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D6CTT0 (D6CTT0_THIA3) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

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 II RuBisCO are composed solely of large subunits By similarity. HAMAP-Rule MF_01339

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily. HAMAP-Rule MF_01339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1681Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2891Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01339
Binding site1131Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1701Substrate By similarity HAMAP-Rule MF_01339
Binding site2901Substrate By similarity HAMAP-Rule MF_01339
Binding site3231Substrate By similarity HAMAP-Rule MF_01339
Binding site3701Substrate By similarity HAMAP-Rule MF_01339
Site3311Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
D6CTT0 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 15B9E0F51FEAA8D3

FASTA46150,819
        10         20         30         40         50         60 
MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE SSTGTNVEVS 

        70         80         90        100        110        120 
TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR FMIVSFLTLV IGNNQGMGDV 

       130        140        150        160        170        180 
EYGKMIDFYV PERAIQMFDG PATDISNLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ 

       190        200        210        220        230        240 
AAYQFWLGGD FIKNDEPQGN QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH 

       250        260        270        280        290        300 
EMCARADFAL EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS 

       310        320        330        340        350        360 
SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC QGPVYYQKWY 

       370        380        390        400        410        420 
GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG HIDSPAAGAK SLRQAYECWK 

       430        440        450        460 
AGADPIEYAK EHIEFARAFE SFPGDADKLF PGWRDKLGVH K 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FP475956 Genomic DNA. Translation: CAZ88699.1.
RefSeqYP_003624515.1. NC_014145.1.

3D structure databases

ProteinModelPortalD6CTT0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAZ88699; CAZ88699; THI_2041.
GeneID13879779.
KEGGthi:THI_2041.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD6CTT0_THIA3
AccessionPrimary (citable) accession number: D6CTT0
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: March 19, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)