Ribulose bisphosphate carboxylase small chain - Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)

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P04716 (RBS_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	cbbS
Synonyms:	rbcS
Ordered Locus Names:	syc0129_c

Organism

Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]

Taxonomic identifier

269084 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

Protein attributes

Sequence length	111 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.
Sequence similarities	Belongs to the RuBisCO small chain family.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photosynthesis
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
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

Initiator methionine

Removed

Chain

2 – 111

110

Ribulose bisphosphate carboxylase small chain

PRO_0000198624

Regions

Region

12 – 21

Hydrophobic

Secondary structure

111

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04716 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F854F73FA70BD57B
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FASTA

111

13,333

        10         20         30         40         50         60 
MSMKTLPKER RFETFSYLPP LSDRQIAAQI EYMIEQGFHP LIEFNEHSNP EEFYWTMWKL 

        70         80         90        100        110 
PLFDCKSPQQ VLDEVRECRS EYGDCYIRVA GFDNIKQCQT VSFIVHRPGR Y

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene for the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase is located close to the gene for the large subunit in the cyanobacterium Anacystis nidulans 6301." Shinozaki K., Sugiura M. Nucleic Acids Res. 11:6957-6963(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genes for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase constitute a single operon in a cyanobacterium Anacystis nidulans 6301." Shinozaki K., Sugiura M. Mol. Gen. Genet. 200:27-32(1985) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization." Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M. Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[4]	"The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution." Newman J., Gutteridge S. J. Biol. Chem. 268:25876-25886(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate." Newman J., Gutteridge S. Structure 2:495-502(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03220 Genomic DNA. Translation: CAA26973.1.
AP008231 Genomic DNA. Translation: BAD78319.1.

PIR

RKYCS. S07351.

RefSeq

YP_170839.1. NC_006576.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RBL	X-ray	2.20	I/J/K/L/M/N/O/P	2-109	[»]
1RSC	X-ray	2.30	I/J/K/L/M/N/O/P	1-111	[»]
1UZH	X-ray	2.20	C/F/I/J/M/P/T/W	47-53	[»]

ProteinModelPortal

P04716.

SMR

P04716. Positions 2-110.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6211N.

STRING

269084.syc0129_c.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD78319; BAD78319; syc0129_c.

GeneID

3200023.

KEGG

syc:syc0129_c.

PATRIC

32485753. VBISynElo117686_0155.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG4451.

HOGENOM

HOG000141332.

K01602.

OMA

WAVNIEF.

ProtClustDB

CLSK893428.

Enzyme and pathway databases

BioCyc

SELO269084:GCDQ-134-MONOMER.

SABIO-RK

P04716.

Family and domain databases

Gene3D

3.30.190.10. 1 hit.

InterPro

IPR000894. RuBisCO_sc_dom.
[Graphical view]

Pfam

PF00101. RuBisCO_small. 1 hit.
[Graphical view]

SMART

SM00961. RuBisCO_small. 1 hit.
[Graphical view]

SUPFAM

SSF55239. RuBisCO_small. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P04716.

Entry information

Entry name

RBS_SYNP6

Accession

Primary (citable) accession number: P04716

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents