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C5CPR2 (RBL_VARPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:Vapar_3032
OrganismVariovorax paradoxus (strain S110) [Complete proteome] [HAMAP]
Taxonomic identifier543728 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVariovorax

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

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" By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_1000214694

Sites

Active site1801Proton acceptor By similarity
Active site2981Proton acceptor By similarity
Metal binding2061Magnesium; via carbamate group By similarity
Metal binding2081Magnesium By similarity
Metal binding2091Magnesium By similarity
Binding site1281Substrate; in homodimeric partner By similarity
Binding site1781Substrate By similarity
Binding site1821Substrate By similarity
Binding site2991Substrate By similarity
Binding site3311Substrate By similarity
Binding site3831Substrate By similarity
Site3381Transition state stabilizer By similarity

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CPR2 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 7D8A9FC3516E2A80

FASTA48853,698
        10         20         30         40         50         60 
MGNMNEAIQI TDAKKRYSAG VLKYAQMGYW DGDYVPKDTD ILALFRITPQ EGVDAIEAAA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT ACDMYRAKAY KVEPVPNNPG QYFCYVAYDL SLFEEGSITN 

       130        140        150        160        170        180 
VTASIIGNVF SFKPLKAARL EDMKFPVAYV KTFPGPPTGI VVERERLDKF GRPLLGATTK 

       190        200        210        220        230        240 
PKLGLSGRNY GRVVYEGLRG GLDFMKDDEN INSQPFMHWR DRFLFVMDAV NKASAATGEV 

       250        260        270        280        290        300 
KGSYLNVTAG TMEEMYRRAQ FAKELGSVIV MVDLVIGYTA IQSMSNWCRQ NDMILHLHRA 

       310        320        330        340        350        360 
GHGTYTRQKN HGVSFRVIAK WMRLAGVDHI HAGTAVGKLE GDPMTVQGYY NVCRDTHTKV 

       370        380        390        400        410        420 
DLPRGIYFDQ DWGALRKVMP VASGGIHAGQ MHQLLDLFGD DVVLQFGGGT IGHPQGIQAG 

       430        440        450        460        470        480 
ATANRVALEA MVLARNEGRD IANEGPQILR DAAKWCTPLA AALDTWGEIS FNYASTDTSD 


YVPTPSVA 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile plant growth-promoting endophyte, Variovorax paradoxus S110."
Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G., O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C., Ovchinnikova G., Goodwin L., Han C.
J. Bacteriol. 193:1183-1190(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001635 Genomic DNA. Translation: ACS19651.1.
RefSeqYP_002944917.1. NC_012791.1.

3D structure databases

ProteinModelPortalC5CPR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING543728.Vapar_3032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS19651; ACS19651; Vapar_3032.
GeneID7973752.
KEGGvap:Vapar_3032.
PATRIC24006473. VBIVarPar36677_3025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycVPAR543728:GHLL-3061-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_VARPS
AccessionPrimary (citable) accession number: C5CPR2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families