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Q8U1P9 (RBL_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:rbcL
Ordered Locus Names:PF1156
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase By similarity. HAMAP-Rule MF_01133

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01133

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01133

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01133

Subunit structure

Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits By similarity.

Miscellaneous

Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains (PubMed:17303759).

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062676

Regions

Region343 – 3453Substrate binding By similarity
Region365 – 3684Substrate binding By similarity

Sites

Active site1551Proton acceptor By similarity
Active site2731Proton acceptor By similarity
Metal binding1811Magnesium; via carbamate group By similarity
Metal binding1831Magnesium By similarity
Metal binding1841Magnesium By similarity
Binding site1571Substrate By similarity
Binding site2741Substrate By similarity
Binding site3061Substrate By similarity
Site3131Transition state stabilizer By similarity

Amino acid modifications

Modified residue1811N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8U1P9 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 0271D055DCFF3DC4

FASTA42047,348
        10         20         30         40         50         60 
MKVEWYLDFV DLDYTPGRDE LIVEYYFEPN GVSPEEAAGR IASESSIGTW TTLWKMPEMA 

        70         80         90        100        110        120 
KRSMAKVFYL EKSGEGYIAK IAYPLTLFEE GSIVQLLSAI AGNIFGMKAL KNLRLLDFHP 

       130        140        150        160        170        180 
PYEYLRHFKG PQYGVKGIRE FMGVKERPLT ATVPKPKMGW SVDEYAEIAY ELWSGGIDLL 

       190        200        210        220        230        240 
KDDENFTSFP FNRFEERVKK LYRIRDIVEA ETEERKEYLI NITGSVDVME KRAELVANEG 

       250        260        270        280        290        300 
GQYVMIDIIV TGWSALQYMR EVTEDLGLAI HAHRAMHAAF TRNPKHGITM YAIAKLARMI 

       310        320        330        340        350        360 
GVDQIHTGTA VGKMAGDYEE VKRINDFLLS KWEHIREVFP VASGGLHPGL MPELIRLFGK 

       370        380        390        400        410        420 
DLVIQAGGGV MGHPDGPRAG AKALRDAIDA ALEGVDLEEK AKSSPELKKA LDKWGYLKPK 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81280.1.
RefSeqNP_578885.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U1P9.
SMRQ8U1P9. Positions 1-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1156.

Proteomic databases

PRIDEQ8U1P9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81280; AAL81280; PF1156.
GeneID1469025.
KEGGpfu:PF1156.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
ProtClustDBPRK04208.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01133. RuBisCO_L_type3.
InterProIPR017712. RuBisCO_III.
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.
TIGRFAMsTIGR03326. rubisco_III. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRBL_PYRFU
AccessionPrimary (citable) accession number: Q8U1P9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 79 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