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E6VIT9 (E6VIT9_RHOPX) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 19. 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 large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Rpdx1_3960 EMBL ADU45516.1
OrganismRhodopseudomonas palustris (strain DX-1) [Complete proteome] [HAMAP] EMBL ADU45516.1
Taxonomic identifier652103 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length485 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_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1761Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2941Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2021Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium By similarity HAMAP-Rule MF_01338
Binding site1241Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1741Substrate By similarity HAMAP-Rule MF_01338
Binding site1781Substrate By similarity HAMAP-Rule MF_01338
Binding site2951Substrate By similarity HAMAP-Rule MF_01338
Binding site3271Substrate By similarity HAMAP-Rule MF_01338
Binding site3791Substrate By similarity HAMAP-Rule MF_01338
Site3341Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2021N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
E6VIT9 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 29FD9930F05EBC20

FASTA48553,885
        10         20         30         40         50         60 
MNETTTIRGK DRYKSGVMEY KKMGYWEPDY EPKDTDVIAL FRVTPQDGVD PIEAAAAVAG 

        70         80         90        100        110        120 
ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSPGQYFA YIAYDLDLFE PGSISNLTAS 

       130        140        150        160        170        180 
IIGNVFGFKP LKALRLEDMR LPIAYVKTFQ GPATGIVVER ERMDKFGRPL LGATVKPKLG 

       190        200        210        220        230        240 
LSGRNYGRVV YEALKGGLDF TKDDENINSQ PFMHWRERFQ YCMEAVNKAQ AQTGEIKGTY 

       250        260        270        280        290        300 
LNVTAATMED MYERAEYAKE LGSIIVMIDL VIGYTAIQSM AKWARKNDMI LHLHRAGHST 

       310        320        330        340        350        360 
YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR EDFNPMALEN 

       370        380        390        400        410        420 
GLFFDQHWAS LNKLMPVASG GIHAGQMHQL LHLLGEDVVL QFGGGTIGHP MGIAAGATAN 

       430        440        450        460        470        480 
RVALEAMILA RNEGRDYLHE GPEILAKAAQ TCTPLKAALD TWKNVTFNYE STDTPDYAPT 


PSVSV 

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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: ADU45516.1.
RefSeqYP_004110249.1. NC_014834.1.

3D structure databases

ProteinModelPortalE6VIT9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU45516; ADU45516; Rpdx1_3960.
GeneID10066193.
KEGGrpx:Rpdx1_3960.
PATRIC45348364. VBIRhoPal82507_4025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycRPAL652103:GHQR-4008-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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 nameE6VIT9_RHOPX
AccessionPrimary (citable) accession number: E6VIT9
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)