[1]	PROTEIN SEQUENCE. Martin P.G.; "Amino acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase from spinach."; Aust. J. Plant Physiol. 6:401-408(1979).
[2]	SEQUENCE REVISION TO 68-70. Martin P.G.; Submitted (OCT-1982) to the PIR data bank.

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.
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.
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the RuBisCO small chain family.
WEB RESOURCE: Name=Protein Spotlight; Note=The Plant Kingdom's sloth - Issue 38 of September 2003; URL="http://www.expasy.org/spotlight/back_issues/sptlt038.shtml";.

Copyright

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

Cross-references

Sequence databases

PIR

A01089; RKSPS.

3D structure databases

PDB

1RBO; X-ray; 2.30 A; C/F/I/S=1-123.	[ExPASy / RCSB / EBI]
1RCO; X-ray; 2.30 A; C/F/I/M/P/S/T/W=1-123.	[ExPASy / RCSB / EBI]
1RCX; X-ray; 2.40 A; C/F/I/M/P/S/T/W=1-123.	[ExPASy / RCSB / EBI]
1RXO; X-ray; 2.20 A; C/F/I/S=1-123.	[ExPASy / RCSB / EBI]
8RUC; X-ray; 1.60 A; I/J/K/L=1-123.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RBO; -.
1RCO; -.
1RCX; -.
1RXO; -.
8RUC; -.

ModBase

P00870.

Protein-protein interaction databases

DIP

DIP:27640N; -.

Ontologies

GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009853;	Biological process: photorespiration (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from UniProtKB-KW).
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]

Other

P00870; -.

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

Keywords

3D-structure; Carbon dioxide fixation; Chloroplast; Direct protein sequencing; Lyase; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 123`	`123`	`Ribulose bisphosphate carboxylase small chain.`	`PRO_0000198589`
`MOD_RES`	`1 1`		`Methionine derivative.`
`VARIANT`	`94 94`	`1`	`P -> Y.`
`TURN`	`14 17`	`4`
`HELIX`	`23 35`	`13`
`STRAND`	`39 47`	`9`
`STRAND`	`68 71`	`4`
`HELIX`	`80 93`	`14`
`STRAND`	`97 105`	`9`
`TURN`	`106 109`	`4`
`STRAND`	`110 118`	`9`

Sequence information

Length: 123 AA [This is the length of the unprocessed precursor]

Molecular weight: 14283 Da [This is the MW of the unprocessed precursor]

CRC64: DC727DD6EF1EF59B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQVWPPLGLK KFETLSYLPP LTTEQLLAEV NYLLVKGWIP PLEFEVKDGF VYREHDKSPG 

        70         80         90        100        110        120 
YYDGRYWTMW KLPMFGGTDP AQVVNEVEEV KKAPPDAFVR FIGFNDKREV QCISFIAYKP 


AGY

P00870 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