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A3DND9 (A3DND9_STAMF) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 50. 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
Ordered Locus Names:Smar_1051 EMBL ABN70149.1
OrganismStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP] EMBL ABN70149.1
Taxonomic identifier399550 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus

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
A3DND9 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: C5D759EF6DED7861

FASTA44349,740
        10         20         30         40         50         60 
MPHKFEPYHS YIDKNYVPDL ENDIIAVFRI KPAKGFTIED AAGGVAAESS TGTWTTLYPW 

        70         80         90        100        110        120 
YNTERVRKLS GKAYYFKDLG DGSWIVRIAY PVELFEEANM PGLLASIAGN VFGMKRVEGL 

       130        140        150        160        170        180 
RLEDIYLPKK FLQYFKGPSK GVEGVKKIFR VTDRPIVGTV PKPKVGYSPE EVEKLAYELL 

       190        200        210        220        230        240 
VGGMDYIKDD ENLTSPSFCR FSERAKHIMR AIDRAEKETG ERKVWFANIT SDIREMEKRL 

       250        260        270        280        290        300 
KLVADYDNPY VMVDVVVTGW STLTYIRDLA EEYGLAIHAH RAMHAAFTRN PYHGISMYVL 

       310        320        330        340        350        360 
AKLYRIIGVD QLHIGTAGVG KLEGGKIDVI RYARILREKH FKPDPDDVFH IEQEMYHIKP 

       370        380        390        400        410        420 
AMPVSSGGLH PGNLPGVIDA LGTELVLQIG GGVLGHPDGP RAGAMAVRQS LEAILKGIPL 

       430        440 
DEYAKTHREL ARALEKWGFA KPI 

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References

[1]"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota."
Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.
BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.
[2]"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1."
Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C.
Stand. Genomic Sci. 1:183-188(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000575 Genomic DNA. Translation: ABN70149.1.
RefSeqYP_001041057.1. NC_009033.1.

3D structure databases

ProteinModelPortalA3DND9.
SMRA3DND9. Positions 11-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399550.Smar_1051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN70149; ABN70149; Smar_1051.
GeneID4906732.
KEGGsmr:Smar_1051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMADDEICAN.

Enzyme and pathway databases

BioCycSMAR399550:GHK2-1083-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 nameA3DND9_STAMF
AccessionPrimary (citable) accession number: A3DND9
Entry history
Integrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: June 11, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)