P69571 · RBL_PSEMZ

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.

Type
IDPosition(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
    P69571
  • Secondary accessions
    • P17249
    • P85933

Subcellular Location

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    475
  • Mass (Da)
    52,728
  • Last updated
    2005-03-29 v1
  • MD5 Checksum
    3617039FBF2B7AD64C9D4ECC3B8663F4
MSPKTETKASVGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEAVPGEESQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQRNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDVTLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREATKWSPELAAACEVWKEIKFEFDTIDYL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X52937
EMBL· GenBank· DDBJ
CAA37107.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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