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Q43832 (RBS2_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain 2, chloroplastic

Short name=RuBisCO small subunit 2
EC=4.1.1.39
Gene names
Name:RBCS2
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Subunit structure

8 large chains + 8 small chains.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the RuBisCO small chain family.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
Photorespiration
Photosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmonooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5757Chloroplast By similarity
Chain58 – 180123Ribulose bisphosphate carboxylase small chain 2, chloroplastic
PRO_0000031558

Secondary structure

............... 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q43832 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 651FF2F212CFD64A

FASTA18020,326
        10         20         30         40         50         60 
MASSVLSSAA VATVSRTPAQ ASMVAPFTGL KSTVGFPATK KNDDITSLAS NGGRVQCMKV 

        70         80         90        100        110        120 
WPTQNMKRYE TLSYLPPLTT DQLARQVDYL LNNKWVPCLE FETDHGFVYR EHHNSPGYYD 

       130        140        150        160        170        180 
GRYWTMWKLP MFGCTDPAQV LNELEECKKE YPNAFIRIIG FDSNRQVQCV SFIAYKPAGY 

« Hide

References

[1]"cDNA cloning and expression of a ribulose-1,5-bisphophate carboxylase small subunit precursor in Spinacia oleracea."
Diogon T., Capelli N., Greppin H., Simon P.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Nobel.
Tissue: Leaf.
[2]"Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants."
Knight S., Andersson I., Braenden C.-I.
Science 244:702-705(1989)
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[3]"Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4-A resolution. Subunit interactions and active site."
Knight S., Andersson I., Braenden C.-I.
J. Mol. Biol. 215:113-160(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate."
Taylor T.C., Fothergill M.D., Andersson I.
J. Biol. Chem. 271:32894-32899(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-123 IN COMPLEX WITH 2 INHIBITORS (4-CABP AND XUBP).
[5]"Large structures at high resolution: the 1.6-A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate."
Andersson I.
J. Mol. Biol. 259:160-174(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP.
[6]"The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate."
Taylor T.C., Andersson I.
J. Mol. Biol. 265:432-444(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ITS NATURAL SUBSTRATE.
[7]"Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate."
Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J., Kato K., Shibata N., Inoue T., Yokota A., Kai Y.
J. Mol. Biol. 316:679-691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The Plant Kingdom's sloth - Issue 38 of September 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97600 mRNA. Translation: CAA66201.1.
PIRS78083.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA1X-ray2.20C/F/I/S60-180[»]
1AUSX-ray2.20S/T/U/V60-180[»]
1IR1X-ray1.80S/T/U/V58-180[»]
1UPMX-ray2.30C/F/I/M/P/S/T/W60-180[»]
1UPPX-ray2.30I/J/K/L60-180[»]
1UZDX-ray2.40C/F/I/J/M/P/T/W103-121[»]
ProteinModelPortalQ43832.
SMRQ43832. Positions 59-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ43832. 1 interaction.
MINTMINT-1522619.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ43832.

Entry information

Entry nameRBS2_SPIOL
AccessionPrimary (citable) accession number: Q43832
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references