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B8HQS5 (RBL_CYAP4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:Cyan7425_3422
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP]
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. HAMAP-Rule MF_01338

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_1000166261

Sites

Active site1761Proton acceptor By similarity
Active site2951Proton acceptor By similarity
Metal binding2021Magnesium; via carbamate group By similarity
Metal binding2041Magnesium By similarity
Metal binding2051Magnesium By similarity
Binding site1241Substrate; in homodimeric partner By similarity
Binding site1741Substrate By similarity
Binding site1781Substrate By similarity
Binding site2961Substrate By similarity
Binding site3281Substrate By similarity
Binding site3801Substrate By similarity
Site3351Transition state stabilizer By similarity

Amino acid modifications

Modified residue2021N6-carboxylysine By similarity
Disulfide bond248Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
B8HQS5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 764F70B5E6EDADEE

FASTA47653,051
        10         20         30         40         50         60 
MSYAQTRTQT KAGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP YEEAAAAVAA 

        70         80         90        100        110        120 
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA YIAYPLDLFE EGSVTNLLTS 

       130        140        150        160        170        180 
LVGNVFGFKA LKALRLEDLR IPVAYLKTFQ GPPHGIQVER DKINKYGRPL LGCTIKPKLG 

       190        200        210        220        230        240 
LSAKNYGRAV YECLRGGLDF TKDDENINSQ PFQRWRDRFL FVADAIHKAQ AETGEVKGHY 

       250        260        270        280        290        300 
LNVTAGTCEE MMKRAAFAKE LEMPIIMHDF LTGGFTANTS LAHYCRDNGL LLHIHRAMHA 

       310        320        330        340        350        360 
VIDRQKNHGI HFRVLSKCLR MSGGDHIHTG TVVGKLEGDK DITLGFIDLL RENYIEENRS 

       370        380        390        400        410        420 
RGIYFTQDWA SMPGVMAVAS GGIHVWHMPA LVDIFGDDAV LQFGGGTLGH PWGNAPGATA 

       430        440        450        460        470 
NRVALEACVQ ARNEGRNLMR EGGDIIREAC RWSPELAAAC ELWKEIKFEF EAVDTV 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001344 Genomic DNA. Translation: ACL45746.1.
RefSeqYP_002484107.1. NC_011884.1.

3D structure databases

ProteinModelPortalB8HQS5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395961.Cyan7425_3422.

Proteomic databases

PRIDEB8HQS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL45746; ACL45746; Cyan7425_3422.
GeneID7289359.
KEGGcyn:Cyan7425_3422.
PATRIC21567811. VBICyaSp30657_3409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycCSP395961:GJDE-3253-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_CYAP4
AccessionPrimary (citable) accession number: B8HQS5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families