Q9FM99 · ATCA8_ARATH

Function

function

Reversible hydration of carbon dioxide.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for active site, binding site.

138950100150200250300350
Type
IDPosition(s)Description
Active site204Proton acceptor
Binding site232Zn2+ (UniProtKB | ChEBI); catalytic
Binding site234Zn2+ (UniProtKB | ChEBI); catalytic
Binding site251Zn2+ (UniProtKB | ChEBI); catalytic
Binding site320-321substrate

GO annotations

AspectTerm
Cellular Componentchloroplast stroma
Molecular Functioncarbonate dehydratase activity
Molecular Functionzinc ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha carbonic anhydrase 8
  • EC number
  • Short names
    AtaCA8; AtalphaCA8
  • Alternative names
    • Alpha carbonate dehydratase 8

Gene names

    • Name
      ACA8
    • ORF names
      MCD7.6
    • Ordered locus names
      At5g56330

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FM99

Proteomes

Organism-specific databases

Subcellular Location

Note: Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_000042973423-389Alpha carbonic anhydrase 8
Disulfide bond163↔324
Glycosylation196N-linked (GlcNAc...) asparagine
Glycosylation385N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.

Keywords

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region21-153Disordered
Compositional bias24-129Pro residues
Domain138-374Alpha-carbonic anhydrase

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    389
  • Mass (Da)
    42,567
  • Last updated
    2015-07-22 v3
  • Checksum
    4F8BE5E07B8E75A9
MKISSLGWVLVLIFISITIVSSAPAPKPPKPKPAPAPTPPKPKPTPAPTPPKPKPKPAPTPPKPKPAPAPTPPKPKPAPAPTPPKPKPKPAPTPPNPKPTPAPTPPKPKPAPAPAPTPAPKPKPAPKPAPGGEVEDETEFSYETKGNKGPAKWGTLDAEWKMCGIGKMQSPIDLRDKNVVVSNKFGLLRSQYLPSNTTIKNRGHDIMLKFKGGNKGIGVTIRGTRYQLQQLHWHSPSEHTINGKRFALEEHLVHESKDKRYAVVAFLYNLGASDPFLFSLEKQLKKITDTHASEEHVGIIDPKKLSFESKHYYRYSGSLTAPPCSENVIWSVSKEIRTVSSKQVKLLRVAVHDASDSNARPLQAVNKRKVYLYKPKVKLMKKYCNISSY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8BGF7A0A1P8BGF7_ARATHACA8308

Sequence caution

The sequence AED96750.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence AED96750.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.
The sequence BAB11260.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BAB11260.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias24-129Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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.

Genome annotation databases

Similar Proteins

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