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G0HNE1 (G0HNE1_THES4) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 19. 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 AEK73792.1
Ordered Locus Names:GQS_09490 EMBL AEK73792.1
OrganismThermococcus sp. (strain CGMCC 1.5172 / 4557) [Complete proteome] [HAMAP] EMBL AEK73792.1
Taxonomic identifier1042877 [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
G0HNE1 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 7636B3F260130FC7

FASTA44450,281
        10         20         30         40         50         60 
MVEKFDEIYD YYVDKAYEPN KKRDIIAVFR ITPAKGYTIE AAAGAVAAES STGTWTTLYE 

        70         80         90        100        110        120 
WYEKERWADL SAKAYDFHDM GDGSWIVKIA YPSHAFEDGN MPGFLASIAG NIFGMKRVEW 

       130        140        150        160        170        180 
LRLEDIYLPE RFLRNYPGPN FGIEGVRKKL EIYDRPLYGV VPKPKVGYSP EELYKLANDL 

       190        200        210        220        230        240 
FLGGADYIKD DENLTSPWYN RFEERVKIVT KAMERAENET GEKKTWFANI TAPILEMEER 

       250        260        270        280        290        300 
LEILADYGVP HAMIDVVVLG WGVLDYIREL ADDYGIALHA HRAMHTAFAR NPYHGISMFV 

       310        320        330        340        350        360 
LAKLYRLIGV DQLHIGTAGA GKMEGEKWEV IQYKRIITED HYVPDENDVF HLEQKFYHIK 

       370        380        390        400        410        420 
PVFPTSSGGL HPGNIQPVID ALGKDIVLQL GGGTMGHPDG PKAGAMAVRQ ALDAIMQGIP 

       430        440 
LDEYAKSHRE LARALEKWGH VTPV 

« Hide

References

[1]"Complete Genome Sequence of Thermococcus sp. Strain 4557, a Hyperthermophilic Archaeon Isolated from a Deep-Sea Hydrothermal Vent Area."
Wang X., Gao Z., Xu X., Ruan L.
J. Bacteriol. 193:5544-5545(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CGMCC 1.5172 / 4557.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002920 Genomic DNA. Translation: AEK73792.1.
RefSeqYP_004763469.1. NC_015865.1.

3D structure databases

ProteinModelPortalG0HNE1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEK73792; AEK73792; GQS_09490.
GeneID11016580.
KEGGthe:GQS_09490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycTSP1042877:GHEX-1932-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 nameG0HNE1_THES4
AccessionPrimary (citable) accession number: G0HNE1
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)