||
| Sequence conflict | 189 | 1 | K → N in AAM66044. Ref.5 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases 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] | "Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] 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. Ecker J.R.Science 302:842-846(2003) [PubMed: 14593172] [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] | "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 (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 212-358. Strain: cv. Columbia. Tissue: Root. |
| [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 | AP002032 Genomic DNA. Translation: BAB09807.1. CP002688 Genomic DNA. Translation: AED91056.1. AK118827 mRNA. Translation: BAC43417.1. BT008584 mRNA. Translation: AAP40411.1. AY088509 mRNA. Translation: AAM66044.1. Y11794 mRNA. Translation: CAA72490.1. |
| IPI | IPI00528868. |
| RefSeq | NP_196291.1. NM_120756.2. |
| UniGene | At.90. |
3D structure databases | |
| ProteinModelPortal | Q9FG34. |
| SMR | Q9FG34. Positions 32-335. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9FG34. |
Protein family/group databases | |
| PeroxiBase | 220. AtPrx54. |
Proteomic databases | |
| PRIDE | Q9FG34. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT5G06730.1; AT5G06730.1; AT5G06730. |
| GeneID | 830562. |
| GenomeReviews | Gene locus AT5G06730 in contig BA000015_GR. |
| KEGG | ath:AT5G06730. |
| NMPDR | fig|3702.1.peg.22804. |
Organism-specific databases | |
| GeneFarm | 1908. 61. |
| TAIR | At5g06730. |
Phylogenomic databases | |
| GeneTree | EPGT00070000028241. |
| HOGENOM | HBG597790. |
| InParanoid | Q9FG34. |
| PhylomeDB | Q9FG34. |
| ProtClustDB | CLSN2686891. |
Gene expression databases | |
| ArrayExpress | Q9FG34. |
| Genevestigator | Q9FG34. |
| GermOnline | AT5G06730. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| KO | K00430. |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00458. PEROXIDASE. PR00461. PLPEROXIDASE. |
| SUPFAM | SSF48113. Peroxidase_super. 1 hit. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PER54_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9FG34 Secondary accession number(s): P93729 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with