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I3ZVF2 (I3ZVF2_9EURY) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 9. 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
ORF Names:CL1_1487 EMBL AFL95686.1
OrganismThermococcus sp. CL1 EMBL AFL95686.1
Taxonomic identifier163003 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length444 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 site1631Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2811Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1891Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1911Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium By similarity HAMAP-Rule MF_01133
Binding site1111Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01133
Binding site1651Substrate By similarity HAMAP-Rule MF_01133
Binding site2821Substrate By similarity HAMAP-Rule MF_01133
Binding site3141Substrate By similarity HAMAP-Rule MF_01133
Binding site3671Substrate By similarity HAMAP-Rule MF_01133
Site3221Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1891N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
I3ZVF2 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 43CE0E4FD39BCDF0

FASTA44449,679
        10         20         30         40         50         60 
MVEKFDRIYD YYVDKDYEPN RKRDIIAVFR ITPAEGYSIE AVAGGVAAES STGTWTTLYN 

        70         80         90        100        110        120 
WYEEERWADL SAKAFDFHDM GDGSWIVKIA YPFHAFEEAN LPGLLASIAG NVFGMKRAKA 

       130        140        150        160        170        180 
LRLEDLYFPE KLIREFDGPA FGIEGVRKML DIKDRPIYGV VPKPKVGYSP EEFEKLAYDL 

       190        200        210        220        230        240 
LSNGADYMKD DENLTSPWYN RFEERAEIIA RIIDRVENET GEKKTWFANI TANLPEMEER 

       250        260        270        280        290        300 
IEILADLGLK HAMVDVVITG WGALQYIRDL AADYGLAIHG HRAMHAAFTR NPYHGISMFV 

       310        320        330        340        350        360 
LAKLYRLIGI DQLHVGTAGA GKLEGGKWDV IQNARVLREE TYRPDEGDVF HLEQKFYGIK 

       370        380        390        400        410        420 
AAFPTSSGGL HPGNLPPVIE ALGTDIVLQL GGGTLGHPDG PAAGARAVRQ AIDAIMQGIP 

       430        440 
LDEYAKTHKE LARALEKWGH VTPV

« Hide

References

[1]"Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus sp. Strain CL1, Isolated from a Paralvinella sp. Polychaete Worm Collected from a Hydrothermal Vent."
Jung J.H., Holden J.F., Seo D.H., Park K.H., Shin H., Ryu S., Lee J.H., Park C.S.
J. Bacteriol. 194:4769-4770(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]Jung J.-H., Lee J.-H., Holden J.F., Seo D.-H., Shin H., Ryu S., Park C.-S.
Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003651 Genomic DNA. Translation: AFL95686.1.
RefSeqYP_006425480.1. NC_018015.1.

3D structure databases

ProteinModelPortalI3ZVF2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFL95686; AFL95686; CL1_1487.
GeneID13037891.
KEGGthm:CL1_1487.

Phylogenomic databases

KOK01601.

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 nameI3ZVF2_9EURY
AccessionPrimary (citable) accession number: I3ZVF2
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: May 1, 2013
This is version 9 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