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Protein

Ribulose bisphosphate carboxylase small chain 3B, chloroplastic

Gene

RBCS-3B

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain 3B, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 3B
Gene namesi
Name:RBCS-3B
Synonyms:ATS3B
Ordered Locus Names:At5g38410
ORF Names:MXI10.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G38410.

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 – 5555ChloroplastAdd
BLAST
Chaini56 – 181126Ribulose bisphosphate carboxylase small chain 3B, chloroplasticPRO_0000031466Add
BLAST

Proteomic databases

PaxDbiP10798.
PRIDEiP10798.

2D gel databases

SWISS-2DPAGEP99057.

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

BioGridi19079. 5 interactions.
IntActiP10798. 5 interactions.
STRINGi3702.AT5G38410.3.

Structurei

3D structure databases

ProteinModelPortaliP10798.
SMRiP10798. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiP10798.
PhylomeDBiP10798.

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.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P10798-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASSMLSSAA VVTSPAQATM VAPFTGLKSS AAFPVTRKTN KDITSIASNG
60 70 80 90 100
GRVSCMKVWP PIGKKKFETL SYLPDLSDVE LAKEVDYLLR NKWIPCVEFE
110 120 130 140 150
LEHGFVYREH GNTPGYYDGR YWTMWKLPLF GCTDSAQVLK EVEECKKEYP
160 170 180
GAFIRIIGFD NTRQVQCISF IAYKPPSFTE A
Length:181
Mass (Da):20,284
Last modified:January 23, 2002 - v2
Checksum:i9A5688A9D055254D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471A → T in CAA32702 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS03719. RKMUB3.
RefSeqiNP_198657.1. NM_123202.3. [P10798-1]
UniGeneiAt.20381.
At.24772.
At.46639.
At.49098.
At.49366.
At.70032.
At.70053.
At.71313.
At.74604.
At.75410.
At.75674.

Genome annotation databases

EnsemblPlantsiAT5G38410.1; AT5G38410.1; AT5G38410. [P10798-1]
GeneIDi833828.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS03719. RKMUB3.
RefSeqiNP_198657.1. NM_123202.3. [P10798-1]
UniGeneiAt.20381.
At.24772.
At.46639.
At.49098.
At.49366.
At.70032.
At.70053.
At.71313.
At.74604.
At.75410.
At.75674.

3D structure databases

ProteinModelPortaliP10798.
SMRiP10798. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19079. 5 interactions.
IntActiP10798. 5 interactions.
STRINGi3702.AT5G38410.3.

2D gel databases

SWISS-2DPAGEP99057.

Proteomic databases

PaxDbiP10798.
PRIDEiP10798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G38410.1; AT5G38410.1; AT5G38410. [P10798-1]
GeneIDi833828.

Organism-specific databases

TAIRiAT5G38410.

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiP10798.
PhylomeDBiP10798.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP10798.

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.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRBS3B_ARATH
AccessioniPrimary (citable) accession number: P10798
Secondary accession number(s): Q9FF21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are four genes coding for RBS in Arabidopsis thaliana.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.