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Protein

Ribulose bisphosphate carboxylase small chain, chloroplastic

Gene

RBCS

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

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

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain, chloroplastic (EC:4.1.1.39)
Short name:
Ribulose bisphosphate carboxylase small chain C
Short name:
RuBisCO small subunit
Short name:
RuBisCO small subunit C
Gene namesi
Name:RBCS
Synonyms:RBCS-C
ORF Names:OsI_018348
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
ProteomesiUP000007015 Componenti: Chromosome 5

Organism-specific databases

GrameneiA2Y205.

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 – 4747ChloroplastAdd
BLAST
Chaini48 – 175128Ribulose bisphosphate carboxylase small chain, chloroplasticPRO_0000302886Add
BLAST

Proteomic databases

PRIDEiA2Y205.

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

STRINGi39947.LOC_Os12g17600.1.

Structurei

3D structure databases

ProteinModelPortaliA2Y205.
SMRiA2Y205. Positions 49-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 645Interaction with large subunit

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2Y205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSVMASSA TTVAPFQGLK STAGMPVARR SGNSSFGNVS NGGRIRCMQV
60 70 80 90 100
WPIEGIKKFE TLSYLPPLTV EDLLKQIEYL LRSKWVPCLE FSKVGFVYRE
110 120 130 140 150
NHRSPGYYDG RYWTMWKLPM FGCTDATQVL KELEEAKKAY PDAFVRIIGF
160 170
DNVRQVQLIS FIAYKPPGCE ESGGN
Length:175
Mass (Da):19,647
Last modified:September 11, 2007 - v2
Checksum:iE95B68AC3178A7D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031R → K in EAY97115 (PubMed:15685292).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017364 mRNA. Translation: AAB70544.1.
CM000130 Genomic DNA. Translation: EAY97115.1.
EF576320 mRNA. Translation: ABR25908.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017364 mRNA. Translation: AAB70544.1.
CM000130 Genomic DNA. Translation: EAY97115.1.
EF576320 mRNA. Translation: ABR25908.1.

3D structure databases

ProteinModelPortaliA2Y205.
SMRiA2Y205. Positions 49-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os12g17600.1.

Proteomic databases

PRIDEiA2Y205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiA2Y205.

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRBS1_ORYSI
AccessioniPrimary (citable) accession number: A2Y205
Secondary accession number(s): A6N0Y8
, O65105, P05347, P18567, Q2QU37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: March 4, 2015
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.