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Q8DIS5 (RBL_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:tll1506
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 475475Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062649

Sites

Active site1751Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2011Magnesium; via carbamate group By similarity
Metal binding2031Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site1231Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site1771Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue2011N6-carboxylysine By similarity
Disulfide bond247Interchain; in linked form By similarity

Secondary structure

......................................................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8DIS5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B4A97CD4D6A3EB91

FASTA47553,025
        10         20         30         40         50         60 
MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF EEAAAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY IAYPLDLFEE GSVTNMLTSI 

       130        140        150        160        170        180 
VGNVFGFKAL KALRLEDLRI PVAYLKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL 

       250        260        270        280        290        300 
NVTAPTCEEM LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV 

       310        320        330        340        350        360 
MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR ENYIEQDRSR 

       370        380        390        400        410        420 
GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL QFGGGTLGHP WGNAPGATAN 

       430        440        450        460        470 
RVALEACIQA RNEGRDLMRE GGDIIREAAR WSPELAAACE LWKEIKFEFE AQDTI 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC09058.1.
RefSeqNP_682296.1. NC_004113.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBVX-ray2.30A/C/E/G/I/K/M/O1-475[»]
3ZXWX-ray2.10A/C/E/G1-475[»]
ProteinModelPortalQ8DIS5.
SMRQ8DIS5. Positions 12-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll1506.

Proteomic databases

PRIDEQ8DIS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC09058; BAC09058; BAC09058.
GeneID1011208.
KEGGtel:tll1506.
PATRIC23928370. VBITheElo119873_1580.

Phylogenomic databases

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

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_THEEB
AccessionPrimary (citable) accession number: Q8DIS5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 72 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references