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Protein

Ribulose bisphosphate carboxylase small chain, chromosomal

Gene

cbxSC

Organism
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain, chromosomal (EC:4.1.1.39)
Short name:
RuBisCO small subunit
Gene namesi
Name:cbxSC
Synonyms:cbbS, cfxSC, rbcS
OrganismiCupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Taxonomic identifieri106590 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Ribulose bisphosphate carboxylase small chain, chromosomalPRO_0000198607Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

DIPiDIP-6120N.
STRINGi381666.H16_B1394.

Structurei

Secondary structure

1
139
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Helixi16 – 2813Combined sources
Beta strandi32 – 398Combined sources
Beta strandi49 – 535Combined sources
Helixi61 – 7414Combined sources
Beta strandi76 – 8510Combined sources
Turni87 – 893Combined sources
Beta strandi92 – 976Combined sources
Helixi102 – 1043Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi121 – 1266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70I/J/K/L1-139[»]
ProteinModelPortaliP09658.
SMRiP09658. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09658.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

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.

P09658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRITQGTFSF LPELTDEQIT KQLEYCLNQG WAVGLEYTDD PHPRNTYWEM
60 70 80 90 100
FGLPMFDLRD AAGILMEINN ARNTFPNHYI RVTAFDSTHT VESVVMSFIV
110 120 130
NRPADEPGFR LVRQEEPGRT LRYSIESYAV QARPEGSRY
Length:139
Mass (Da):16,143
Last modified:July 15, 1999 - v2
Checksum:iBDD2679F24897A1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17744 Genomic DNA. Translation: AAC28130.1.
PIRiB26954. RKALSE.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17744 Genomic DNA. Translation: AAC28130.1.
PIRiB26954. RKALSE.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70I/J/K/L1-139[»]
ProteinModelPortaliP09658.
SMRiP09658. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6120N.
STRINGi381666.H16_B1394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP09658.

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

  1. "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products."
    Andersen K., Caton J.
    J. Bacteriol. 169:4547-4558(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.
  2. Andersen K.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits."
    Hansen S., Vollan V.B., Hough E., Andersen K.
    J. Mol. Biol. 288:609-621(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.

Entry informationi

Entry nameiRBSC_CUPNE
AccessioniPrimary (citable) accession number: P09658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1999
Last modified: June 24, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.