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Protein

Ribulose bisphosphate carboxylase small chain

Gene

cbbS

Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
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

Enzyme and pathway databases

BioCyciHNEA555778:GIVV-950-MONOMER.
BRENDAi4.1.1.39. 6349.

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:Hneap_0921
OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Taxonomic identifieri555778 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
ProteomesiUP000009102 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110Ribulose bisphosphate carboxylase small chainPRO_0000198631Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

STRINGi555778.Hneap_0921.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 184Combined sources
Helixi24 – 3613Combined sources
Beta strandi40 – 467Combined sources
Helixi48 – 503Combined sources
Beta strandi57 – 604Combined sources
Helixi69 – 8214Combined sources
Beta strandi86 – 949Combined sources
Turni95 – 984Combined sources
Beta strandi99 – 1079Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80M1-110[»]
ProteinModelPortaliP45686.
SMRiP45686. Positions 3-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45686.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
KOiK01602.
OMAiWNPAIEH.
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.

P45686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEMQDYKQS LKYETFSYLP PMNAERIRAQ IKYAIAQGWS PGIEHVEVKN
60 70 80 90 100
SMNQYWYMWK LPFFGEQNVD NVLAEIEACR SAYPTHQVKL VAYDNYAQSL
110
GLAFVVYRGN
Length:110
Mass (Da):12,855
Last modified:November 1, 1995 - v1
Checksum:i9C4F1AB8D29B104D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038430 Genomic DNA. Translation: AAC32550.1.
CP001801 Genomic DNA. Translation: ACX95764.1.
RefSeqiWP_012823800.1. NC_013422.1.

Genome annotation databases

EnsemblBacteriaiACX95764; ACX95764; Hneap_0921.
KEGGihna:Hneap_0921.
PATRICi32205716. VBIHalNea120669_0940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038430 Genomic DNA. Translation: AAC32550.1.
CP001801 Genomic DNA. Translation: ACX95764.1.
RefSeqiWP_012823800.1. NC_013422.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80M1-110[»]
ProteinModelPortaliP45686.
SMRiP45686. Positions 3-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi555778.Hneap_0921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACX95764; ACX95764; Hneap_0921.
KEGGihna:Hneap_0921.
PATRICi32205716. VBIHalNea120669_0940.

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
KOiK01602.
OMAiWNPAIEH.
OrthoDBiEOG6G20PM.

Enzyme and pathway databases

BioCyciHNEA555778:GIVV-950-MONOMER.
BRENDAi4.1.1.39. 6349.

Miscellaneous databases

EvolutionaryTraceiP45686.

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. "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth."
    Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.
    J. Bacteriol. 180:4133-4139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23641 / c2.
  3. "The structure of Halothiobacillus neapolitanus Rubisco."
    Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K., Yeates T.O.
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiRBS_HALNC
AccessioniPrimary (citable) accession number: P45686
Secondary accession number(s): D0KZ91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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.