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I6V1K5 (I6V1K5_9EURY) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 16. Feed History...

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

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

Short name=RuBisCO HAMAP-Rule MF_01133
EC=4.1.1.39 HAMAP-Rule MF_01133
Gene names
Name:rbcL HAMAP-Rule MF_01133 EMBL AFN03948.1
ORF Names:PFC_05005 EMBL AFN03948.1
OrganismPyrococcus furiosus COM1 [Complete proteome] EMBL AFN03948.1
Taxonomic identifier1185654 [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. HAMAP-Rule MF_01133

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) By similarity. HAMAP-Rule MF_01133

Sequence similarities

Belongs to the RuBisCO large chain family. Type III subfamily. HAMAP-Rule MF_01133

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region343 – 3453Substrate binding By similarity HAMAP-Rule MF_01133
Region365 – 3684Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1551Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2731Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1811Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1831Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1841Magnesium By similarity HAMAP-Rule MF_01133
Binding site1571Substrate By similarity HAMAP-Rule MF_01133
Binding site2741Substrate By similarity HAMAP-Rule MF_01133
Binding site3061Substrate By similarity HAMAP-Rule MF_01133
Site3131Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1811N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
I6V1K5 [UniParc].

Last modified October 3, 2012. 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]"Genome Sequencing of a Genetically Tractable Pyrococcus furiosus Strain Reveals a Highly Dynamic Genome."
Bridger S.L., Lancaster W.A., Poole F.L.II., Schut G.J., Adams M.W.
J. Bacteriol. 194:4097-4106(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COM1 EMBL AFN03948.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003685 Genomic DNA. Translation: AFN03948.1.
RefSeqYP_006492240.1. NC_018092.1.

3D structure databases

ProteinModelPortalI6V1K5.
SMRI6V1K5. Positions 1-411.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEI6V1K5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFN03948; AFN03948; PFC_05005.
GeneID13301761.
KEGGpfi:PFC_05005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycPFUR1185654:GLJ1-992-MONOMER.

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 nameI6V1K5_9EURY
AccessionPrimary (citable) accession number: I6V1K5
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: June 11, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)