P28425 · RBL_HYDVI

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 site114substrate; in homodimeric partner
Binding site164substrate
Active site166Proton acceptor
Binding site168substrate
Binding site192Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site194Mg2+ (UniProtKB | ChEBI)
Binding site195Mg2+ (UniProtKB | ChEBI)
Active site285Proton acceptor
Binding site286substrate
Binding site318substrate
Site325Transition state stabilizer
Binding site370substrate

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 > Boraginales > Hydrophyllaceae > Hydrophyllum

Accessions

  • Primary accession
    P28425

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_00000624941-467Ribulose bisphosphate carboxylase large chain
Modified residue5N6,N6,N6-trimethyllysine
Modified residue192N6-carboxylysine
Disulfide bond238Interchain; 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
    467
  • Mass (Da)
    51,905
  • Last updated
    1992-12-01 v1
  • Checksum
    AFD680117497BD9B
SVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIDPVLGEEDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRLLFCAEAIFKSQAETGEIKGHYLNATAGNCEEMMKRAVFARELGVPIVMHDYLTGGFTANTTLASYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERNITLSFVVLLRDDYIEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQARNEGRDLAREGNDIIREACKWSPELAAACEVWKEIKFEFTDMDTLD

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L01927
EMBL· GenBank· DDBJ
AAA84324.2
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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