A0A8T1YD65 · A0A8T1YD65_9BRAS
- Proteinperoxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids318 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 61 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 65 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 71 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 73 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 75 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 84 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 157 | substrate | ||||
Sequence: P | ||||||
Binding site | 187 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 188 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 238 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | vacuole | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameperoxidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionA0A8T1YD65
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MGLVRFFCSFLVFLSCLIAVYG | ||||||
Chain | PRO_5035728356 | 23-318 | peroxidase | |||
Sequence: QSTRIGFYSTTCPNAETIVQTTVASHFGSDPKVAPGLLRMHNHDCFVQGCDGSVLLSGPNSERTAGANVNLRGFEVIDDAKTQLEAACPGVVSCADILALAARDSVALTNGQSWQVPTGRRDGRVSLASNVNNLPSPSDSLAIQQRKFAAFRLNTRDLVALVGGHTIGTAACGFIMNRIFNSTGNIADPTMDQTFVPQLQRLCPQNGDGSARLDLDTGSGNTFDTSYFINLSRNRGILQSDHVLWTNPTTRPIVQEFMISTSNFNVQFARSMVKMSNIGVKTGRNGEIRRVCSAVN | ||||||
Disulfide bond | 34↔110 | |||||
Sequence: CPNAETIVQTTVASHFGSDPKVAPGLLRMHNHDCFVQGCDGSVLLSGPNSERTAGANVNLRGFEVIDDAKTQLEAAC | ||||||
Disulfide bond | 67↔72 | |||||
Sequence: CFVQGC | ||||||
Disulfide bond | 116↔314 | |||||
Sequence: CADILALAARDSVALTNGQSWQVPTGRRDGRVSLASNVNNLPSPSDSLAIQQRKFAAFRLNTRDLVALVGGHTIGTAACGFIMNRIFNSTGNIADPTMDQTFVPQLQRLCPQNGDGSARLDLDTGSGNTFDTSYFINLSRNRGILQSDHVLWTNPTTRPIVQEFMISTSNFNVQFARSMVKMSNIGVKTGRNGEIRRVC | ||||||
Disulfide bond | 194↔225 | |||||
Sequence: CGFIMNRIFNSTGNIADPTMDQTFVPQLQRLC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-318 | Plant heme peroxidase family profile | ||||
Sequence: STRIGFYSTTCPNAETIVQTTVASHFGSDPKVAPGLLRMHNHDCFVQGCDGSVLLSGPNSERTAGANVNLRGFEVIDDAKTQLEAACPGVVSCADILALAARDSVALTNGQSWQVPTGRRDGRVSLASNVNNLPSPSDSLAIQQRKFAAFRLNTRDLVALVGGHTIGTAACGFIMNRIFNSTGNIADPTMDQTFVPQLQRLCPQNGDGSARLDLDTGSGNTFDTSYFINLSRNRGILQSDHVLWTNPTTRPIVQEFMISTSNFNVQFARSMVKMSNIGVKTGRNGEIRRVCSAVN |
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)34,294
- Last updated2022-10-12 v1
- Checksum3794EA4B6D108FF0