A0A7U3VIU7 · A0A7U3VIU7_9LILI

  • Protein
    Ribulose bisphosphate carboxylase large chain
  • Gene
    rbcL
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 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

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Dioscoreales > Dioscoreaceae > Dioscorea

Accessions

  • Primary accession
    A0A7U3VIU7

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.

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    53,835
  • Last updated
    2021-06-02 v1
  • Checksum
    672F644D727641BB
MSCKEELMSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIETVVGEEDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALFKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEYKPVDTLDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MT906794
EMBL· GenBank· DDBJ
QQP00829.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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