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D7D9Q5 (D7D9Q5_STAHD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Shell_1412
OrganismStaphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8) [Complete proteome] [HAMAP]
Taxonomic identifier591019 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus ›

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_01133

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form III RuBisCO are composed solely of large subunits 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

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 site1101Substrate; in homodimeric partner 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
Binding site3661Substrate 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

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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...

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.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 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: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info