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E8RAK5 (E8RAK5_DESM0) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 21. 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:Desmu_1141 EMBL ADV65441.1
OrganismDesulfurococcus mucosus (strain ATCC 35584 / DSM 2162 / JCM 9187 / O7/1) [Complete proteome] [HAMAP] EMBL ADV65441.1
Taxonomic identifier765177 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeDesulfurococcus

Protein attributes

Sequence length445 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

Region368 – 3703Substrate binding By similarity HAMAP-Rule MF_01133
Region390 – 3934Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1641Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2821Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1901Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1931Magnesium By similarity HAMAP-Rule MF_01133
Binding site1661Substrate By similarity HAMAP-Rule MF_01133
Binding site2831Substrate By similarity HAMAP-Rule MF_01133
Binding site3151Substrate By similarity HAMAP-Rule MF_01133
Site3231Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1901N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
E8RAK5 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: B2BC578CEDE48E49

FASTA44549,623
        10         20         30         40         50         60 
MSSKFDFETY HEYVNRDYNP DPDNDVVAVF RVKPAPGFTI EDAAGGVAAE SSTGTWTSLY 

        70         80         90        100        110        120 
SWYDVTRVRR LSGKAYFFRD LGDGSWIVRI AYPVELFEEG NIPGLLASIA GNIFGMKRVE 

       130        140        150        160        170        180 
ALRLEDIYLP RKFLESFKGP SKGVAGVKEI FKVSDRPIVG TVPKPKEGYS PDEVEKLAFE 

       190        200        210        220        230        240 
LLSGGLDYVK DDENLTSPSF CRFEARAKAI MRVIDKVEKE TGERKAWFAN ITSDIREMEK 

       250        260        270        280        290        300 
RLRLVADYGN PYVMVDVVIT GWSALTYIRD IAEEYGLAIH GHRAMHAAFT RNPYHGISMY 

       310        320        330        340        350        360 
VLAKLYRIIG IDQLHIGTAG AGKLEGGKID VIRYARILRE NHFKPDQDDQ FHLEQPMHHI 

       370        380        390        400        410        420 
KPAMPVSSGG LHPGNIQPVI EALGSNIVLQ IGGGVIGHPD GPRAGALAVR QALEAISKGI 

       430        440 
PLDEYMKTHR ELARAIEKWG FVKPI 

« Hide

References

[1]"The complete genome of Desulfurococcus mucosus DSM 2162."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Chertkov O., Held B., Brettin T., Detter J.C., Tapia R., Han C., Land M. expand/collapse author list , Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Wirth R., Bilek Y., Hader T., Klenk H.-P., Eisen J.A.
Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35584 / DSM 2162 / JCM 9187 / O7/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002363 Genomic DNA. Translation: ADV65441.1.
RefSeqYP_004176923.1. NC_014961.1.

3D structure databases

ProteinModelPortalE8RAK5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV65441; ADV65441; Desmu_1141.
GeneID10153855.
KEGGdmu:Desmu_1141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycDMUC765177:GHQE-1178-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 nameE8RAK5_DESM0
AccessionPrimary (citable) accession number: E8RAK5
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: June 11, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)