Q43832 (RBS2_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase small chain 2, chloroplastic
Short name=RuBisCO small subunit 2
EC=4.1.1.39

Gene names

Name:

RBCS2

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Chenopodioideae › Anserineae › Spinacia

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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	Plastid › chloroplast.
Sequence similarities	Belongs to the RuBisCO small chain family.

Ontologies

Keywords
Biological process	Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW photorespiration Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 57

57

Chloroplast By similarity

Chain

58 – 180

123

Ribulose bisphosphate carboxylase small chain 2, chloroplastic

PRO_0000031558

Secondary structure

1

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180

Helix Strand Turn

Details...

Turn

71 – 74

4

Helix

80 – 92

13

Beta strand

96 – 104

9

Beta strand

125 – 128

4

Helix

137 – 150

14

Beta strand

154 – 162

9

Turn

163 – 166

4

Beta strand

167 – 175

9

Sequences

	Sequence		Length	Mass (Da)
	Q43832 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 651FF2F212CFD64A	FASTA	180	20,326
	10 20 30 40 50 60 MASSVLSSAA VATVSRTPAQ ASMVAPFTGL KSTVGFPATK KNDDITSLAS NGGRVQCMKV 70 80 90 100 110 120 WPTQNMKRYE TLSYLPPLTT DQLARQVDYL LNNKWVPCLE FETDHGFVYR EHHNSPGYYD 130 140 150 160 170 180 GRYWTMWKLP MFGCTDPAQV LNELEECKKE YPNAFIRIIG FDSNRQVQCV SFIAYKPAGY

References

[1]	"cDNA cloning and expression of a ribulose-1,5-bisphophate carboxylase small subunit precursor in Spinacia oleracea." Diogon T., Capelli N., Greppin H., Simon P. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Nobel. Tissue: Leaf.
[2]	"Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants." Knight S., Andersson I., Braenden C.-I. Science 244:702-705(1989) Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[3]	"Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4-A resolution. Subunit interactions and active site." Knight S., Andersson I., Braenden C.-I. J. Mol. Biol. 215:113-160(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate." Taylor T.C., Fothergill M.D., Andersson I. J. Biol. Chem. 271:32894-32899(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-123 IN COMPLEX WITH 2 INHIBITORS (4-CABP AND XUBP).
[5]	"Large structures at high resolution: the 1.6-A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate." Andersson I. J. Mol. Biol. 259:160-174(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP.
[6]	"The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate." Taylor T.C., Andersson I. J. Mol. Biol. 265:432-444(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ITS NATURAL SUBSTRATE.
[7]	"Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate." Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J., Kato K., Shibata N., Inoue T., Yokota A., Kai Y. J. Mol. Biol. 316:679-691(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOGUE 2-CABP.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The Plant Kingdom's sloth - Issue 38 of September 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97600 mRNA. Translation: CAA66201.1.

PIR

S78083.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AA1	X-ray	2.20	C/F/I/S	60-180	[»]
1AUS	X-ray	2.20	S/T/U/V	60-180	[»]
1IR1	X-ray	1.80	S/T/U/V	58-180	[»]
1UPM	X-ray	2.30	C/F/I/M/P/S/T/W	60-180	[»]
1UPP	X-ray	2.30	I/J/K/L	60-180	[»]
1UZD	X-ray	2.40	C/F/I/J/M/P/T/W	103-121	[»]

ProteinModelPortal

Q43832.

SMR

Q43832. Positions 59-180.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q43832. 1 interaction.

MINT

MINT-1522619.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.190.10. 1 hit.

InterPro

IPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]

Pfam

PF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]

PRINTS

PR00152. RUBISCOSMALL.

SMART

SM00961. RuBisCO_small. 1 hit.
[Graphical view]

SUPFAM

SSF55239. RuBisCO_small. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q43832.

Entry information

Entry name

RBS2_SPIOL

Accession

Primary (citable) accession number: Q43832

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program