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F8AF48 (F8AF48_PYRYC) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

Short name=RuBisCO HAMAP-Rule MF_01133
EC=4.1.1.39 HAMAP-Rule MF_01133
Gene names
Name:rbcL HAMAP-Rule MF_01133
Ordered Locus Names:PYCH_00090 EMBL AEH23722.1
OrganismPyrococcus yayanosii (strain CH1 / JCM 16557) [Complete proteome] [HAMAP] EMBL AEH23722.1
Taxonomic identifier529709 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01133

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01133

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01133

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01133

Subunit structure

Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits By similarity. HAMAP-Rule MF_01133

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 (PubMed:17303759) By similarity. HAMAP-Rule MF_01133

Sequence similarities

Belongs to the RuBisCO large chain family. Type III subfamily. HAMAP-Rule MF_01133

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region344 – 3463Substrate binding By similarity HAMAP-Rule MF_01133
Region366 – 3694Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1561Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2741Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1821Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1841Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1851Magnesium By similarity HAMAP-Rule MF_01133
Binding site1581Substrate By similarity HAMAP-Rule MF_01133
Binding site2751Substrate By similarity HAMAP-Rule MF_01133
Binding site3071Substrate By similarity HAMAP-Rule MF_01133
Site3141Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1821N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
F8AF48 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: DC4D0153E37B1599

FASTA42147,126
        10         20         30         40         50         60 
MSKVEWYLDF VDLDYTPGRD ELIVEYYFEP NGVSPEEAAG RIASESSIGT WTTLWKLPDM 

        70         80         90        100        110        120 
AKRSMAKVFS LEKSGEGYIA KIAYPLTLFE EGNLVQLFSA IAGNIFGMKA LKNLRLLDFH 

       130        140        150        160        170        180 
PPYEYLRHFK GPQYGVKGIR EFMGIEDRPL TATVPKPKMG WSVDEYAEIA YELWSGGIDL 

       190        200        210        220        230        240 
LKDDENFTSF PFNRFEERVR KLYAVRDRVE AETGETKEYL INITGPAHVM EKRAQLVAAE 

       250        260        270        280        290        300 
GGQYIMIDIV VVGWSALQYM REVAEDLGLA IHAHRAMHAA FTRNPRHGIS MFVLAKAARM 

       310        320        330        340        350        360 
VGVDQIHTGT AVGKMAGDYE EVKRINGFLL SEWEHIKPIF PVASGGLHPG LMPELIRLFG 

       370        380        390        400        410        420 
RDLVIQVGGG VMGHPDGPRA GAKALRDAIE AAIEGVSLEE KAKESPELKK ALEKWGYLKP 


K 

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References

[1]"Complete genome sequence of the obligate piezophilic hyperthermophilic archaeon Pyrococcus yayanosii CH1."
Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.
J. Bacteriol. 193:4297-4298(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH1 / JCM 16557.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002779 Genomic DNA. Translation: AEH23722.1.
RefSeqYP_004622994.1. NC_015680.1.

3D structure databases

ProteinModelPortalF8AF48.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEH23722; AEH23722; PYCH_00090.
GeneID10836592.
KEGGpya:PYCH_00090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAIFRESHY.

Enzyme and pathway databases

BioCycPYAY529709:GHZ0-9-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01133. RuBisCO_L_type3.
InterProIPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsTIGR03326. rubisco_III. 1 hit.
ProtoNetSearch...

Entry information

Entry nameF8AF48_PYRYC
AccessionPrimary (citable) accession number: F8AF48
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: June 11, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)