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Protein

Ribulose bisphosphate carboxylase small chain

Gene

rbcS

Organism
Galdieria sulphuraria (Red alga)
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 (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
OrganismiGaldieria sulphuraria (Red alga)
Taxonomic identifieri130081 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

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 – 138138Ribulose bisphosphate carboxylase small chainPRO_0000198598Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

DIPiDIP-60090N.

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 104Combined sources
Helixi16 – 2813Combined sources
Beta strandi32 – 398Combined sources
Beta strandi49 – 524Combined sources
Helixi61 – 7414Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 869Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi121 – 1277Combined sources
Helixi128 – 1314Combined sources
Helixi134 – 1363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0HX-ray1.96B1-138[»]
4F0KX-ray2.05B1-138[»]
4F0MX-ray2.25B1-138[»]
ProteinModelPortaliP23756.
SMRiP23756. Positions 1-138.
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.

P23756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRITQGTFSF LPDLTDEQIK KQIDYMISKK LAIGIEYTND IHPRNSFWEM
60 70 80 90 100
WGLPLFEVTD PAPVLFEINA CRKAKSNFYI KVVGFSSERG IESTIISFIV
110 120 130
NRPKHEPGFN LIRQEDKSRS IKYSIQAYET YKPEDQRY
Length:138
Mass (Da):16,206
Last modified:October 31, 1991 - v1
Checksum:i5E946BA51DAFAEC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55524 Genomic DNA. Translation: CAA39141.2.
AF233069 Genomic DNA. Translation: AAF81682.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55524 Genomic DNA. Translation: CAA39141.2.
AF233069 Genomic DNA. Translation: AAF81682.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0HX-ray1.96B1-138[»]
4F0KX-ray2.05B1-138[»]
4F0MX-ray2.25B1-138[»]
ProteinModelPortaliP23756.
SMRiP23756. Positions 1-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60090N.

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 of the Rubisco operon from the unicellular red alga Cyanidium caldarium: evidence for a polyphyletic origin of the plastids."
    Valentin K.-U., Zetsche K.
    Mol. Gen. Genet. 222:425-430(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 14-1-1 / Isolate 107.79/Goettingen.
  2. Whitney S.M., Andrews J.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: UTEX 2393.

Entry informationi

Entry nameiRBS_GALSU
AccessioniPrimary (citable) accession number: P23756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1991
Last sequence update: October 31, 1991
Last modified: February 3, 2015
This is version 79 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.

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.