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Protein

Ribulose bisphosphate carboxylase small chain 2, chloroplastic

Gene

RBCS2

Organism
Spinacia oleracea (Spinach)
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.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation, Photorespiration, Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain 2, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 2
Gene namesi
Name:RBCS2
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5757ChloroplastBy similarityAdd
BLAST
Chaini58 – 180123Ribulose bisphosphate carboxylase small chain 2, chloroplasticPRO_0000031558Add
BLAST

Interactioni

Subunit structurei

8 large chains + 8 small chains.6 Publications

Protein-protein interaction databases

IntActiQ43832. 2 interactions.
MINTiMINT-1522619.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni71 – 744Combined sources
Helixi80 – 9213Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi125 – 1284Combined sources
Helixi137 – 15014Combined sources
Beta strandi154 – 1629Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 1759Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA1X-ray2.20C/F/I/S58-180[»]
1AUSX-ray2.20S/T/U/V58-180[»]
1IR1X-ray1.80S/T/U/V58-180[»]
1UPMX-ray2.30C/F/I/M/P/S/T/W58-180[»]
1UPPX-ray2.30I/J/K/L58-180[»]
1UZDX-ray2.40C/F/I/J/M/P/T/W103-121[»]
ProteinModelPortaliQ43832.
SMRiQ43832. Positions 59-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43832.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSVLSSAA VATVSRTPAQ ASMVAPFTGL KSTVGFPATK KNDDITSLAS
60 70 80 90 100
NGGRVQCMKV WPTQNMKRYE TLSYLPPLTT DQLARQVDYL LNNKWVPCLE
110 120 130 140 150
FETDHGFVYR EHHNSPGYYD GRYWTMWKLP MFGCTDPAQV LNELEECKKE
160 170 180
YPNAFIRIIG FDSNRQVQCV SFIAYKPAGY
Length:180
Mass (Da):20,326
Last modified:November 1, 1996 - v1
Checksum:i651FF2F212CFD64A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97600 mRNA. Translation: CAA66201.1.
PIRiS78083.

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97600 mRNA. Translation: CAA66201.1.
PIRiS78083.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA1X-ray2.20C/F/I/S58-180[»]
1AUSX-ray2.20S/T/U/V58-180[»]
1IR1X-ray1.80S/T/U/V58-180[»]
1UPMX-ray2.30C/F/I/M/P/S/T/W58-180[»]
1UPPX-ray2.30I/J/K/L58-180[»]
1UZDX-ray2.40C/F/I/J/M/P/T/W103-121[»]
ProteinModelPortaliQ43832.
SMRiQ43832. Positions 59-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ43832. 2 interactions.
MINTiMINT-1522619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ43832.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  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) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX WITH TRANSITION-STATE ANALOG, SUBUNIT.
  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) OF ACTIVATED HOLOENZYME IN COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM.
  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 OF INACTIVE HOLOENZYME IN COMPLEX WITH INHIBITORS 4-CABP AND XUBP, SUBUNIT.
  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) OF ACTIVATED HOLOENZYME IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT.
  6. "Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase."
    Taylor T.C., Andersson I.
    Biochemistry 36:4041-4046(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 58-180 OF ACTIVATED HOLOENZYME IN COMPLEX WITH 3-PHOSPHOGLYCERATE AND MAGNESIUM, SUBUNIT.
  7. "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) OF HOLOENZYME IN COMPLEX WITH SUBSTRATE AND CALCIUM IN ACTIVATED AND INACTIVATED STATE, SUBUNIT.
  8. "Calcium supports loop closure but not catalysis in Rubisco."
    Karkehabadi S., Taylor T.C., Andersson I.
    J. Mol. Biol. 334:65-73(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 58-180 OF HOLOENZYME IN COMPLEX WITH TRANSITION STATE ANALOG 2-CABP AND CALCIUM.

Entry informationi

Entry nameiRBS2_SPIOL
AccessioniPrimary (citable) accession number: Q43832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.