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Protein

Ribulose bisphosphate carboxylase small chain 1, chloroplastic

Gene

RBCS-1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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

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 1, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 1
Gene namesi
Name:RBCS-1
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

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 – 4545ChloroplastAdd
BLAST
Chaini46 – 185140Ribulose bisphosphate carboxylase small chain 1, chloroplasticPRO_0000031472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N-methylmethionine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PRIDEiP00873.

Interactioni

Subunit structurei

8 large chains + 8 small chains.1 Publication

Protein-protein interaction databases

STRINGi3055.EDO96904.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni59 – 624Combined sources
Helixi68 – 8013Combined sources
Beta strandi84 – 907Combined sources
Helixi92 – 943Combined sources
Helixi100 – 1045Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1224Combined sources
Helixi131 – 14414Combined sources
Beta strandi148 – 1569Combined sources
Turni157 – 1604Combined sources
Beta strandi161 – 1699Combined sources
Helixi180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK8X-ray1.40I/K/M/O46-185[»]
1UW9X-ray2.05C/F/I/J/M/P/T/W46-185[»]
1UWAX-ray2.30C/F/I/J/M/P/T/W46-185[»]
1UZDX-ray2.40C/F/I/J/M/P/T/W46-90[»]
C/F/I/J/M/P/T/W116-185[»]
1UZHX-ray2.20C/F/I/J/M/P/T/W46-185[»]
2V63X-ray1.80I/J/K/L/M/N/O/P46-185[»]
2V67X-ray2.00I/J/K/L/M/N/O/P46-185[»]
2V68X-ray2.30I/J/K/L/M/N/O/P46-185[»]
2V69X-ray2.80I/J/K/L/M/N/O/P46-185[»]
2V6AX-ray1.50I/J/K/L/M/N/O/P46-185[»]
2VDHX-ray2.30I/J/K/L/M/N/O/P46-185[»]
2VDIX-ray2.65I/J/K/L/M/N/O/P46-185[»]
ProteinModelPortaliP00873.
SMRiP00873. Positions 47-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00873.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4451.
KOiK01602.
OMAiVAPATFV.

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.
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.

P00873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT
60 70 80 90 100
PVNNKMFETF SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE
110 120 130 140 150
SAIRFGSVSC LYYDNRYWTM WKLPMFGCRD PMQVLREIVA CTKAFPDAYV
160 170 180
RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA NKRSV
Length:185
Mass (Da):20,620
Last modified:January 1, 1988 - v1
Checksum:iB4114FD98E807F16
GO

Sequence cautioni

The sequence CAA28159.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04471 Genomic DNA. Translation: CAA28159.1. Different initiation.
PIRiA25785. RKKMS1.
RefSeqiXP_001702409.1. XM_001702357.1.
UniGeneiCre.3435.

Genome annotation databases

GeneIDi5727949.
KEGGicre:CHLREDRAFT_82986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04471 Genomic DNA. Translation: CAA28159.1. Different initiation.
PIRiA25785. RKKMS1.
RefSeqiXP_001702409.1. XM_001702357.1.
UniGeneiCre.3435.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK8X-ray1.40I/K/M/O46-185[»]
1UW9X-ray2.05C/F/I/J/M/P/T/W46-185[»]
1UWAX-ray2.30C/F/I/J/M/P/T/W46-185[»]
1UZDX-ray2.40C/F/I/J/M/P/T/W46-90[»]
C/F/I/J/M/P/T/W116-185[»]
1UZHX-ray2.20C/F/I/J/M/P/T/W46-185[»]
2V63X-ray1.80I/J/K/L/M/N/O/P46-185[»]
2V67X-ray2.00I/J/K/L/M/N/O/P46-185[»]
2V68X-ray2.30I/J/K/L/M/N/O/P46-185[»]
2V69X-ray2.80I/J/K/L/M/N/O/P46-185[»]
2V6AX-ray1.50I/J/K/L/M/N/O/P46-185[»]
2VDHX-ray2.30I/J/K/L/M/N/O/P46-185[»]
2VDIX-ray2.65I/J/K/L/M/N/O/P46-185[»]
ProteinModelPortaliP00873.
SMRiP00873. Positions 47-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDO96904.

Proteomic databases

PRIDEiP00873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5727949.
KEGGicre:CHLREDRAFT_82986.

Phylogenomic databases

eggNOGiCOG4451.
KOiK01602.
OMAiVAPATFV.

Miscellaneous databases

EvolutionaryTraceiP00873.

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.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii."
    Goldschmidt-Clermont M., Rahire M.
    J. Mol. Biol. 191:421-432(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii."
    Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.
    J. Biol. Chem. 276:48159-48164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 46-185 IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP, METHYLATION AT MET-46.
    Strain: 2137.

Entry informationi

Entry nameiRBS1_CHLRE
AccessioniPrimary (citable) accession number: P00873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: June 24, 2015
This is version 121 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. 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.