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C6A4V2

- C6A4V2_THESM

UniProt

C6A4V2 - C6A4V2_THESM

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, TSIB_1596
Organism
Thermococcus sibiricus (strain MM 739 / DSM 12597)
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 sitei166 – 1661Proton acceptor By similarityUniRule annotation
Binding sitei168 – 1681Substrate By similarityUniRule annotation
Metal bindingi192 – 1921Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi194 – 1941Magnesium By similarityUniRule annotation
Metal bindingi195 – 1951Magnesium By similarityUniRule annotation
Active sitei284 – 2841Proton acceptor By similarityUniRule annotation
Binding sitei285 – 2851Substrate By similarityUniRule annotation
Binding sitei317 – 3171Substrate By similarityUniRule annotation
Sitei325 – 3251Transition 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 annotationImported, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTSIB604354:GHMS-1639-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:TSIB_1596Imported
OrganismiThermococcus sibiricus (strain MM 739 / DSM 12597)Imported
Taxonomic identifieri604354 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000009079: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-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

Protein-protein interaction databases

STRINGi604354.TSIB_1596.

Structurei

3D structure databases

ProteinModelPortaliC6A4V2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3723Substrate binding By similarityUniRule annotation
Regioni392 – 3954Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.

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.

C6A4V2-1 [UniParc]FASTAAdd to Basket

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MVKMPEKFDK IYDYYVDKNY EPNFKRDIVA VFRITPTDGY TIEQAAGAVA    50
AESSTGTWTT LYPWYEEERW SDLSAKAYYF HDMGDGSWIV RVAYPAHAFE 100
EWNLPGLLAS IAGNVFGMKR VKGLRLEDLY LPEIVLRDFS GPNKGIKGVR 150
ETLEIKDRPI YGVVPKPKVG YSPEELEKLS YELLSAGADY IKDDENLTGP 200
WYNRFEERAD VMARVIDRVE AETGEKKTWF ANITADIREM ENRLEILAEY 250
GLPHAMVDVV IVGWASLEYI RDLAEDYDIA LHAHRAMHAT FTRNHYHGIS 300
MFVLAKLYRI IGLDQLHVGT AGAGKLEGEK WDVIQNARIL REEHYKPDKN 350
DVFHLDQKFY HIKPAFPTSS GGLHPGNLPQ VINALGSDIV LQLGGGTLGH 400
PDGPAAGAKA VRQALDAIMQ GISLDEYAKT HKELARALEK WGHVTPV 447
Length:447
Mass (Da):50,441
Last modified:September 1, 2009 - v1
Checksum:i3864194B64ADDBB5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001463 Genomic DNA. Translation: ACS90647.1.
RefSeqiYP_002994996.1. NC_012883.1.

Genome annotation databases

EnsemblBacteriaiACS90647; ACS90647; TSIB_1596.
GeneIDi8096606.
KEGGitsi:TSIB_1596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001463 Genomic DNA. Translation: ACS90647.1 .
RefSeqi YP_002994996.1. NC_012883.1.

3D structure databases

ProteinModelPortali C6A4V2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 604354.TSIB_1596.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACS90647 ; ACS90647 ; TSIB_1596 .
GeneIDi 8096606.
KEGGi tsi:TSIB_1596.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.

Enzyme and pathway databases

BioCyci TSIB604354:GHMS-1639-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. "Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
    Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
    Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MM 739 / DSM 12597.

Entry informationi

Entry nameiC6A4V2_THESM
AccessioniPrimary (citable) accession number: C6A4V2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: September 3, 2014
This is version 37 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

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