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I3XT42 (I3XT42_9CREN) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 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:Desfe_1247 EMBL AFL67116.1
OrganismDesulfurococcus fermentans DSM 16532 EMBL AFL67116.1
Taxonomic identifier768672 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Desulfurococcus ›

Protein attributes

Sequence length445 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 site1641Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2821Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1901Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1921Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1931Magnesium By similarity HAMAP-Rule MF_01133
Binding site1121Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01133
Binding site1661Substrate By similarity HAMAP-Rule MF_01133
Binding site2831Substrate By similarity HAMAP-Rule MF_01133
Binding site3151Substrate By similarity HAMAP-Rule MF_01133
Binding site3681Substrate By similarity HAMAP-Rule MF_01133
Site3231Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1901N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
I3XT42 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 8D9CB8CBA1CB7A78

FASTA44549,514
        10         20         30         40         50         60 
MSGKFEFETY HEYIDKNYTP DPSNDVIAVY RVKPAQGFTI EDAAGGVAAE SSTGTWTSLY 

        70         80         90        100        110        120 
NWYDVGRVRR LSGKAYYFKD LGDGSWIVKI AYPVELFEEG NIPGLLASIA GNIFGMKRVE 

       130        140        150        160        170        180 
GLRLEDIYLP KKFLESFKGP SKGLNGVREI FGIKDRPIVG TVPKPKEGYS PEEVEKLALE 

       190        200        210        220        230        240 
LLSGGLDYIK DDENLTSPSF CRFEARAKAI MKVIDKVEKE TGERKVWFAN ITSDIREMER 

       250        260        270        280        290        300 
RLRLVADYGN PYIMVDVVIA GWSALTYIRD LAEEYGLAIH GHRAMHAAFT RNPYHGISMY 

       310        320        330        340        350        360 
VLAKLYRIIG IDQLHIGTAG AGKLEGGKLD VVRYAKILRE THFKPDPDDI YHLEQPMHHI 

       370        380        390        400        410        420 
KPAMPVSSGG LHPGNLPPVI EALGTNLVLQ IGGGVIGHPD GPRAGALAVR QALEAIMNNI 

       430        440 
PLDEYAKTHR ELARALEKWG FVKPI

« Hide

References

[1]"Complete Genome Sequence of Desulfurococcus fermentans, a Hyperthermophilic Cellulolytic Crenarchaeon Isolated from a Freshwater Hot Spring in Kamchatka, Russia."
Susanti D., Johnson E.F., Rodriguez J.R., Anderson I., Perevalova A.A., Kyrpides N., Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Mavrommatis K., Peters L., Land M.L., Hauser L., Gopalan V., Chan P.P. expand/collapse author list , Lowe T.M., Atomi H., Bonch-Osmolovskaya E.A., Woyke T., Mukhopadhyay B.
J. Bacteriol. 194:5703-5704(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 16532 EMBL AFL67116.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003321 Genomic DNA. Translation: AFL67116.1.
RefSeqYP_006402691.1. NC_018001.1.

3D structure databases

ProteinModelPortalI3XT42.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFL67116; AFL67116; Desfe_1247.
GeneID13061643.
KEGGdfd:Desfe_1247.

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycDFER768672:GLCL-1285-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 nameI3XT42_9CREN
AccessionPrimary (citable) accession number: I3XT42
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: May 29, 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