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I3YGD3 (I3YGD3_THIV6) 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_01339
Short name=RuBisCO HAMAP-Rule MF_01339
EC=4.1.1.39 HAMAP-Rule MF_01339
Gene names
Name:cbbM HAMAP-Rule MF_01339
Ordered Locus Names:Thivi_4238 EMBL AFL76051.1
OrganismThiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium violascens) [Complete proteome] [HAMAP] EMBL AFL76051.1
Taxonomic identifier765911 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Thiocystis ›

Protein attributes

Sequence length464 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
I3YGD3 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 29C196158DBF639E

FASTA46450,760
        10         20         30         40         50         60 
MALDQSARYS DLSLTEADLI AGGKHILVAY KMKPKGGIGY LEAAAHFAAE SSTGTNVEVS 

        70         80         90        100        110        120 
TTDDFTKGVD ALVYYIDEAN EDMRIAYPLD LFDRNMTDGR MMIVSFLTLV IGNNQGMGDI 

       130        140        150        160        170        180 
EYGQMIDFHM PDRAIQLFDG PSKDISDLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAH 

       190        200        210        220        230        240 
AAYQFWLGGD FIKNDEPQGN QTFCPSKKVI PLVYDSLKRA QDETGQAKLF SANITADDHY 

       250        260        270        280        290        300 
EMCARADFIL ETFGPDADKV AFLVDGFVGG PGMITTARRQ YPNQYLHYHR AGHGMITSPS 

       310        320        330        340        350        360 
ANRGYTAFVL AKISRLQGAS GIHVGTMGYG KMEGGADDKI IAYMIERDEC QGPVYYQKWH 

       370        380        390        400        410        420 
GMKPTTPIIS GGMNALRLPG FFANLGHGNV INTAGGGSYG HIDSPAAGAI SLRQSYECWK 

       430        440        450        460 
AGADPIEFAK EHKEFARAFA SFPLDADKLF PGWRDKLGAA AEHK

« Hide

References

[1]"Complete sequence of Thiocystis violascens DSM 198."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K. expand/collapse author list , Liu Z., Frigaard N.-U., Bryant D., Woyke T.
Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17096 / DSM 198 / 6111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003154 Genomic DNA. Translation: AFL76051.1.
RefSeqYP_006416176.1. NC_018012.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFL76051; AFL76051; Thivi_4238.
GeneID13049814.
KEGGtvi:Thivi_4238.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI3YGD3_THIV6
AccessionPrimary (citable) accession number: I3YGD3
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)
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