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D2REY6 (D2REY6_ARCPA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 33. 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:Arcpr_1634 EMBL ADB58680.1
OrganismArchaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18) [Complete proteome] [HAMAP] EMBL ADB58680.1
Taxonomic identifier572546 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length447 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

Region370 – 3723Substrate binding By similarity HAMAP-Rule MF_01133
Region392 – 3954Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1661Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2841Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01133
Binding site1681Substrate By similarity HAMAP-Rule MF_01133
Binding site2851Substrate By similarity HAMAP-Rule MF_01133
Binding site3171Substrate By similarity HAMAP-Rule MF_01133
Site3251Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1921N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
D2REY6 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 1C59F7CBE3BCBA72

FASTA44750,333
        10         20         30         40         50         60 
MLHRTRVMPD FEMYFEYVDK SYEPSERDLI AVFRVKPSEG FKIEDVAGAI ASESSTGTWT 

        70         80         90        100        110        120 
TLYDWCDKDR IKKLSAKAYE FIDLEDGSWI VKIAYPVELF ERGSITCLLA SIAGNIFGMK 

       130        140        150        160        170        180 
RVAGLRLEDV YLPKEFLKYF EGPNFGKDVR KIFKVYDRPI VGTVPKPKVG YTPDEVEKLA 

       190        200        210        220        230        240 
YELLSGGMDY IKDDENLTSQ DFCKFEERAK AIMKAIDKAE SDTGEKKVWF ANITGDVKEM 

       250        260        270        280        290        300 
EKRMKIVADY GNPYVMIDVV IAGWSVLKYM RELANDYGLA IHAHRAMHSA FTRNRYHGIS 

       310        320        330        340        350        360 
MFVLAKLYRV IGVDQLHIGT AGYGKLEGGM WEVVQYAKIL RESSYVPDEK DIFHIKQEFH 

       370        380        390        400        410        420 
HIKPAMPVSS GGLHPGNVAG VIDALGEDII IQVGGGVMGH PDGPKAGAKA VRQALEAIKL 

       430        440 
GIPLDEYAKD HKELAKALEK WGYVKPV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001857 Genomic DNA. Translation: ADB58680.1.
RefSeqYP_003401353.1. NC_013741.1.

3D structure databases

ProteinModelPortalD2REY6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB58680; ADB58680; Arcpr_1634.
GeneID8740327.
KEGGapo:Arcpr_1634.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycAPRO572546:GJI1-1685-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 nameD2REY6_ARCPA
AccessionPrimary (citable) accession number: D2REY6
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: June 11, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)