Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6N0B6 (A6N0B6_ORYSI) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 45. Feed History...

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

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain RuleBase RU003627

EC=4.1.1.39 RuleBase RU003627
Gene names
ORF Names:OsI_38042 EMBL EEC69124.1
OrganismOryza sativa subsp. indica (Rice) EMBL ABR25686.1
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
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. SAAS SAAS024681 RuleBase RU003627

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. SAAS SAAS024681 RuleBase RU003627

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. SAAS SAAS024681 RuleBase RU003627

Subunit structure

8 large chains + 8 small chains By similarity. SAAS SAAS024681 RuleBase RU003627

Sequence similarities

Belongs to the RuBisCO small chain family. RuleBase RU003627

Ontologies

Keywords
   Biological processCarbon dioxide fixation SAAS SAAS024681 RuleBase RU003627
Photorespiration SAAS SAAS024681 RuleBase RU003627
Photosynthesis SAAS SAAS024681 RuleBase RU003627
   Cellular componentChloroplast SAAS SAAS024681
Plastid
   Molecular functionLyase SAAS SAAS024681 RuleBase RU003627
Monooxygenase SAAS SAAS024681 RuleBase RU003627
Oxidoreductase
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

chloroplast ribulose bisphosphate carboxylase complex biogenesis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

response to blue light

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cold

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

chloroplast envelope

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast thylakoid membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosolic ribosome

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

thylakoid lumen

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A6N0B6 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: BB1F731484324EF9

FASTA17519,631
        10         20         30         40         50         60 
MAPTVMASSA TSVAPFQGLK STAGLPVSRR STNSGFGNVS NGGRIKCMQV 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

[1]"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., Chen H., 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., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Improved gene annotation of the rice (Oryza sativa) genomes."
Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., Li J., Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R., Kristiansen K., Wong G.K.-S.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[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.
[4]Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., Li J., Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R., Kristiansen K., Wong G.K.-S.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF576098 mRNA. Translation: ABR25686.1.
CM000137 Genomic DNA. Translation: EEC69124.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING39947.LOC_Os12g19381.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameA6N0B6_ORYSI
AccessionPrimary (citable) accession number: A6N0B6
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: July 24, 2007
Last modified: March 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)