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C5A1I4 (C5A1I4_THEGJ) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 39. 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 ACS34253.1
Ordered Locus Names:TGAM_1751 EMBL ACS34253.1
OrganismThermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3) [Complete proteome] [HAMAP] EMBL ACS34253.1
Taxonomic identifier593117 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length488 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

Region411 – 4133Substrate binding By similarity HAMAP-Rule MF_01133
Region433 – 4364Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site2071Proton acceptor By similarity HAMAP-Rule MF_01133
Active site3251Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding2331Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding2351Magnesium By similarity HAMAP-Rule MF_01133
Metal binding2361Magnesium By similarity HAMAP-Rule MF_01133
Binding site2091Substrate By similarity HAMAP-Rule MF_01133
Binding site3261Substrate By similarity HAMAP-Rule MF_01133
Binding site3581Substrate By similarity HAMAP-Rule MF_01133
Site3661Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue2331N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
C5A1I4 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 60A0F453AC3CDFFC

FASTA48855,159
        10         20         30         40         50         60 
MADPFSFLCP YLGRKFNKPL FPSFLPPARR LNSRRGENPL RWLRMVEKFD KIYDYYVDKD 

        70         80         90        100        110        120 
YEPNKKRDII AVFRVTPAEG YTIEQAAGAV AAESSTGTWT TLYPWYEQER WADLSAKAYD 

       130        140        150        160        170        180 
FIDMGDGSWI VKIAYPFHAF EEWNLPGLLA SIAGNVFGMK RVKGLRLEDL YFPEIVLRNF 

       190        200        210        220        230        240 
SGPAFGIEGV RKMLEIYDRP LYGVVPKPKV GYSPEEFEKL AYELLSNGAD YIKDDENLTS 

       250        260        270        280        290        300 
PWYNRFDERA EIVTRVIDKV ENETGEKKTW FANITADIRE MERRLEVLAD LGLKHAMVDV 

       310        320        330        340        350        360 
VITGWGALEY IRDLAADYGL AIHGHRAMHA AFTRNKYHGI SMFVLAKLYR IIGIDQLHVG 

       370        380        390        400        410        420 
TAGAGKLEGG KWDVIQNARI LREETYKPDE NDVFHLEQKF YGMKAAFPTS SGGLHPGNIE 

       430        440        450        460        470        480 
PVIEALGKDI VLQLGGGTLG HPDGPGAGAR AVRQAIDAIM QGIPLDEYAK THKELARALE 


KWGHVTPV 

« Hide

References

[1]"Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea."
Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.
Genome Biol. 10:R70.1-R70.23(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15229 / JCM 11827 / EJ3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001398 Genomic DNA. Translation: ACS34253.1.
RefSeqYP_002960117.1. NC_012804.1.

3D structure databases

ProteinModelPortalC5A1I4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING593117.TGAM_1751.

Proteomic databases

PaxDbC5A1I4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS34253; ACS34253; TGAM_1751.
GeneID7987470.
KEGGtga:TGAM_1751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAVIVTFRV.

Enzyme and pathway databases

BioCycTGAM593117:GHFT-1782-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 nameC5A1I4_THEGJ
AccessionPrimary (citable) accession number: C5A1I4
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)