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E1TEV1 (E1TEV1_BURSG) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 26. 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:BC1003_5439 EMBL ADN61357.1
OrganismBurkholderia sp. (strain CCGE1003) [Complete proteome] [HAMAP] EMBL ADN61357.1
Taxonomic identifier640512 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length499 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 site1911Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3091Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2171Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2191Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2201Magnesium By similarity HAMAP-Rule MF_01338
Binding site1391Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1891Substrate By similarity HAMAP-Rule MF_01338
Binding site1931Substrate By similarity HAMAP-Rule MF_01338
Binding site3101Substrate By similarity HAMAP-Rule MF_01338
Binding site3421Substrate By similarity HAMAP-Rule MF_01338
Binding site3941Substrate By similarity HAMAP-Rule MF_01338
Site3491Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
E1TEV1 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 4C25DD925848040E

FASTA49955,227
        10         20         30         40         50         60 
MNDFSQPAIE SLHKPRNAGN PRERYAAGVM KYREMGYWQP DYTPKDTDVI ALFRITPQPG 

        70         80         90        100        110        120 
VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPASSASE PQYFAYIAYE 

       130        140        150        160        170        180 
LDLFEEGSVA NLTASIIGNV FGFKPLKALR LEDMRIPVAY LKTFQGPPTG IVVERERLDK 

       190        200        210        220        230        240 
YGRPLLGATV KPKLGLSGKN YGRVVYEGLR GGLDFLKDDE NINSQAFMHW RDRFLFSMEA 

       250        260        270        280        290        300 
VNRAQAETGE VKGHYLNVTA GTMEDMYERA EFARELGSCI VMIDLVVGWT AIQSMGRWAR 

       310        320        330        340        350        360 
KNDMILHLHR AGHSTYTRQR NHGISFRVIA KWLRMAGVDH AHAGTAVGKL EGDPLTVQGF 

       370        380        390        400        410        420 
YNVCREARNE VDLSRGIFFD QPWAGLRKVM PVASGGIHAG QMHQLLDLFG DDAILQFGGG 

       430        440        450        460        470        480 
TIGHPGGIQA GAVANRVALE AMVKARNEGR DIREEGPDIL EAAARWCGPL KQALDTWRDV 

       490 
TFNYASTDSP DFAATPTAA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia sp. CCGE1003."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G. expand/collapse author list , Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCGE1003.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002218 Genomic DNA. Translation: ADN61357.1.
RefSeqYP_003910648.1. NC_014540.1.

3D structure databases

ProteinModelPortalE1TEV1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN61357; ADN61357; BC1003_5439.
GeneID9764153.
KEGGbgf:BC1003_5439.
PATRIC42217762. VBIBurSp98639_5838.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycBSP640512:GBXV-5514-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 nameE1TEV1_BURSG
AccessionPrimary (citable) accession number: E1TEV1
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: June 11, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)