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B1WXH3 (RBL_CYAA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:cce_3166
OrganismCyanothece sp. (strain ATCC 51142) [Complete proteome] [HAMAP]
Taxonomic identifier43989 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length471 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 – 471471Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000355749

Sites

Active site1711Proton acceptor By similarity
Active site2901Proton acceptor By similarity
Metal binding1971Magnesium; via carbamate group By similarity
Metal binding1991Magnesium By similarity
Metal binding2001Magnesium By similarity
Binding site1191Substrate; in homodimeric partner By similarity
Binding site1691Substrate By similarity
Binding site1731Substrate By similarity
Binding site2911Substrate By similarity
Binding site3231Substrate By similarity
Binding site3751Substrate By similarity
Site3301Transition state stabilizer By similarity

Amino acid modifications

Modified residue1971N6-carboxylysine By similarity
Disulfide bond243Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
B1WXH3 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 549FB4FF3AFDE916

FASTA47152,462
        10         20         30         40         50         60 
MAQATKSGFN AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QPGVPPEEAG AAVAAESSTG 

        70         80         90        100        110        120 
TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQYFCFIAYP LDLFEEGSVT NVLTSLVGNV 

       130        140        150        160        170        180 
FGFKALRALR LEDIRFPVAL IKTFQGPPHG ITVERDKLNK YGRPLLGCTI KPKLGLSAKN 

       190        200        210        220        230        240 
YGRAVYECLR GGLDFTKDDE NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA 

       250        260        270        280        290        300 
GTCEEMMKRA EFAKEIGTPI VMHDFLTGGF TANTTLAKFC RDNGILLHIH RAMHAVIDRQ 

       310        320        330        340        350        360 
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV EEDRSRGIFF 

       370        380        390        400        410        420 
TQDYASMPGT MPVASGGIHV WHMPALVEIF GDDSCLQFGG GTLGHPWGNA PGATANRVAL 

       430        440        450        460        470 
EACIQARNEG RNLAREGNDV IREACKWSPE LAAACELWKE ITFEFEAMDT L 

« Hide

References

[1]"The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle."
Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.
Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51142.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000806 Genomic DNA. Translation: ACB52514.1.
RefSeqYP_001804580.1. NC_010546.1.

3D structure databases

ProteinModelPortalB1WXH3.
SMRB1WXH3. Positions 8-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING43989.cce_3166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB52514; ACB52514; cce_3166.
GeneID6170227.
KEGGcyt:cce_3166.
PATRIC21544734. VBICyaSp130209_3185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCSP43989:GKC8-3206-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_CYAA5
AccessionPrimary (citable) accession number: B1WXH3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 38 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