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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
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 sitei160 – 1601Proton acceptorUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Metal bindingi186 – 1861Magnesium; via carbamate groupUniRule annotation
Metal bindingi188 – 1881MagnesiumUniRule annotation
Metal bindingi189 – 1891MagnesiumUniRule annotation
Active sitei278 – 2781Proton acceptorUniRule annotation
Binding sitei279 – 2791SubstrateUniRule annotation
Binding sitei311 – 3111SubstrateUniRule annotation
Sitei319 – 3191Transition 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

BioCyciHBUT415426:GC56-503-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:Hbut_0503Imported
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)Imported
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861N6-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

Protein-protein interaction databases

STRINGi415426.Hbut_0503.

Structurei

3D structure databases

ProteinModelPortaliA2BK54.
SMRiA2BK54. Positions 12-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663Substrate bindingUniRule annotation
Regioni386 – 3894Substrate 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.
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.

A2BK54-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHEHFDSIYL EFVDESYKPG KDEVIAVFRV TPAQGISIKD AAGRIAAESS
60 70 80 90 100
VGTWTTLSVK PSWFEKLKAK AYRFHDLGDG SWLVWVAYPV ELFEEGSIPN
110 120 130 140 150
FASSILGNIF GMKAIAGLRV EDVYFPPSYL ETFPGPNKGI QGVREILGIK
160 170 180 190 200
DRPILATVPK PKLGYTPEEY GRVAYEILIG GIDLVKDDEN FASQPFCRFE
210 220 230 240 250
ARLKEVMKAI DRAEKETGER KGYLANVTAP IREMEKRIKL VADYGNKFIM
260 270 280 290 300
IDFLTAGWAA LQHARELAEE YDLAIHGHRA FHAAFTRNPK HGVSMFLVAK
310 320 330 340 350
LARMAGVDHV HVGTPGVGKM DAKTREVLEH TRIVREQYYR PKEGDLFHLE
360 370 380 390 400
QPWSNIKPVF PVASGGLHPG TLPEVIRVMG KDIIMQVGGG VLGHPDGPEA
410 420 430 440
GARAVRQAVE AAMKGISLDE YAREHRELAR ALEKWGYVRP V
Length:441
Mass (Da):49,178
Last modified:February 20, 2007 - v1
Checksum:iF8A627C6D6189C16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM80365.1.
RefSeqiYP_001012710.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM80365; ABM80365; Hbut_0503.
GeneIDi4781477.
KEGGihbu:Hbut_0503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM80365.1.
RefSeqiYP_001012710.1. NC_008818.1.

3D structure databases

ProteinModelPortaliA2BK54.
SMRiA2BK54. Positions 12-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi415426.Hbut_0503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM80365; ABM80365; Hbut_0503.
GeneIDi4781477.
KEGGihbu:Hbut_0503.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciHBUT415426:GC56-503-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
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. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403Imported.

Entry informationi

Entry nameiA2BK54_HYPBU
AccessioniPrimary (citable) accession number: A2BK54
Entry historyi
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: February 4, 2015
This is version 52 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.