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Protein

Ribulose bisphosphate carboxylase small chain

Gene

cbbS

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed-Annotation score: Annotation score: 2 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, Photosynthesis

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
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118118Ribulose bisphosphate carboxylase small chainPRO_0000198621Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

3D structure databases

ProteinModelPortaliO32741.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Phylogenomic databases

HOGENOMiHOG000141332.

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.

O32741-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVQDYPSR LSRPESRKMG TFSYLPPMGE AEIRRQVEWI VKNGWNPGIE
60 70 80 90 100
HTEPDFAAQI YWYMWKLPMF GETDVDAILA ELKACHEANP GHHVRLIGYD
110
NFTQSQGANM IVYRGTAV
Length:118
Mass (Da):13,548
Last modified:January 1, 1998 - v1
Checksum:i59BC06D008370315
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L82000 Genomic DNA. Translation: AAC37142.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L82000 Genomic DNA. Translation: AAC37142.1.

3D structure databases

ProteinModelPortaliO32741.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000141332.

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. Shively J.M.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiRBS_RHOCA
AccessioniPrimary (citable) accession number: O32741
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 1, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.