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Protein

Ribulose bisphosphate carboxylase small chain

Gene

RBCS

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 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

  1. monooxygenase activity Source: UniProtKB-KW
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. photorespiration Source: UniProtKB-KW
  3. photosynthesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation, Photorespiration, Photosynthesis

Enzyme and pathway databases

BRENDAi4.1.1.39. 5812.

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
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Protein family/group databases

Allergomei3814. Spi o RuBisCO.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Ribulose bisphosphate carboxylase small chainPRO_0000198589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Methionine derivative

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

DIPiDIP-27640N.

Structurei

Secondary structure

1
123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni14 – 174Combined sources
Helixi23 – 3513Combined sources
Beta strandi39 – 479Combined sources
Beta strandi68 – 714Combined sources
Helixi80 – 9314Combined sources
Beta strandi97 – 1059Combined sources
Turni106 – 1094Combined sources
Beta strandi110 – 1189Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RBOX-ray2.30C/F/I/S1-123[»]
1RCOX-ray2.30C/F/I/M/P/S/T/W1-123[»]
1RCXX-ray2.40C/F/I/M/P/S/T/W1-123[»]
1RXOX-ray2.20C/F/I/S1-123[»]
8RUCX-ray1.60I/J/K/L1-123[»]
ProteinModelPortaliP00870.
SMRiP00870. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00870.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

P00870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVWPPLGLK KFETLSYLPP LTTEQLLAEV NYLLVKGWIP PLEFEVKDGF
60 70 80 90 100
VYREHDKSPG YYDGRYWTMW KLPMFGGTDP AQVVNEVEEV KKAPPDAFVR
110 120
FIGFNDKREV QCISFIAYKP AGY
Length:123
Mass (Da):14,283
Last modified:July 21, 1986 - v1
Checksum:iDC727DD6EF1EF59B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941P → Y.

Sequence databases

PIRiA01089. RKSPS.

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

PIRiA01089. RKSPS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RBOX-ray2.30C/F/I/S1-123[»]
1RCOX-ray2.30C/F/I/M/P/S/T/W1-123[»]
1RCXX-ray2.40C/F/I/M/P/S/T/W1-123[»]
1RXOX-ray2.20C/F/I/S1-123[»]
8RUCX-ray1.60I/J/K/L1-123[»]
ProteinModelPortaliP00870.
SMRiP00870. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-27640N.

Protein family/group databases

Allergomei3814. Spi o RuBisCO.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.1.1.39. 5812.

Miscellaneous databases

EvolutionaryTraceiP00870.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase from spinach."
    Martin P.G.
    Aust. J. Plant Physiol. 6:401-408(1978)
    Cited for: PROTEIN SEQUENCE.
  2. Martin P.G.
    Submitted (SEP-1982) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 68-70.

Entry informationi

Entry nameiRBS1_SPIOL
AccessioniPrimary (citable) accession number: P00870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 104 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, Direct protein sequencing

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

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.