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I3TDF0 (I3TDF0_THEC1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 8. 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:TCELL_0363 EMBL AFK50788.1
OrganismThermogladius cellulolyticus (strain 1633) [Complete proteome] [HAMAP] EMBL AFK50788.1
Taxonomic identifier1184251 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Thermogladius ›

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
I3TDF0 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 9CCE1238EE66CCA6

FASTA44449,590
        10         20         30         40         50         60 
MTKEGFEPYP EYVDKKYQPD PDTHVIVTFR VKPASGFTVE DAAGGVAAES STGTWTTLFS 

        70         80         90        100        110        120 
WYDVSRVKKL SGRAYYFKDL KDGSYIVRVA YPVELFEEGN MPAFLASVAG NIFGMRRVEG 

       130        140        150        160        170        180 
LRVEDIYLPK QFLQYFKGPF KGVKGVREIF KVHDRPIVGT VPKPKVGYTP EEVEKLALEL 

       190        200        210        220        230        240 
LMGGMDYIKD DENLASPSFC RFEARAKSIM KIIDKVEKET GERKAWFANI TADVREMEKR 

       250        260        270        280        290        300 
LKLVADYGNP YIMVDVVVTG WSALTYIRDL AEEYKLAIHA HRAMHAAITR NPYHGISMFA 

       310        320        330        340        350        360 
LAKLYRFIGM DQLHIGTAGA GKLEGAKLDV VRIAKMLRAE DYQPDPDDDF HLPQKMYHIK 

       370        380        390        400        410        420 
PMMPVSSGGL HPGNLPIVIE ALGTDLVLQI GGGTIGHPDG PRAGATAVRQ ALDAIIKGIP 

       430        440 
LEEYAKDHKE LARALEKWGF AKPI

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References

[1]"Complete genome sequence of the hyperthermophilic cellulolytic Crenarchaeon 'Thermogladius cellulolyticus' 1633."
Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.
J. Bacteriol. 194:4446-4447(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1633 EMBL AFK50788.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003531 Genomic DNA. Translation: AFK50788.1.
RefSeqYP_006362926.1. NC_017954.1.

3D structure databases

ProteinModelPortalI3TDF0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFK50788; AFK50788; TCELL_0363.
GeneID13012650.
KEGGthg:TCELL_0363.

Organism-specific databases

CMRSearch...

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 nameI3TDF0_THEC1
AccessionPrimary (citable) accession number: I3TDF0
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: May 1, 2013
This is version 8 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