A0A1B7VW33 · A0A1B7VW33_APHFL

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'.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site124substrate; in homodimeric partner
Binding site174substrate
Active site176Proton acceptor
Binding site178substrate
Binding site202Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site204Mg2+ (UniProtKB | ChEBI)
Binding site205Mg2+ (UniProtKB | ChEBI)
Active site295Proton acceptor
Binding site296substrate
Binding site328substrate
Site335Transition state stabilizer
Binding site380substrate

GO annotations

AspectTerm
Cellular Componentcarboxysome
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
    • Synonyms
      cbbL
    • ORF names
      AN481_11755

Organism names

Accessions

  • Primary accession
    A0A1B7VW33

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, disulfide bond.

Type
IDPosition(s)Description
Modified residue202N6-carboxylysine
Disulfide bond248Interchain; 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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-145Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal
Domain155-463Ribulose 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
    476
  • Mass (Da)
    53,083
  • Last updated
    2016-11-02 v1
  • Checksum
    C22240EE1EE2910F
MSYAQTKTQAKSGYQAGVKDYRLTYYTPDYTPKDTDLLAAFRMTPQPGVPPEEAGAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQYICYVAYPLDLFEEGSITNVLTSIVGNVFGFKALRALRLEDIRFPVAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSAPFQRWRDRFLFVSEAINKAQAETGEIKGHYLNVTAPTCEQMIQRAEYAKELKQPIIMHDYLTAGFTANTTLARWCRDNGILLHIHRAMHAVIDRQKNHGIHFRVLAKALRLSGGDHIHTGTVVGKLEGERGITMGFVDLLRENYVEQDKSRGIYFTQDWASLPGVMAVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEAVVQARNEGRNLAREGNDIIREAAKWSPELAVACELWKEIKFEFEAMDTV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LJOY01000036
EMBL· GenBank· DDBJ
OBQ25133.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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