Q9MVE5 · RBL_TAXDI

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 (By similarity).

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' (By similarity).

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

Accessions

  • Primary accession
    Q9MVE5

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
PropeptidePRO_00002657461-2
Modified residue3N-acetylproline
ChainPRO_00002657473-475Ribulose bisphosphate carboxylase large chain
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 (By similarity).

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    475
  • Mass (Da)
    52,792
  • Last updated
    2000-10-01 v1
  • Checksum
    EF06A2377FD2F56E
MSPQTETKASVGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPLPGEESQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQRIHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREVTLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREATKWSPELAAACEVWKEIKFEFDTIDRL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict21in Ref. 2
Sequence conflict30in Ref. 2

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF119185
EMBL· GenBank· DDBJ
AAF34889.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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