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Protein

Ribulose bisphosphate carboxylase small chain

Gene

cbbS

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

GO - Molecular functioni

  1. monooxygenase activity Source: UniProtKB-KW
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Enzyme and pathway databases

BioCyciSELO269084:GCDQ-134-MONOMER.
SABIO-RKP04716.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain (EC:4.1.1.39)
Short name:
RuBisCO small subunit
Gene namesi
Name:cbbS
Synonyms:rbcS
Ordered Locus Names:syc0129_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001175: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 111110Ribulose bisphosphate carboxylase small chainPRO_0000198624Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

DIPiDIP-6211N.
STRINGi269084.syc0129_c.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni14 – 174Combined sources
Helixi23 – 3614Combined sources
Beta strandi39 – 468Combined sources
Beta strandi56 – 605Combined sources
Helixi68 – 8114Combined sources
Beta strandi85 – 939Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1069Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/W12-58[»]
C/F/I/J/M/P/T/W102-110[»]
ProteinModelPortaliP04716.
SMRiP04716. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04716.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 2110Hydrophobic

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
KOiK01602.
OMAiYIPAVEF.
OrthoDBiEOG6G20PM.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04716-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP
60 70 80 90 100
EEFYWTMWKL PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT
110
VSFIVHRPGR Y
Length:111
Mass (Da):13,333
Last modified:January 23, 2007 - v3
Checksum:iF854F73FA70BD57B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03220 Genomic DNA. Translation: CAA26973.1.
AP008231 Genomic DNA. Translation: BAD78319.1.
PIRiS07351. RKYCS.
RefSeqiWP_011242443.1. NC_006576.1.
YP_170839.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD78319; BAD78319; syc0129_c.
GeneIDi3200023.
KEGGisyc:syc0129_c.
PATRICi32485753. VBISynElo117686_0155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03220 Genomic DNA. Translation: CAA26973.1.
AP008231 Genomic DNA. Translation: BAD78319.1.
PIRiS07351. RKYCS.
RefSeqiWP_011242443.1. NC_006576.1.
YP_170839.1. NC_006576.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/W12-58[»]
C/F/I/J/M/P/T/W102-110[»]
ProteinModelPortaliP04716.
SMRiP04716. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6211N.
STRINGi269084.syc0129_c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD78319; BAD78319; syc0129_c.
GeneIDi3200023.
KEGGisyc:syc0129_c.
PATRICi32485753. VBISynElo117686_0155.

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
KOiK01602.
OMAiYIPAVEF.
OrthoDBiEOG6G20PM.

Enzyme and pathway databases

BioCyciSELO269084:GCDQ-134-MONOMER.
SABIO-RKP04716.

Miscellaneous databases

EvolutionaryTraceiP04716.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiRBS_SYNP6
AccessioniPrimary (citable) accession number: P04716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.