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P10798 (RBS3B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain 3B, chloroplastic

Short name=RuBisCO small subunit 3B
EC=4.1.1.39
Gene names
Name:RBCS-3B
Synonyms:ATS3B
Ordered Locus Names:At5g38410
ORF Names:MXI10.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Miscellaneous

There are four genes coding for RBS in Arabidopsis thaliana.

Sequence similarities

Belongs to the RuBisCO small chain family.

Ontologies

Keywords
   Biological processCalvin cycle
Carbon dioxide fixation
Photorespiration
Photosynthesis
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphotorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmonooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P10798-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast
Chain56 – 181126Ribulose bisphosphate carboxylase small chain 3B, chloroplastic
PRO_0000031466

Experimental info

Sequence conflict471A → T in CAA32702. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 9A5688A9D055254D

FASTA18120,284
        10         20         30         40         50         60 
MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG GRVSCMKVWP 

        70         80         90        100        110        120 
PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE LEHGFVYREH GNTPGYYDGR 

       130        140        150        160        170        180 
YWTMWKLPLF GCTDSAQVLK EVEECKKEYP GAFIRIIGFD NTRQVQCISF IAYKPPSFTE 


A 

« Hide

References

« Hide 'large scale' references
[1]"Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana."
Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.
Plant Mol. Biol. 11:745-759(1988) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Columbia K85.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14564 Genomic DNA. Translation: CAA32702.1.
AB005248 Genomic DNA. Translation: BAB09353.1.
CP002688 Genomic DNA. Translation: AED94311.1.
AF360124 mRNA. Translation: AAK25834.1.
AY054552 mRNA. Translation: AAK96743.1.
AY051025 mRNA. Translation: AAK93702.1.
AF410314 mRNA. Translation: AAK95300.1.
AF462822 mRNA. Translation: AAL58912.1.
AY064686 mRNA. Translation: AAL47390.1.
AY098970 mRNA. Translation: AAM19980.1.
BT000721 mRNA. Translation: AAN31863.1.
PIRRKMUB3. S03719.
RefSeqNP_198657.1. NM_123202.3.
UniGeneAt.20381.
At.24772.
At.46639.
At.49098.
At.49366.
At.70032.
At.70053.
At.71313.
At.74604.
At.75410.
At.75674.

3D structure databases

ProteinModelPortalP10798.
SMRP10798. Positions 56-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19079. 5 interactions.
IntActP10798. 5 interactions.

2D gel databases

SWISS-2DPAGEP99057.

Proteomic databases

PaxDbP10798.
PRIDEP10798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G38410.1; AT5G38410.1; AT5G38410. [P10798-1]
GeneID833828.
KEGGath:AT5G38410.

Organism-specific databases

TAIRAT5G38410.

Phylogenomic databases

eggNOGCOG4451.
HOGENOMHOG000141332.
InParanoidP10798.
KOK01602.
PhylomeDBP10798.
ProtClustDBPLN02289.

Enzyme and pathway databases

BioCycARA:GQT-1595-MONOMER.
ARA:GQT-1596-MONOMER.
MetaCyc:AT5G38410-MONOMER.

Gene expression databases

GenevestigatorP10798.

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.
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRBS3B_ARATH
AccessionPrimary (citable) accession number: P10798
Secondary accession number(s): Q9FF21
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 131 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names