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Q9UZD7 (RBL_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:rbcL
Ordered Locus Names:PYRAB12110
ORF Names:PAB1580
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length424 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.

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).

Sequence similarities

Belongs to the RuBisCO large chain family. Type III subfamily.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
   LigandMagnesium
Metal-binding
   Molecular functionLyase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processAMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

carbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062675

Regions

Region347 – 3493Substrate binding By similarity
Region369 – 3724Substrate binding By similarity

Sites

Active site1591Proton acceptor By similarity
Active site2771Proton acceptor By similarity
Metal binding1851Magnesium; via carbamate group By similarity
Metal binding1871Magnesium By similarity
Metal binding1881Magnesium By similarity
Binding site1611Substrate By similarity
Binding site2781Substrate By similarity
Binding site3101Substrate By similarity
Site3171Transition state stabilizer By similarity

Amino acid modifications

Modified residue1851N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UZD7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CFBC3EEDB1D16A1F

FASTA42447,606
        10         20         30         40         50         60 
MVSSMKVEWY LDFVDLNYEP GRDELIVEYY FEPNGVSPEE AAGRIASESS IGTWTTLWKL 

        70         80         90        100        110        120 
PEMAKRSMAK VFYLEKHGEG YIAKIAYPLT LFEEGSLVQL FSAIAGNVFG MKALKNLRLL 

       130        140        150        160        170        180 
DFHPPYEYLR HFKGPQFGVK GIREFMGIKD RPLTATVPKP KMGWSVEEYA EIAYELWSGG 

       190        200        210        220        230        240 
IDLLKDDENF TSFPFNRFEE RVKKLYRVRD RVEAETGETK EYLINITGPV NVMEKRAELV 

       250        260        270        280        290        300 
ANEGGQYVMI DIVVAGWSAL QYMREVTEDL GLAIHAHRAM HAAFTRNPKH GITMFALAKA 

       310        320        330        340        350        360 
ARMIGVDQIH TGTAVGKMAG DYEEIKKIND FLLSKWEHIR PVFPVASGGL HPGLMPELIR 

       370        380        390        400        410        420 
LFGKDLVIQA GGGVMGHPDG PRAGAKALRD AIDAAIEGLD LEEKAKSSPE LKKALDKWGY 


LKPK 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248286 Genomic DNA. Translation: CAB50122.1.
HE613800 Genomic DNA. Translation: CCE70647.1.
PIRE75102.
RefSeqNP_126892.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UZD7.
SMRQ9UZD7. Positions 8-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50122; CAB50122; PAB1580.
GeneID1496593.
KEGGpab:PAB1580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

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 nameRBL_PYRAB
AccessionPrimary (citable) accession number: Q9UZD7
Secondary accession number(s): G8ZKK4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families