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A2BK54

- A2BK54_HYPBU

UniProt

A2BK54 - A2BK54_HYPBU

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Protein

Ribulose bisphosphate carboxylase

Gene
rbcL, Hbut_0503
Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
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 sitei160 – 1601Proton acceptor By similarityUniRule annotation
Binding sitei162 – 1621Substrate By similarityUniRule annotation
Metal bindingi186 – 1861Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi188 – 1881Magnesium By similarityUniRule annotation
Metal bindingi189 – 1891Magnesium By similarityUniRule annotation
Active sitei278 – 2781Proton acceptor By similarityUniRule annotation
Binding sitei279 – 2791Substrate By similarityUniRule annotation
Binding sitei311 – 3111Substrate By similarityUniRule annotation
Sitei319 – 3191Transition state stabilizer By similarityUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: InterPro
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-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

STRINGi415426.Hbut_0503.

Structurei

3D structure databases

ProteinModelPortaliA2BK54.
SMRiA2BK54. Positions 12-440.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663Substrate binding By similarityUniRule annotation
Regioni386 – 3894Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Belongs to the RuBisCO large chain family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.

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

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MHEHFDSIYL EFVDESYKPG KDEVIAVFRV TPAQGISIKD AAGRIAAESS    50
VGTWTTLSVK PSWFEKLKAK AYRFHDLGDG SWLVWVAYPV ELFEEGSIPN 100
FASSILGNIF GMKAIAGLRV EDVYFPPSYL ETFPGPNKGI QGVREILGIK 150
DRPILATVPK PKLGYTPEEY GRVAYEILIG GIDLVKDDEN FASQPFCRFE 200
ARLKEVMKAI DRAEKETGER KGYLANVTAP IREMEKRIKL VADYGNKFIM 250
IDFLTAGWAA LQHARELAEE YDLAIHGHRA FHAAFTRNPK HGVSMFLVAK 300
LARMAGVDHV HVGTPGVGKM DAKTREVLEH TRIVREQYYR PKEGDLFHLE 350
QPWSNIKPVF PVASGGLHPG TLPEVIRVMG KDIIMQVGGG VLGHPDGPEA 400
GARAVRQAVE AAMKGISLDE YAREHRELAR ALEKWGYVRP V 441
Length:441
Mass (Da):49,178
Last modified:February 20, 2007 - v1
Checksum:iF8A627C6D6189C16
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM80365.1.
RefSeqiWP_011821683.1. NC_008818.1.
YP_001012710.1. NC_008818.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM80365.1 .
RefSeqi WP_011821683.1. NC_008818.1.
YP_001012710.1. NC_008818.1.

3D structure databases

ProteinModelPortali A2BK54.
SMRi A2BK54. Positions 12-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 415426.Hbut_0503.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM80365 ; ABM80365 ; Hbut_0503 .
GeneIDi 4781477.
KEGGi hbu:Hbut_0503.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci HBUT415426:GC56-503-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
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. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Brugger 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 9403.

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: September 3, 2014
This is version 47 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, Reference proteome

External Data

Dasty 3

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