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F0LLL8

- F0LLL8_THEBM

UniProt

F0LLL8 - F0LLL8_THEBM

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Protein

Ribulose bisphosphate carboxylase

Gene
rbcL, TERMP_00818
Organism
Thermococcus barophilus (strain DSM 11836 / MP)
Status
Unreviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei163 – 1631Proton acceptor By similarityUniRule annotation
Binding sitei165 – 1651Substrate By similarityUniRule annotation
Metal bindingi189 – 1891Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi191 – 1911Magnesium By similarityUniRule annotation
Metal bindingi192 – 1921Magnesium By similarityUniRule annotation
Active sitei281 – 2811Proton acceptor By similarityUniRule annotation
Binding sitei282 – 2821Substrate By similarityUniRule annotation
Binding sitei314 – 3141Substrate By similarityUniRule annotation
Sitei322 – 3221Transition state stabilizer By similarityUniRule 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-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF0LLL8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 3693Substrate binding By similarityUniRule annotation
Regioni389 – 3924Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiIFRESHY.

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

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MSEKFDKIYD YYVDKSYEPN KKRDIIAVFR ITPAEGYSIE AVAGGVAAES    50
STGTWTTLYN WYEEERWADL SAKAYDFHDM GDGSWIVKIA YPFHAFEEAN 100
LPGLLASIAG NIFGMRRAKA LRLEDIYFPE KLIREFDGPA FGMEGVRKML 150
EIKDRPIYGV VPKPKVGYSP EEFEKLATEL LMNGADYMKD DENLTSPWYN 200
RFEERAEIIA RIIEKVENET GEKKTWFANI TANVPEMEER LEILADLGLK 250
HAMVDVVITG WGALQYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV 300
LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARIFRES HYKPDENDVF 350
HLEQKFYHIK AGFPTSSGGL HPGNLPIVFD ALGTDIVIQV GGGTLGHPDG 400
PAAGARAVRQ AIDAYMQGIP LDEYAKTHEE LARALEKWGH VTPV 444
Length:444
Mass (Da):49,883
Last modified:May 3, 2011 - v1
Checksum:i8912158B172E6588
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP002372 Genomic DNA. Translation: ADT83795.1 .
RefSeqi WP_013467093.1. NC_014804.1.
YP_004071018.1. NC_014804.1.

3D structure databases

ProteinModelPortali F0LLL8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADT83795 ; ADT83795 ; TERMP_00818 .
GeneIDi 10041136.
KEGGi tba:TERMP_00818.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi IFRESHY.

Enzyme and pathway databases

BioCyci TBAR391623:GH3I-839-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01133. RuBisCO_L_type3.
InterProi IPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
ProtoNeti Search...

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 / MP.

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: September 3, 2014
This is version 22 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 By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi