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Protein

Ribulose bisphosphate carboxylase small chain

Gene

rbcS

Organism
Thalassiosira nordenskioeldii (Marine diatom)
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. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, 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:rbcS
Encoded oniPlastid; Chloroplast
OrganismiThalassiosira nordenskioeldii (Marine diatom)
Taxonomic identifieri83372 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesBacillariophytaCoscinodiscophyceaeThalassiosirophycidaeThalassiosiralesThalassiosiraceaeThalassiosira

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Ribulose bisphosphate carboxylase small chainPRO_0000198606Add
BLAST

Proteomic databases

PRIDEiO98948.

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

3D structure databases

ProteinModelPortaliO98948.
SMRiO98948. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

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]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

O98948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLTQGCFSF LPDLTDTQIE KQVAYAMNKG WAMNVEWTDD PHPRNNYWEL
60 70 80 90 100
WGLPLFDIKD PATVMFELNE ARKSCASGYI RINAFDASYG VESCVMSFIT
110 120 130
NRPATEPGFY LDRTEGPGRQ VIYSIKSYSV QANPEGSRY
Length:139
Mass (Da):15,897
Last modified:May 1, 1999 - v1
Checksum:i7112892F351D10A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018007 Genomic DNA. Translation: BAA75795.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018007 Genomic DNA. Translation: BAA75795.1.

3D structure databases

ProteinModelPortaliO98948.
SMRiO98948. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO98948.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Publicationsi

  1. "Structure and function study of ribulose-1,5-bisphosphate carboxylase/oxygenase of the marine diatom, Thalassiosira nordenskioeldii."
    Tomizawa K.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiRBS_THANO
AccessioniPrimary (citable) accession number: O98948
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1999
Last modified: February 4, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

In this alga, in contrast to plants, the small subunit is encoded in the chloroplast.

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.