Q59462 · RBL2_HYDMR

  • Protein
    Ribulose bisphosphate carboxylase
  • Gene
    cbbM
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Kinetics

Vmax pH TEMPERATURE[C] NOTES EVIDENCE
0.003 μmol/min/mgwith CO2 as substrate, expressed in E.coli
The CO2/O2 specificity factor (tau) is 14.8.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site116substrate; in homodimeric partner
Active site171Proton acceptor
Binding site173substrate
Binding site196Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site198Mg2+ (UniProtKB | ChEBI)
Binding site199Mg2+ (UniProtKB | ChEBI)
Active site294Proton acceptor
Binding site295substrate
Binding site328substrate
Site336Transition state stabilizer
Binding site375substrate

GO annotations

AspectTerm
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
  • EC number
  • Short names
    RuBisCO

Gene names

    • Name
      cbbM
    • Synonyms
      cbbL-3

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 11271 / JCM 7688 / MH-110
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Piscirickettsiaceae > Hydrogenovibrio

Accessions

  • Primary accession
    Q59462
  • Secondary accessions
    • Q75W26

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000626622-463Ribulose bisphosphate carboxylase
Modified residue196N6-carboxylysine

Expression

Induction

mRNA expression is constant at all CO2 concentrations tested, however more protein accumulates at 15% and 2% CO2 than at 0.15% and 0.03% CO2 (at protein level).

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    50,729
  • Last updated
    2007-01-23 v3
  • Checksum
    A7F8E289FF92E996
MDQSNRYADLTLTEEKLVADGNHLLVAYRLKPAAGYGFLEVAAHVAAESSTGTNVEVSTTDDFTRGVDALVYEIDEAAFGDKGGLMKIAYPVDLFDPNLIDGHYNVSHMWSLILGNNQGMGDHEGLRMLDFLVPEKMVKRFDGPATDISDLWKVLGRPEVDGGYIAGTIIKPKLGLRPEPFAKACYDFWLGGDFIKNDEPQANQNFCPMEVVIPKVAEAMDRAQQATGQAKLFSANVTADFHEEMIKRGEYVLGEFAKYGNEKHVAFLVDGFVTGPAGVTTSRRAFPDTYLHFHRAGHGAVTSYKSPMGMDPLCYMKLARLMGASGIHTGTMGYGKMEGHNDERVLAYMLERDECQGPYFYQKWYGMKPTTPIISGGMDALRLPGFFENLGHGNVINTCGGGSFGHIDSPAAGGISLGQAYACWKTGAEPIEAPREFARAFESFPGDADKIFPGWREKLGVHK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict379in Ref. 3; BAD15326
Sequence conflict422in Ref. 3; BAD15326
Sequence conflict429in Ref. 3; BAD15326
Sequence conflict433-435in Ref. 3; BAD15326

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D28135
EMBL· GenBank· DDBJ
BAA05677.1
EMBL· GenBank· DDBJ
Genomic DNA
AB122071
EMBL· GenBank· DDBJ
BAD15326.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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