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P54205 (RBL_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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·Interactions·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:slr0009
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length470 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trxAP522313EBI-862277,EBI-862916

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062655

Sites

Active site1701Proton acceptor By similarity
Active site2891Proton acceptor By similarity
Metal binding1961Magnesium; via carbamate group By similarity
Metal binding1981Magnesium By similarity
Metal binding1991Magnesium By similarity
Binding site1181Substrate; in homodimeric partner By similarity
Binding site1681Substrate By similarity
Binding site1721Substrate By similarity
Binding site2901Substrate By similarity
Binding site3221Substrate By similarity
Binding site3741Substrate By similarity
Site3291Transition state stabilizer By similarity

Amino acid modifications

Modified residue1961N6-carboxylysine By similarity
Disulfide bond242Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
P54205 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 45B9322482745B2B

FASTA47052,491
        10         20         30         40         50         60 
MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA AVAAESSTGT 

        70         80         90        100        110        120 
WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL DLFEEGSVTN VLTSLVGNVF 

       130        140        150        160        170        180 
GFKALRALRL EDIRFPVALI KTFQGPPHGI TVERDKLNKY GRPLLGCTIK PKLGLSAKNY 

       190        200        210        220        230        240 
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG 

       250        260        270        280        290        300 
TCEEMMKRAE FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 

       310        320        330        340        350        360 
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE EDRSRGIFFT 

       370        380        390        400        410        420 
QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE 

       430        440        450        460        470 
ACVQARNEGR NLAREGNDVI REACRWSPEL AAACELWKEI KFEFEAMDTL 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a Synechocystis PCC6803 mutant suitable for the study of variant hexadecameric ribulose bisphosphate carboxylase/oxygenase enzymes."
Amichay D., Levitz R., Gurevitz M.
Plant Mol. Biol. 23:465-476(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[3]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65960 Genomic DNA. Translation: CAA46773.1.
BA000022 Genomic DNA. Translation: BAA10190.1.
PIRS39561.
RefSeqNP_442120.1. NC_000911.1.
YP_005652178.1. NC_017277.1.
YP_007451997.1. NC_020286.1.

3D structure databases

ProteinModelPortalP54205.
SMRP54205. Positions 6-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP54205. 4 interactions.
STRING1148.slr0009.

Proteomic databases

PaxDbP54205.
PRIDEP54205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10190; BAA10190; BAA10190.
GeneID952593.
KEGGsyn:slr0009.
syy:SYNGTS_2225.
syz:MYO_122490.
PATRIC23841842. VBISynSp132158_2465.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.
PhylomeDBP54205.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-750.
SABIO-RKP54205.

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_SYNY3
AccessionPrimary (citable) accession number: P54205
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families