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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
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 sitei207 – 2071Proton acceptorUniRule annotation
Binding sitei209 – 2091SubstrateUniRule annotation
Metal bindingi233 – 2331Magnesium; via carbamate groupUniRule annotation
Metal bindingi235 – 2351MagnesiumUniRule annotation
Metal bindingi236 – 2361MagnesiumUniRule annotation
Active sitei325 – 3251Proton acceptorUniRule annotation
Binding sitei326 – 3261SubstrateUniRule annotation
Binding sitei358 – 3581SubstrateUniRule annotation
Sitei366 – 3661Transition 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 annotationImported, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTGAM593117:GHFT-1782-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 annotationImported
Ordered Locus Names:TGAM_1751Imported
OrganismiThermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)Imported
Taxonomic identifieri593117 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000001488: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331N6-carboxylysineUniRule annotation

Proteomic databases

PaxDbiC5A1I4.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi593117.TGAM_1751.

Structurei

3D structure databases

ProteinModelPortaliC5A1I4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4133Substrate bindingUniRule annotation
Regioni433 – 4364Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
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.

C5A1I4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADPFSFLCP YLGRKFNKPL FPSFLPPARR LNSRRGENPL RWLRMVEKFD
60 70 80 90 100
KIYDYYVDKD YEPNKKRDII AVFRVTPAEG YTIEQAAGAV AAESSTGTWT
110 120 130 140 150
TLYPWYEQER WADLSAKAYD FIDMGDGSWI VKIAYPFHAF EEWNLPGLLA
160 170 180 190 200
SIAGNVFGMK RVKGLRLEDL YFPEIVLRNF SGPAFGIEGV RKMLEIYDRP
210 220 230 240 250
LYGVVPKPKV GYSPEEFEKL AYELLSNGAD YIKDDENLTS PWYNRFDERA
260 270 280 290 300
EIVTRVIDKV ENETGEKKTW FANITADIRE MERRLEVLAD LGLKHAMVDV
310 320 330 340 350
VITGWGALEY IRDLAADYGL AIHGHRAMHA AFTRNKYHGI SMFVLAKLYR
360 370 380 390 400
IIGIDQLHVG TAGAGKLEGG KWDVIQNARI LREETYKPDE NDVFHLEQKF
410 420 430 440 450
YGMKAAFPTS SGGLHPGNIE PVIEALGKDI VLQLGGGTLG HPDGPGAGAR
460 470 480
AVRQAIDAIM QGIPLDEYAK THKELARALE KWGHVTPV
Length:488
Mass (Da):55,159
Last modified:July 28, 2009 - v1
Checksum:i60A0F453AC3CDFFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001398 Genomic DNA. Translation: ACS34253.1.
RefSeqiYP_002960117.1. NC_012804.1.

Genome annotation databases

EnsemblBacteriaiACS34253; ACS34253; TGAM_1751.
GeneIDi7987470.
KEGGitga:TGAM_1751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001398 Genomic DNA. Translation: ACS34253.1.
RefSeqiYP_002960117.1. NC_012804.1.

3D structure databases

ProteinModelPortaliC5A1I4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi593117.TGAM_1751.

Proteomic databases

PaxDbiC5A1I4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS34253; ACS34253; TGAM_1751.
GeneIDi7987470.
KEGGitga:TGAM_1751.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciTGAM593117:GHFT-1782-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. "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea."
    Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.
    Genome Biol. 10:R70.1-R70.23(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 15229 / JCM 11827 / EJ3Imported.

Entry informationi

Entry nameiC5A1I4_THEGJ
AccessioniPrimary (citable) accession number: C5A1I4
Entry historyi
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: January 7, 2015
This is version 44 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 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.