P08475 (RBS2_CHLRE) 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:

RBCS-2

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	185 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
PTM	Methylation
Technical term	3D-structure Direct protein sequencing
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 – 45

45

Chloroplast

Chain

46 – 185

140

Ribulose bisphosphate carboxylase small chain 2, chloroplastic

PRO_0000031473

Amino acid modifications

Modified residue

46

1

N-methylmethionine

Secondary structure

1

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185

Helix Strand Turn

Details...

Turn

59 – 62

4

Helix

68 – 80

13

Beta strand

84 – 90

7

Helix

92 – 94

3

Helix

100 – 104

5

Helix

131 – 144

14

Beta strand

148 – 156

9

Turn

157 – 160

4

Beta strand

161 – 169

9

Helix

180 – 182

3

Sequences

	Sequence		Length	Mass (Da)
	P08475 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: E19A3627EF484F50	FASTA	185	20,647
	10 20 30 40 50 60 MAAVIAKSSV SAAVARPARS SVRPMAALKP AVKAAPVAAP AQANQMMVWT PVNNKMFETF 70 80 90 100 110 120 SYLPPLSDEQ IAAQVDYIVA NGWIPCLEFA ESDKAYVSNE SAIRFGSVSC LYYDNRYWTM 130 140 150 160 170 180 WKLPMFGCRD PMQVLREIVA CTKAFPDAYV RLVAFDNQKQ VQIMGFLVQR PKSARDWQPA NKRSV

References

[1]	"Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii." Goldschmidt-Clermont M., Rahire M. J. Mol. Biol. 191:421-432(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Partial purification and properties of enzymes involved in the processing of a chloroplast import protein from Chlamydomonas reinhardii." Su Q., Boschetti A. Eur. J. Biochem. 217:1039-1047(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-60.
[3]	"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) OF 46-185 IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP. Strain: 137c / CC-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04472 Genomic DNA. Translation: CAA28160.1.

PIR

RKKMS2. B25785.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IR2	X-ray	1.84	1/2/3/4/5/6/7/8/I/J/K/L/M/N/O/P	46-185	[»]
1UZH	X-ray	2.20	C/F/I/J/M/P/T/W	-	[»]

ProteinModelPortal

P08475.

SMR

P08475. Positions 46-185.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG4451.

OMA

KSARDWQ.

Family and domain databases

Gene3D

3.30.190.10. 1 hit.

InterPro

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

Pfam

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

P08475.

Entry information

Entry name

RBS2_CHLRE

Accession

Primary (citable) accession number: P08475

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program