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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermococcus barophilus (strain DSM 11836 / MP)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei163 – 1631Proton acceptorUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Metal bindingi189 – 1891Magnesium; via carbamate groupUniRule annotation
Metal bindingi191 – 1911MagnesiumUniRule annotation
Metal bindingi192 – 1921MagnesiumUniRule annotation
Active sitei281 – 2811Proton acceptorUniRule annotation
Binding sitei282 – 2821SubstrateUniRule annotation
Binding sitei314 – 3141SubstrateUniRule annotation
Sitei322 – 3221Transition state stabilizerUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. oxidoreductase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. AMP catabolic process Source: UniProtKB-HAMAP
  2. carbon fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTBAR391623:GH3I-839-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Ordered Locus Names:TERMP_00818Imported
OrganismiThermococcus barophilus (strain DSM 11836 / MP)Imported
Taxonomic identifieri391623 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000007478: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF0LLL8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 3693Substrate bindingUniRule annotation
Regioni389 – 3924Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
InterProiIPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

Sequencei

Sequence statusi: Complete.

F0LLL8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEKFDKIYD YYVDKSYEPN KKRDIIAVFR ITPAEGYSIE AVAGGVAAES
60 70 80 90 100
STGTWTTLYN WYEEERWADL SAKAYDFHDM GDGSWIVKIA YPFHAFEEAN
110 120 130 140 150
LPGLLASIAG NIFGMRRAKA LRLEDIYFPE KLIREFDGPA FGMEGVRKML
160 170 180 190 200
EIKDRPIYGV VPKPKVGYSP EEFEKLATEL LMNGADYMKD DENLTSPWYN
210 220 230 240 250
RFEERAEIIA RIIEKVENET GEKKTWFANI TANVPEMEER LEILADLGLK
260 270 280 290 300
HAMVDVVITG WGALQYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV
310 320 330 340 350
LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARIFRES HYKPDENDVF
360 370 380 390 400
HLEQKFYHIK AGFPTSSGGL HPGNLPIVFD ALGTDIVIQV GGGTLGHPDG
410 420 430 440
PAAGARAVRQ AIDAYMQGIP LDEYAKTHEE LARALEKWGH VTPV
Length:444
Mass (Da):49,883
Last modified:May 3, 2011 - v1
Checksum:i8912158B172E6588
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002372 Genomic DNA. Translation: ADT83795.1.
RefSeqiWP_013467093.1. NC_014804.1.
YP_004071018.1. NC_014804.1.

Genome annotation databases

EnsemblBacteriaiADT83795; ADT83795; TERMP_00818.
GeneIDi10041136.
KEGGitba:TERMP_00818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002372 Genomic DNA. Translation: ADT83795.1.
RefSeqiWP_013467093.1. NC_014804.1.
YP_004071018.1. NC_014804.1.

3D structure databases

ProteinModelPortaliF0LLL8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADT83795; ADT83795; TERMP_00818.
GeneIDi10041136.
KEGGitba:TERMP_00818.

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciTBAR391623:GH3I-839-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
InterProiIPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.
ProtoNetiSearch...

Publicationsi

  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 / MPImported.

Entry informationi

Entry nameiF0LLL8_THEBM
AccessioniPrimary (citable) accession number: F0LLL8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: February 4, 2015
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.