Reviewed,
UniProtKB/Swiss-Prot Q01MI9 (APX3_ORYSI)
Last modified
November 25, 2008.
Version 13.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Probable L-ascorbate peroxidase 3 EC=1.11.1.11 Alternative name(s): OsAPx03 | ||||
| Gene names |
| ||||
| Organism | Oryza sativa subsp. indica (Rice) | ||||
| Taxonomic identifier | 39946 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza |
Protein attributes
| Sequence length | 291 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Plays a key role in hydrogen peroxide removal By similarity. |
| Catalytic activity | L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group By similarity. Binds 1 potassium or calcium ion per subunit By similarity. |
| Subcellular location | Membrane; Single-pass membrane proteinPotential. |
| Sequence similarities | Belongs to the peroxidase family. Ascorbate peroxidase subfamily. |
| Caution | According to Ref.1, it may be peroxisomal. There is however no experimental evidence to prove this. |
Ontologies
Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Membrane |
| Domain | Transmembrane |
| Ligand | Calcium Heme Iron Metal-binding Potassium |
| Molecular function | Oxidoreductase Peroxidase |
Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW potassium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 291 | 291 | Probable L-ascorbate peroxidase 3 | PRO_0000300258 | |||||
Regions | |||||||||
| Transmembrane | 263 – 283 | 21 | Potential | ||||||
Sites | |||||||||
| Active site | 41 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 161 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Metal binding | 162 | 1 | Potassium or calcium By similarity | ||||||
| Metal binding | 178 | 1 | Potassium or calcium By similarity | ||||||
| Metal binding | 185 | 1 | Potassium or calcium By similarity | ||||||
| Site | 37 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome." Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M. J. Mol. Evol. 59:761-770(2004) [PubMed: 15599508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE. |
| [2] | "Sequence and analysis of rice chromosome 4." Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. Han B.Nature 420:316-320(2002) [PubMed: 12447439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Guang-Lu-Ai No.4. |
| [3] | "The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. Yang H.PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11. |
Cross-references
Sequence databases | |
|---|---|
| AY382617 mRNA. Translation: AAQ88105.1. CR855043 Genomic DNA. Translation: CAH66026.1. CM000129 Genomic DNA. Translation: EAY93142.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1APX based on UniProtKB P48534. |
| ModBase | Search... |
Organism-specific databases | |
| Gramene | Q6TY83. |
Family and domain databases | |
| InterPro | IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view] |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00459. ASPEROXIDASE. PR00458. PEROXIDASE. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | APX3_ORYSI | ||||||||
| Accession | Primary (citable) accession number: Q01MI9 Secondary accession number(s): A2XQN2, Q6TY83, Q7XWZ7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


