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B7R258 (B7R258_9EURY) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 32. 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
ORF Names:TAM4_1764 EMBL EEB74397.1
OrganismThermococcus sp. AM4 [Complete proteome] EMBL EEB74397.1
Taxonomic identifier246969 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length444 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

Region367 – 3693Substrate binding By similarity HAMAP-Rule MF_01133
Region389 – 3924Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1631Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2811Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1891Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1911Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium By similarity HAMAP-Rule MF_01133
Binding site1651Substrate By similarity HAMAP-Rule MF_01133
Binding site2821Substrate By similarity HAMAP-Rule MF_01133
Binding site3141Substrate By similarity HAMAP-Rule MF_01133
Site3221Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1891N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
B7R258 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 8BD0A123C21ED7CB

FASTA44449,807
        10         20         30         40         50         60 
MVEKFDKIYD YYVDKGYEPN KKRDIIAVFR VTPAEGYTIE AAAGAVAAES STGTWTTLYP 

        70         80         90        100        110        120 
WYEQERWADL SAKAYDFIDM GDGSWIVRIA YPFHAFEEWN LPGLLASIAG NVFGMKRVKG 

       130        140        150        160        170        180 
LRLEDLYIPE IVLRNFNGPA FGIEGVRKML EIYDRPLYGV VPKPKVGYSP EEFEKLAYEL 

       190        200        210        220        230        240 
LSNGADYMKD DENLTSPWYN RFDERAEIVA RVIDKVENET GEKKTWFANI TADVREMERR 

       250        260        270        280        290        300 
LEILADLGLK HAMVDVVITG WGALEYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV 

       310        320        330        340        350        360 
LAKLYRIIGI DQLHVGTAGA GKLEGGKWDV IQNARILREE TYTPDENDVF HLEQKFYGMK 

       370        380        390        400        410        420 
PAFPTSSGGL HPGNIEPVIE ALGKDIVLQL GGGTLGHPDG PGAGARAVRQ AIDAIMQGIP 

       430        440 
LDEYAKTHKE LARALEKWGH VTPV 

« Hide

References

[1]Bartlett D., Bonch-Osmolovskaya E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: AM4 EMBL EEB74397.1.
[2]"Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide."
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.
J. Bacteriol. 193:7019-7020(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: AM4 EMBL EEB74397.1.
[3]Oger P.M., Solokova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H., Bonch-Osmoloskaya E.A., Lebedinsky A.V.
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: AM4 EMBL EEB74397.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002952 Genomic DNA. Translation: EEB74397.1.
RefSeqYP_002582810.1. NC_016051.1.

3D structure databases

ProteinModelPortalB7R258.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEEB74397; EEB74397; TAM4_1764.
GeneID7419691.
KEGGtha:TAM4_1764.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameB7R258_9EURY
AccessionPrimary (citable) accession number: B7R258
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)