B9VAT0 · B9VAT0_9FLOR

  • 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. 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'.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site283Proton acceptor
Binding site284substrate
Binding site316substrate
Site323Transition state stabilizer
Binding site368substrate

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functionmagnesium ion binding
Molecular Functionmonooxygenase activity
Molecular Functionribulose-bisphosphate carboxylase activity
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

Encoded on

  • Plastid

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Rhodophyta > Florideophyceae > Rhodymeniophycidae > Gigartinales > Gigartinaceae > Chondracanthus

Accessions

  • Primary accession
    B9VAT0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue191N6-carboxylysine

Interaction

Subunit

Heterohexadecamer of 8 large chains and 8 small chains.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-134Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal
Domain144-451Ribulose 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
    474
  • Mass (Da)
    52,441
  • Last updated
    2009-03-24 v1
  • Checksum
    5D605E0F45475A1F
MSVRSGVFHAKMGYWDPDYVVKDTDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDSVPNTSDQYFAYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRAIAAAGETKGHYLNVTAATMEEMYERAEFAKELGSIIIMIDLVIGYTAIQTMAIWARKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIRGFYNTLLLPYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARNEGRDYVSEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTDTADFVETPTANV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FJ513458
EMBL· GenBank· DDBJ
ACM41030.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp