A0A286KLS0 · A0A286KLS0_9MAGN

  • Protein
    Ribulose bisphosphate carboxylase large chain
  • Gene
    rbcL
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site123substrate; in homodimeric partner
Binding site173substrate
Active site175Proton acceptor
Binding site177substrate
Binding site201Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site203Mg2+ (UniProtKB | ChEBI)
Binding site204Mg2+ (UniProtKB | ChEBI)
Active site294Proton acceptor
Binding site295substrate
Binding site327substrate
Site334Transition state stabilizer
Binding site379substrate

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functionmagnesium ion binding
Molecular Functionmonooxygenase activity
Molecular Functionribulose-bisphosphate carboxylase activity
Biological Processphotorespiration
Biological Processreductive pentose-phosphate cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribulose bisphosphate carboxylase large chain
  • EC number
  • Short names
    RuBisCO large subunit

Gene names

    • Name
      rbcL

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Ranunculales > Ranunculaceae > Ranunculoideae > Delphinieae > Aconitum

Accessions

  • Primary accession
    A0A286KLS0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, disulfide bond.

TypeIDPosition(s)Description
Modified residue14N6,N6,N6-trimethyllysine
Modified residue201N6-carboxylysine
Disulfide bond247Interchain; in linked form

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.

Keywords

Interaction

Subunit

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain24-144Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal
Domain154-462Ribulose bisphosphate carboxylase large subunit C-terminal

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    475
  • Mass (Da)
    52,717
  • Last updated
    2017-11-22 v1
  • Checksum
    181F167C2C72D2F5
MSPQTETKASVGFKAGVKDYKLNYYTPEYAPKDTDTLAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAREGNEIIREACKWSLELAAACEVWKEIKFEFEAMDTL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KY407561
EMBL· GenBank· DDBJ
AQY56136.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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