Q9FM99 · ATCA8_ARATH
- ProteinAlpha carbonic anhydrase 8
- GeneACA8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids389 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Reversible hydration of carbon dioxide.
Catalytic activity
- hydrogencarbonate + H+ = CO2 + H2O
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 204 | Proton acceptor | |||
Binding site | 232 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 234 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 251 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 320-321 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Molecular Function | carbonate dehydratase activity | |
Molecular Function | zinc ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha carbonic anhydrase 8
- EC number
- Short namesAtaCA8; AtalphaCA8
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FM99
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-22 | ||||
Chain | PRO_0000429734 | 23-389 | Alpha carbonic anhydrase 8 | ||
Disulfide bond | 163↔324 | ||||
Glycosylation | 196 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 385 | N-linked (GlcNAc...) asparagine | |||
Post-translational modification
N-glycosylated.
Keywords
- PTM
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 21-153 | Disordered | |||
Compositional bias | 24-129 | Pro residues | |||
Domain | 138-374 | Alpha-carbonic anhydrase | |||
Sequence similarities
Belongs to the alpha-class carbonic anhydrase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length389
- Mass (Da)42,567
- Last updated2015-07-22 v3
- Checksum4F8BE5E07B8E75A9
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BGF7 | A0A1P8BGF7_ARATH | ACA8 | 308 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 24-129 | Pro residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB009049 EMBL· GenBank· DDBJ | BAB11260.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED96750.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |