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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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 45ChloroplastAdd BLAST45
ChainiPRO_000003147246 – 185Ribulose bisphosphate carboxylase small chain 1, chloroplasticAdd BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N-methylmethionine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP00873.
PRIDEiP00873.

Interactioni

Subunit structurei

8 large chains + 8 small chains.1 Publication

Protein-protein interaction databases

STRINGi3055.EDO96904.

Structurei

Secondary structure

1185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni59 – 62Combined sources4
Helixi68 – 80Combined sources13
Beta strandi84 – 90Combined sources7
Helixi92 – 94Combined sources3
Helixi100 – 104Combined sources5
Beta strandi114 – 116Combined sources3
Beta strandi119 – 122Combined sources4
Helixi131 – 144Combined sources14
Beta strandi148 – 156Combined sources9
Turni157 – 160Combined sources4
Beta strandi161 – 169Combined sources9
Helixi180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00873.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IM2H. Eukaryota.
COG4451. LUCA.
KOiK01602.
OMAiDSRERCT.

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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

EnsemblPlantsiEDO96904; EDO96904; CHLREDRAFT_82986.
GeneIDi5727949.
GrameneiEDO96904; EDO96904; CHLREDRAFT_82986.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDO96904.

Proteomic databases

PaxDbiP00873.
PRIDEiP00873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDO96904; EDO96904; CHLREDRAFT_82986.
GeneIDi5727949.
GrameneiEDO96904; EDO96904; CHLREDRAFT_82986.
KEGGicre:CHLREDRAFT_82986.

Phylogenomic databases

eggNOGiENOG410IM2H. Eukaryota.
COG4451. LUCA.
KOiK01602.
OMAiDSRERCT.

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...

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: November 2, 2016
This is version 129 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

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.