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F0LLL8 (F0LLL8_THEBM) 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:TERMP_00818 EMBL ADT83795.1
OrganismThermococcus barophilus (strain DSM 11836 / MP) [Complete proteome] [HAMAP] EMBL ADT83795.1
Taxonomic identifier391623 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length444 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

Region367 – 3693Substrate binding By similarity HAMAP-Rule MF_01133
Region389 – 3924Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1631Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2811Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1891Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1911Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium By similarity HAMAP-Rule MF_01133
Binding site1651Substrate By similarity HAMAP-Rule MF_01133
Binding site2821Substrate By similarity HAMAP-Rule MF_01133
Binding site3141Substrate By similarity HAMAP-Rule MF_01133
Site3221Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1891N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
F0LLL8 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 8912158B172E6588

FASTA44449,883
        10         20         30         40         50         60 
MSEKFDKIYD YYVDKSYEPN KKRDIIAVFR ITPAEGYSIE AVAGGVAAES STGTWTTLYN 

        70         80         90        100        110        120 
WYEEERWADL SAKAYDFHDM GDGSWIVKIA YPFHAFEEAN LPGLLASIAG NIFGMRRAKA 

       130        140        150        160        170        180 
LRLEDIYFPE KLIREFDGPA FGMEGVRKML EIKDRPIYGV VPKPKVGYSP EEFEKLATEL 

       190        200        210        220        230        240 
LMNGADYMKD DENLTSPWYN RFEERAEIIA RIIEKVENET GEKKTWFANI TANVPEMEER 

       250        260        270        280        290        300 
LEILADLGLK HAMVDVVITG WGALQYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV 

       310        320        330        340        350        360 
LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARIFRES HYKPDENDVF HLEQKFYHIK 

       370        380        390        400        410        420 
AGFPTSSGGL HPGNLPIVFD ALGTDIVIQV GGGTLGHPDG PAAGARAVRQ AIDAYMQGIP 

       430        440 
LDEYAKTHEE LARALEKWGH VTPV 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic, piezophilic, heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP."
Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.
J. Bacteriol. 193:1481-1482(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11836 / MP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002372 Genomic DNA. Translation: ADT83795.1.
RefSeqYP_004071018.1. NC_014804.1.

3D structure databases

ProteinModelPortalF0LLL8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADT83795; ADT83795; TERMP_00818.
GeneID10041136.
KEGGtba:TERMP_00818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAIFRESHY.

Enzyme and pathway databases

BioCycTBAR391623:GH3I-839-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 nameF0LLL8_THEBM
AccessionPrimary (citable) accession number: F0LLL8
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 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)