P28433 · RBL_NELCA

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 site113substrate; in homodimeric partner
Binding site163substrate
Active site165Proton acceptor
Binding site167substrate
Binding site191Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site193Mg2+ (UniProtKB | ChEBI)
Binding site194Mg2+ (UniProtKB | ChEBI)
Active site284Proton acceptor
Binding site285substrate
Binding site317substrate
Site324Transition state stabilizer
Binding site369substrate

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
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Acanthaceae > Nelsonioideae > Nelsonia

Accessions

  • Primary accession
    P28433

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000625371-466Ribulose bisphosphate carboxylase large chain
Modified residue4N6,N6,N6-trimethyllysine
Modified residue191N6-carboxylysine
Disulfide bond237Interchain; 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.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    466
  • Mass (Da)
    51,626
  • Last updated
    1992-12-01 v1
  • Checksum
    913144ED9C0627BD
VGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVPGEADQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAAEGNTIIREASKWSPELAAACEVWKEIKFEFKAVDTLD

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L01935
EMBL· GenBank· DDBJ
AAA84501.2
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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