D4PBB9 · D4PBB9_PHODC

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. 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 site130substrate; in homodimeric partner
Binding site180substrate
Active site182Proton acceptor
Binding site184substrate
Binding site208Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site210Mg2+ (UniProtKB | ChEBI)
Binding site211Mg2+ (UniProtKB | ChEBI)
Active site301Proton acceptor
Binding site302substrate
Binding site334substrate
Site341Transition state stabilizer
Binding site386substrate

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
    • Synonyms
      cbbL
    • ORF names
      PhdaC_p029

Encoded on

  • Plastid

Organism names

  • Taxonomic identifier
  • Strains
    • DP00001
    • K2
    • N1
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Arecaceae > Coryphoideae > Phoeniceae > Phoenix

Accessions

  • Primary accession
    D4PBB9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, disulfide bond.

TypeIDPosition(s)Description
Modified residue21N6,N6,N6-trimethyllysine
Modified residue208N6-carboxylysine
Disulfide bond254Interchain; 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
Domain31-151Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal
Domain161-469Ribulose bisphosphate carboxylase large subunit C-terminal

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    53,735
  • Last updated
    2010-05-18 v1
  • Checksum
    2E73F276493DA222
MSCREGLMSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIETVVGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAMCARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKAIKFEFEPVDKLDK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GU811709
EMBL· GenBank· DDBJ
ADD63179.1
EMBL· GenBank· DDBJ
Genomic DNA
FJ212316
EMBL· GenBank· DDBJ
ADF28154.1
EMBL· GenBank· DDBJ
Genomic DNA
MF176947
EMBL· GenBank· DDBJ
ATG83023.1
EMBL· GenBank· DDBJ
Genomic DNA
MF197494
EMBL· GenBank· DDBJ
AXA13203.1
EMBL· GenBank· DDBJ
Genomic DNA
MF197495
EMBL· GenBank· DDBJ
AXA13289.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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