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E6VEW0 (E6VEW0_RHOPX) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Rpdx1_4819 EMBL ADU46363.1
OrganismRhodopseudomonas palustris (strain DX-1) [Complete proteome] [HAMAP] EMBL ADU46363.1
Taxonomic identifier652103 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

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 site1671Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2881Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1921Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01339
Binding site1121Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1691Substrate By similarity HAMAP-Rule MF_01339
Binding site2891Substrate By similarity HAMAP-Rule MF_01339
Binding site3221Substrate By similarity HAMAP-Rule MF_01339
Binding site3691Substrate By similarity HAMAP-Rule MF_01339
Site3301Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1921N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
E6VEW0 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 38237BEBAF71147C

FASTA46150,501
        10         20         30         40         50         60 
MDQSNRYANL NLKESELIAG GRHVLCAYIM KPKAGFGNFI QTAAHFAAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTRGVDA LVYEIDEAKS LMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 

       130        140        150        160        170        180 
YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVINGGF IVGTIIKPKL GLRPQPFANA 

       190        200        210        220        230        240 
CYDFWLGGDF IKNDEPQGNQ VFAPFKDTVR AVSEAMRRAQ DKTGEAKLFS FNITADDHYE 

       250        260        270        280        290        300 
MLARGEFILE TFADNADHVA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 

       310        320        330        340        350        360 
QRGYTAFVLS KMSRLQGASG IHVGTMGFGK MEGEASDRAA AFMITEDAAD GPYFHQEWLG 

       370        380        390        400        410        420 
MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH VDGGAAGAKS LRQAEQCWKQ 

       430        440        450        460 
GADPVEFAKD HREFARAFES FPQDADKLYP NWRAKLKPQA A 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris DX-1."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C., Woyke T.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DX-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002418 Genomic DNA. Translation: ADU46363.1.
RefSeqYP_004111096.1. NC_014834.1.

3D structure databases

ProteinModelPortalE6VEW0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU46363; ADU46363; Rpdx1_4819.
GeneID10067063.
KEGGrpx:Rpdx1_4819.
PATRIC45350189. VBIRhoPal82507_4918.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycRPAL652103:GHQR-4878-MONOMER.

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 nameE6VEW0_RHOPX
AccessionPrimary (citable) accession number: E6VEW0
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: June 11, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)