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Protein

Ribulose bisphosphate carboxylase small chain

Gene

cbbS

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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

Enzyme and pathway databases

BioCyciSMEL266834:GJF6-3623-MONOMER.

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
Ordered Locus Names:RB0190
ORF Names:SMb20197
Encoded oniPlasmid pSymB (megaplasmid 2)0 Publication
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976 Componenti: Plasmid pSymB

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Ribulose bisphosphate carboxylase small chainPRO_0000198619Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

STRINGi266834.SM_b20197.

Structurei

3D structure databases

ProteinModelPortaliP58349.
SMRiP58349. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Phylogenomic databases

eggNOGiCOG4451.
KOiK01602.
OMAiYIPAVEF.
OrthoDBiEOG6RC3Q7.

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.

P58349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRITQGCFSF LPDLTDEQIT AQVQYCLGKG WAIGVEYTDD PHPRNTYWEM
60 70 80 90 100
WGNPMFDLKD AKGVMMELED CRKAHPQDYI RLNAFDSSRG LETVTMSFIV
110 120
NRPENEPSLR MTRTESNGRS QHYMWETQR
Length:129
Mass (Da):15,147
Last modified:November 16, 2001 - v1
Checksum:iB3A4DF100179F3FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591985 Genomic DNA. Translation: CAC48590.1.
PIRiF95865.
RefSeqiNP_436730.1. NC_003078.1.

Genome annotation databases

EnsemblBacteriaiCAC48590; CAC48590; SM_b20197.
GeneIDi1236521.
KEGGisme:SM_b20197.
PATRICi23636769. VBISinMel96828_5106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591985 Genomic DNA. Translation: CAC48590.1.
PIRiF95865.
RefSeqiNP_436730.1. NC_003078.1.

3D structure databases

ProteinModelPortaliP58349.
SMRiP58349. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266834.SM_b20197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC48590; CAC48590; SM_b20197.
GeneIDi1236521.
KEGGisme:SM_b20197.
PATRICi23636769. VBISinMel96828_5106.

Phylogenomic databases

eggNOGiCOG4451.
KOiK01602.
OMAiYIPAVEF.
OrthoDBiEOG6RC3Q7.

Enzyme and pathway databases

BioCyciSMEL266834:GJF6-3623-MONOMER.

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. "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti."
    Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.
    Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.

Entry informationi

Entry nameiRBS_RHIME
AccessioniPrimary (citable) accession number: P58349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: January 7, 2015
This is version 82 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

Complete proteome, Plasmid, Reference proteome

Documents

  1. 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.