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Reviewed, UniProtKB/Swiss-Prot P00873 (RBS1_CHLRE)

Last modified November 24, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribulose bisphosphate carboxylase small chain 1, chloroplastic
      Short name=RuBisCO small subunit 1
    EC=4.1.1.39
Gene names
Name: RBCS-1
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

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Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

Plastid › chloroplast.

Sequence similarities

Belongs to the RuBisCO small chain family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Chloroplast
Chain46 – 185140Ribulose bisphosphate carboxylase small chain 1, chloroplastic
PRO_0000031472

Amino acid modifications

Modified residue461N-methylmethionine

Experimental info

Sequence conflict21Missing AA sequence Ref.2
Sequence conflict421Q → E AA sequence Ref.2
Sequence conflict451Q → D AA sequence Ref.2

Secondary structure

1 ..................... 185
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00873-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: B4114FD98E807F16

FASTA18520,620
        10         20         30         40         50         60 
MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF 

        70         80         90        100        110        120 
SYLPPLTDEQ IAAQVDYIVA NGWIPCLEFA EADKAYVSNE SAIRFGSVSC LYYDNRYWTM 

       130        140        150        160        170        180 
WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKTARDFQPA 


NKRSV

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References

[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: 3820291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"NH2-terminal amino acid sequences of precursor and mature forms of the ribulose-1,5-bisphosphate carboxylase small subunit from Chlamydomonas reinhardtii."
Schmidt G.W., Devillers-Thiery A., Desruisseaux H., Blobel G., Chua N.-H.
J. Cell Biol. 83:615-622(1979) [PubMed: 521455] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-57.
[3]"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: 11641402] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 46-185 IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP.
Strain: 2137.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X04471 Genomic DNA. Translation: CAA28159.1. Different initiation.
PIRRKKMS1. A25785.
RefSeqXP_001702409.1.
UniGeneCre.3435

3D structure databases

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/W46-185[»]
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[»]
ModBaseSearch...

Proteomic databases

PRIDEP00873.

Genome annotation databases

GeneID5727949.
KEGGcre:CHLREDRAFT_82986.

Enzyme and pathway databases

BRENDA4.1.1.39. 144.

Family and domain databases

InterProIPR000894. RuBisCO_sc.
[Graphical view]
Gene3DG3DSA:3.30.190.10. RuBisCO_small. 1 hit.
PfamPF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
ProtoNetSearch...

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Entry information

Entry nameRBS1_CHLRE
AccessionPrimary (citable) accession number: P00873
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: November 24, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents