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A2Y205 (RBS1_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain, chloroplastic

Short name=Ribulose bisphosphate carboxylase small chain C
Short name=RuBisCO small subunit
Short name=RuBisCO small subunit C
EC=4.1.1.39
Gene names
Name:RBCS
Synonyms:RBCS-C
ORF Names:OsI_018348
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 By similarity.

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

Plastidchloroplast.

Sequence similarities

Belongs to the RuBisCO small chain family.

Ontologies

Keywords
   Biological processCalvin cycle
Carbon dioxide fixation
Photorespiration
Photosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionLyase
Monooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological_processchloroplast ribulose bisphosphate carboxylase complex biogenesis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

response to blue light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to far red light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to red light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentapoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell wall

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast envelope

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosolic ribosome

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

thylakoid

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionmonooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Chloroplast
Chain48 – 175128Ribulose bisphosphate carboxylase small chain, chloroplastic
PRO_0000302886

Regions

Region60 – 645Interaction with large subunit

Experimental info

Sequence conflict1031R → K in EAY97115. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2Y205 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: E95B68AC3178A7D7

FASTA17519,647
        10         20         30         40         50         60 
MAPSVMASSA TTVAPFQGLK STAGMPVARR SGNSSFGNVS NGGRIRCMQV WPIEGIKKFE 

        70         80         90        100        110        120 
TLSYLPPLTV EDLLKQIEYL LRSKWVPCLE FSKVGFVYRE NHRSPGYYDG RYWTMWKLPM 

       130        140        150        160        170 
FGCTDATQVL KELEEAKKAY PDAFVRIIGF DNVRQVQLIS FIAYKPPGCE ESGGN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of ribulose 1,5-bisphosphate carboxylase small subunit from rice."
Lee M.C., Kim C.S., Eun M.Y.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Milyang 23.
[2]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. 93-11.
[3]"A comparative transcriptome map of early and late salinity stress responses in contrasting genotypes of Oryza sativa L."
Kumari S., Panjabi V., Singla-Pareek S.L., Sopory S.K., Pareek A.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Shoot.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017364 mRNA. Translation: AAB70544.1.
CM000130 Genomic DNA. Translation: EAY97115.1.
EF576320 mRNA. Translation: ABR25908.1.

3D structure databases

ProteinModelPortalA2Y205.
SMRA2Y205. Positions 49-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING39947.LOC_Os12g17600.1.

Proteomic databases

PRIDEA2Y205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneA2Y205.

Phylogenomic databases

eggNOGCOG4451.
HOGENOMHOG000141332.

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRBS1_ORYSI
AccessionPrimary (citable) accession number: A2Y205
Secondary accession number(s): A6N0Y8 expand/collapse secondary AC list , O65105, P05347, P18567, Q2QU37
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 40 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families