[1]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Columbia K85; DOI=10.1007/BF00019515; AGRICOLA=IND91035191 Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.; "Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana."; Plant Mol. Biol. 11:745-759(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/4.3.215; PubMed=9330910 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."; DNA Res. 4:215-230(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).

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.
CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂.
SUBUNIT: 8 large chains + 8 small chains.
INTERACTION:
O04197:COI1; NbExp=2; IntAct=EBI-639640, EBI-401159;
SUBCELLULAR LOCATION: Plastid, chloroplast.
ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.

Name 1

Isoform ID P10798-1

This is the isoform sequence displayed in this entry.
MISCELLANEOUS: There are four genes coding for RBS in Arabidopsis thaliana.
SIMILARITY: Belongs to the RuBisCO small chain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14564; CAA32702.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB005248; BAB09353.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360124; AAK25834.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY054552; AAK96743.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY051025; AAK93702.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410314; AAK95300.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF462822; AAL58912.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY064686; AAL47390.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY098970; AAM19980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000721; AAN31863.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S03719; RKMUB3.

NP_198657.1; -.

3D structure databases

SMR

P10798; 56-178.

ModBase

P10798.

Protein-protein interaction databases

IntAct

P10798; -.

2D gel databases

SWISS-2DPAGE

P99057; -.

Organism-specific databases

TAIR

At5g38410; -.

Gene expression databases

ArrayExpress

P10798; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR000894; RuBisCO_sc.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.190.10; RuBisCO_small; 1.

Pfam

PF00101; RuBisCO_small; 1.
Pfam graphical view of domain structure.

PRINTS

PR00152; RUBISCOSMALL.

ProDom

PD000290; RuBisCO_small; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

P10798.

Genome annotation databases

GeneID

833828; -.

GenomeReviews

BA000015_GR; AT5G38410.

NMPDR

fig|3702.1.peg.25533; -.

Other

ProtoNet

P10798.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Calvin cycle; Carbon dioxide fixation; Chloroplast; Complete proteome; Lyase; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 55`	`55`	`Chloroplast.`
`CHAIN`	`56 181`	`126`	`Ribulose bisphosphate carboxylase small chain 3B, chloroplastic.`	`PRO_0000031466`
`CONFLICT`	`47 47`		`A -> T (in Ref. 1; CAA32702).`

Sequence information

Length: 181 AA [This is the length of the unprocessed precursor]

Molecular weight: 20284 Da [This is the MW of the unprocessed precursor]

CRC64: 9A5688A9D055254D [This is a checksum on the sequence]

        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

P10798 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools