P48706 · RBL_LACSA

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
  • Strains
    • cv. Cisco
    • cv. Salinas
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Cichorioideae > Cichorieae > Lactucinae > Lactuca

Accessions

  • Primary accession
    P48706
  • Secondary accessions
    • Q1KXL5
    • Q5EKL5

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
PropeptidePRO_00000312711-2
Modified residue3N-acetylproline
ChainPRO_00000312723-477Ribulose 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.

Structure

Family & Domains

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    477
  • Mass (Da)
    52,895
  • Last updated
    2006-01-24 v2
  • Checksum
    9F0F8F9D9E4080CA
MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIFKSQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLATEGNEIIREATKWSPELAAACEVWKEIKFEFQAMDTLDQ

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict136in Ref. 1; AAB01595
Sequence conflict140-142in Ref. 1; AAB01595
Sequence conflict146in Ref. 1; AAB01595
Sequence conflict412in Ref. 1; AAB01595

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L14073
EMBL· GenBank· DDBJ
AAB01595.1
EMBL· GenBank· DDBJ
Unassigned DNA
AY874437
EMBL· GenBank· DDBJ
AAW78411.1
EMBL· GenBank· DDBJ
Genomic DNA
AP007232
EMBL· GenBank· DDBJ
BAE47602.1
EMBL· GenBank· DDBJ
Genomic DNA
DQ383816
EMBL· GenBank· DDBJ
ABD47241.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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