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B8D5T5 (B8D5T5_DESK1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. 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:DKAM_1140
OrganismDesulfurococcus kamchatkensis (strain 1221n / DSM 18924) [Complete proteome] [HAMAP] EMBL ACL11466.1
Taxonomic identifier490899 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Desulfurococcus ›

Protein attributes

Sequence length448 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 site1671Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2851Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01133
Binding site1151Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01133
Binding site1691Substrate By similarity HAMAP-Rule MF_01133
Binding site2861Substrate By similarity HAMAP-Rule MF_01133
Binding site3181Substrate By similarity HAMAP-Rule MF_01133
Binding site3711Substrate By similarity HAMAP-Rule MF_01133
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
B8D5T5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 341A7EDE5549F78B

FASTA44849,948
        10         20         30         40         50         60 
MKLMSGKFEF ETYHEYIDKN YTPDPSNDVI AVYRVKPAQG FTIEDAAGGV AAESSTGTWT 

        70         80         90        100        110        120 
SLYNWYDVGR VRRLSGKAYY FKDLDDGSWI VKIAYPVELF EEGNIPGLLA SIAGNIFGMK 

       130        140        150        160        170        180 
RVEGLRLEDI YLPKKFLESF KGPSKGLNGV REIFGVKDRP IVGTVPKPKE GYSPEEVEKL 

       190        200        210        220        230        240 
ALELLSGGLD YIKDDENLTS PSFCRFEARA KAIMKVIDKV EKETGERKVW FANITSDIRE 

       250        260        270        280        290        300 
MEKRLRLVAD YGNPYIMVDV VITGWSALTY IRDLAEEYGL AIHGHRAMHA AFTRNPYHGI 

       310        320        330        340        350        360 
SMYVLAKLYR IIGIDQLHIG TAGAGKLEGG KLDVIRYAKI LREIHFKPDP DDMYHLEQPM 

       370        380        390        400        410        420 
HHIKPAMPVS SGGLHPGNLP PVIEALGTNL VLQIGGGVIG HPDGPRAGAL AVRQALEAIM 

       430        440 
NNIPLDEYAK THRELARALE KWGFAKPI

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References

[1]"Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis."
Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V., Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.
J. Bacteriol. 191:2371-2379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1221n / DSM 18924.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001140 Genomic DNA. Translation: ACL11466.1.
RefSeqYP_002428833.1. NC_011766.1.

3D structure databases

ProteinModelPortalB8D5T5.
ModBaseSearch...

Protein-protein interaction databases

STRING490899.DKAM_1140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL11466; ACL11466; DKAM_1140.
GeneID7171232.
KEGGdka:DKAM_1140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycDKAM490899:GHYH-1171-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 nameB8D5T5_DESK1
AccessionPrimary (citable) accession number: B8D5T5
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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