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Q2JV67 (RBL_SYNJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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
Synonyms:rbcL
Ordered Locus Names:CYA_1194
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length474 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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

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 By similarity. HAMAP-Rule MF_01338

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 – 474474Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251461

Sites

Active site1741Proton acceptor By similarity
Active site2931Proton acceptor By similarity
Metal binding2001Magnesium; via carbamate group By similarity
Metal binding2021Magnesium By similarity
Metal binding2031Magnesium By similarity
Binding site1221Substrate; in homodimeric partner By similarity
Binding site1721Substrate By similarity
Binding site1761Substrate By similarity
Binding site2941Substrate By similarity
Binding site3261Substrate By similarity
Binding site3781Substrate By similarity
Site3331Transition state stabilizer By similarity

Amino acid modifications

Modified residue2001N6-carboxylysine By similarity
Disulfide bond246Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JV67 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 55B14AF7F6EDCFD2

FASTA47452,804
        10         20         30         40         50         60 
MAYSATQTKK GYQAGVKDYR LTYYTPDYTP KDTDVLACFR VTPQPGVPPE EAGAAVAAES 

        70         80         90        100        110        120 
STGTWTTVWT DLLTDLDRYK GRCYDIEPVP GEENQYFCFV AYPLDLFEEG SVTNMLTSIV 

       130        140        150        160        170        180 
GNVFGFKALK ALRLEDVRIP VAYLKTFQGP PHGIQVERDK LNKYGRPLLG CTIKPKLGLS 

       190        200        210        220        230        240 
AKNYGRAVYE ALRGGLDFTK DDENINSQPF QRWRDRYLFV MEAVHKAQAE TGEIKGHYLN 

       250        260        270        280        290        300 
VTAPTCEEMF KRAEFAKEIG APIIMHDYLT AGFTANTSLA KWCRDNGILL HIHRAMHAVI 

       310        320        330        340        350        360 
DRQKNHGIHF RVLAKCLRMS GGDHLHAGTV VGKLEGDRAI TMGFVDLMRE NYVEADRSRG 

       370        380        390        400        410        420 
IFFTQDWASM PGVMPVASGG IHVWHMPALV EIFGDDAVLQ FGGGTLGHPW GNAPGATANR 

       430        440        450        460        470 
VALEACIQAR NEGRDLAREG NEIIREAAKW SPELAAACEL WKEIKFEFKP VDTL 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000239 Genomic DNA. Translation: ABC99380.1.
RefSeqYP_474643.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JV67.
SMRQ2JV67. Positions 11-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321327.CYA_1194.

Proteomic databases

PRIDEQ2JV67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC99380; ABC99380; CYA_1194.
GeneID3898903.
KEGGcya:CYA_1194.
PATRIC23810659. VBISynSp90045_1183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP321327:GHFX-1188-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_SYNJA
AccessionPrimary (citable) accession number: Q2JV67
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 56 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