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O28635 (RBL_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:rbcL
Ordered Locus Names:AF_1638
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Enzyme regulation

Reversibly inhibited by O2. HAMAP-Rule MF_01133

Subunit structure

Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.

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.

Biophysicochemical properties

Temperature dependence:

Active over a broad temperature range. HAMAP-Rule MF_01133

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062671

Regions

Region364 – 3663Substrate binding By similarity
Region386 – 3894Substrate binding By similarity

Sites

Active site1601Proton acceptor By similarity
Active site2781Proton acceptor By similarity
Metal binding1861Magnesium; via carbamate group By similarity
Metal binding1881Magnesium By similarity
Metal binding1891Magnesium By similarity
Binding site1621Substrate By similarity
Binding site2791Substrate By similarity
Binding site3111Substrate By similarity
Site3191Transition state stabilizer By similarity

Amino acid modifications

Modified residue1861N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O28635 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F191B4A83F36F3FD

FASTA44148,557
        10         20         30         40         50         60 
MAEFEIYREY VDKSYEPQKD DIVAVFRITP AEGFTIEDAA GAVAAESSTG TWTSLHPWYD 

        70         80         90        100        110        120 
EERVKGLSAK AYDFVDLGDG SSIVRIAYPS ELFEPHNMPG LLASIAGNVF GMKRVKGLRL 

       130        140        150        160        170        180 
EDLQLPKSFL KDFKGPSKGK EGVKKIFGVA DRPIVGTVPK PKVGYSAEEV EKLAYELLSG 

       190        200        210        220        230        240 
GMDYIKDDEN LTSPAYCRFE ERAERIMKVI EKVEAETGEK KSWFANITAD VREMERRLKL 

       250        260        270        280        290        300 
VAELGNPHVM VDVVITGWGA LEYIRDLAED YDLAIHGHRA MHAAFTRNAK HGISMFVLAK 

       310        320        330        340        350        360 
LYRIIGIDQL HIGTAGAGKL EGQKWDTVQN ARIFSEVEYT PDEGDAFHLS QNFHHIKPAM 

       370        380        390        400        410        420 
PVSSGGLHPG NLEPVIDALG KEIVIQVGGG VLGHPMGAKA GAKAVRQALD AIISAIPLEE 

       430        440 
HAKQHPELQA ALEKWGRVTP I 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89603.1.
PIRE69454.
RefSeqNP_070466.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28635.
SMRO28635. Positions 10-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF1638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89603; AAB89603; AF_1638.
GeneID1484861.
KEGGafu:AF1638.

Phylogenomic databases

eggNOGCOG1850.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-1672-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 nameRBL_ARCFU
AccessionPrimary (citable) accession number: O28635
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 98 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