Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D7D9Q5 (D7D9Q5_STAHD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 25. 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 attributes

Sequence length443 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

Region366 – 3683Substrate binding By similarity HAMAP-Rule MF_01133
Region388 – 3914Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1621Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2801Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1881Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1901Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1911Magnesium By similarity HAMAP-Rule MF_01133
Binding site1641Substrate By similarity HAMAP-Rule MF_01133
Binding site2811Substrate By similarity HAMAP-Rule MF_01133
Binding site3131Substrate By similarity HAMAP-Rule MF_01133
Site3211Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1881N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
D7D9Q5 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 4C7B43A1C1960033

FASTA44349,518
        10         20         30         40         50         60 
MSHTFEPYHS YVDKNYVPDP DNDIIAVFRI KPAKGFTIED AAGGVAAESS TGTWTTLYPW 

        70         80         90        100        110        120 
YDTERVRKLS GKAYYFKDLG DGSWIVRIAY PAELFEEANM PGLLASIAGN VFGMKRVEGL 

       130        140        150        160        170        180 
RLEDIYLPKK FLQYFKGPSK GVDGVRKIFG INDRPIVGTV PKPKVGYSPE EVEKLAYELL 

       190        200        210        220        230        240 
VGGIDYIKDD ENMTSPSFCR FSERAKHIMR AIDRAEKETG ERKVWFANIT SDIREMEKRL 

       250        260        270        280        290        300 
KLVADYGNPY VMVDVVVTGW SALTYIRDLA EEYGLAIHAH RAMHSAFTRN PYHGISMYVL 

       310        320        330        340        350        360 
AKLYRIIGVD QLHIGTAGVG KLEGGKIEVI RYARILREKH FKPDPDDIFH LEQEMHHIKP 

       370        380        390        400        410        420 
AMPVSSGGLH PGNLPGVIEA LGTELILQIG GGVLGHPDGP RAGAMAVRQS LEAILKGVPL 

       430        440 
DEYAKTHREL ARALEKWGFA KPI 

« Hide

References

[1]"Complete sequence of Staphylothermus hellenicus DSM 12710."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002051 Genomic DNA. Translation: ADI32501.1.
RefSeqYP_003669400.1. NC_014205.1.

3D structure databases

ProteinModelPortalD7D9Q5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI32501; ADI32501; Shell_1412.
GeneID9234703.
KEGGshc:Shell_1412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycSHEL591019:GC4A-1449-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 nameD7D9Q5_STAHD
AccessionPrimary (citable) accession number: D7D9Q5
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: February 19, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)