Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A7T0IGD0 · A0A7T0IGD0_NEOHI

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'.

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.

Type
IDPosition(s)Description
Binding site115substrate; in homodimeric partner
Binding site165substrate
Active site167Proton acceptor
Binding site169substrate
Binding site193Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site195Mg2+ (UniProtKB | ChEBI)
Binding site196Mg2+ (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 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
    A0A7T0IGD0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue193N6-carboxylysine

Interaction

Subunit

Heterohexadecamer of 8 large chains and 8 small chains.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-136Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal
Domain148-453Ribulose 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
    Fragment
  • Length
    476
  • Mass (Da)
    52,586
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    8F70D538CEA03208D2F00A12E8D436AC
SERYESGVIPYAKMGYWDADYVIKETDVLALFRITPQPGVDPIEASAAIAGESSTATWTVVWTDLLTACDLYRAKAYRVDPVPNVADQYFAYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRMPVAYLKTFQGPATGLIVERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWKERFLYSMEGVNKASAAAGEIKGHYLNVTAATMEDMYERAEFSKEVGSIICMIDLVVGYTAIQTMAIWARKHDMILHLHRAGNSTYSRQKNHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLESETDINLPQGLFFAQNWASLRKVVPVASGGTHAGQMHQLLDYLGDDVVLQFGGGTIGHPDGVQAGATANRVALESMVMARNEGRNYVAEGPQILRDAAKTCGPLQTALDLWKDISFNYTSTDTADFVETPTANI

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MT025697
EMBL· GenBank· DDBJ
QPK40925.1
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.
Help