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F4HJW7 (F4HJW7_PYRSN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:PNA2_1620
OrganismPyrococcus sp. (strain NA2) [Complete proteome] [HAMAP]
Taxonomic identifier342949 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_01133

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form III RuBisCO are composed solely of large subunits 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

Sites

Active site1531Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2711Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1791Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1811Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1821Magnesium By similarity HAMAP-Rule MF_01133
Binding site1011Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01133
Binding site1551Substrate By similarity HAMAP-Rule MF_01133
Binding site2721Substrate By similarity HAMAP-Rule MF_01133
Binding site3041Substrate By similarity HAMAP-Rule MF_01133
Binding site3411Substrate By similarity HAMAP-Rule MF_01133
Site3111Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1791N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
F4HJW7 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: F355A0BB4552D10E

FASTA41847,086
        10         20         30         40         50         60 
MEWYLDFVDL DYTPGRDELI VEYYFEPNGV SPEEAAGRIA SESSIGTWTT LWKLPEMAKR 

        70         80         90        100        110        120 
SIAKVFYLEK HGEGYIAKIA YPLTLFEEGS LVQLFSAIAG NVFGMKALKN LRLLDFHPPY 

       130        140        150        160        170        180 
EYLRHFKGPQ FGVHGIREFM GVKDRPLTAT VPKPKMGWSV EEYAEIAYEL WSGGIDLLKD 

       190        200        210        220        230        240 
DENFTSFPFN RFEERVRKLY RVRDKVEEET GETKEYLINI TGPVHVMEKR AELVACEGGR 

       250        260        270        280        290        300 
YVMIDIVVVG WSALQYMREI TEDLGLAIHA HRAMHAAFTR NPRHGITMLA LAKAARMIGV 

       310        320        330        340        350        360 
DQIHTGTAVG KMAGDYEEIK RINDFLLSKW EHIRPVFPVA SGGLHPGLMP ELIRLFGKDL 

       370        380        390        400        410 
VIQAGGGVMG HPDGPRAGAK ALRDAIEAAV EGVDLEEKAK SSPELKKALE KWGYLKPK

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References

[1]"Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2, isolated from a deep-sea hydrothermal vent area."
Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.
J. Bacteriol. 193:3666-3667(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002670 Genomic DNA. Translation: AEC52535.1.
RefSeqYP_004424539.1. NC_015474.1.

3D structure databases

ProteinModelPortalF4HJW7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEC52535; AEC52535; PNA2_1620.
GeneID10555107.
KEGGpyn:PNA2_1620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycPSP342949:GI74-1655-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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
TIGRFAMsTIGR03326. rubisco_III. 1 hit.
ProtoNetSearch...

Entry information

Entry nameF4HJW7_PYRSN
AccessionPrimary (citable) accession number: F4HJW7
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 1, 2013
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info