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P04716 (RBS_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain

Short name=RuBisCO small subunit
EC=4.1.1.39
Gene names
Name:cbbS
Synonyms:rbcS
Ordered Locus Names:syc0129_c
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length111 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Both reactions occur simultaneously and in competition at the same active site.

Catalytic activity

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

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

Subunit structure

8 large chains + 8 small chains.

Sequence similarities

Belongs to the RuBisCO small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 111110Ribulose bisphosphate carboxylase small chain
PRO_0000198624

Regions

Region12 – 2110Hydrophobic

Secondary structure

............. 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04716 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F854F73FA70BD57B

FASTA11113,333
        10         20         30         40         50         60 
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP EEFYWTMWKL 

        70         80         90        100        110 
PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT VSFIVHRPGR Y 

« Hide

References

« Hide 'large scale' references
[1]"The gene for the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase is located close to the gene for the large subunit in the cyanobacterium Anacystis nidulans 6301."
Shinozaki K., Sugiura M.
Nucleic Acids Res. 11:6957-6963(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genes for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase constitute a single operon in a cyanobacterium Anacystis nidulans 6301."
Shinozaki K., Sugiura M.
Mol. Gen. Genet. 200:27-32(1985)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[4]"The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution."
Newman J., Gutteridge S.
J. Biol. Chem. 268:25876-25886(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate."
Newman J., Gutteridge S.
Structure 2:495-502(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03220 Genomic DNA. Translation: CAA26973.1.
AP008231 Genomic DNA. Translation: BAD78319.1.
PIRRKYCS. S07351.
RefSeqYP_170839.1. NC_006576.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RBLX-ray2.20I/J/K/L/M/N/O/P2-110[»]
1RSCX-ray2.30I/J/K/L/M/N/O/P1-111[»]
1UZHX-ray2.20C/F/I/J/M/P/T/W47-53[»]
ProteinModelPortalP04716.
SMRP04716. Positions 2-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6211N.
STRING269084.syc0129_c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD78319; BAD78319; syc0129_c.
GeneID3200023.
KEGGsyc:syc0129_c.
PATRIC32485753. VBISynElo117686_0155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4451.
HOGENOMHOG000141332.
KOK01602.
OMAMFDLKDA.
OrthoDBEOG6G20PM.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-134-MONOMER.
SABIO-RKP04716.

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamPF00101. RuBisCO_small. 1 hit.
[Graphical view]
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04716.

Entry information

Entry nameRBS_SYNP6
AccessionPrimary (citable) accession number: P04716
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 106 of the entry and version 3 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