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E8YSE3 (E8YSE3_9BURK) 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
ORF Names:BC1001_3963 EMBL ADX57374.1
OrganismBurkholderia sp. CCGE1001 [Complete proteome] EMBL ADX57374.1
Taxonomic identifier640510 [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
E8YSE3 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 6991FC31B6094257

FASTA49955,261
        10         20         30         40         50         60 
MNDFSQPAIE SLHKPRNAGD PRERYAAGVM KYREMGYWQP DYTPKDTDVI ALFRITPQPG 

        70         80         90        100        110        120 
VEPEEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPASNAGE 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 EFAKELGSCI VMIDLVIGWT AIQSMGRWAR 

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

       370        380        390        400        410        420 
YNVCREARNE VDLSRGLFFD QPWAGLRKVM PVASGGIHAG QMHQLLELFG DDAILQFGGG 

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

       490 
TFNYASTDSP DFAATPTAA 

« Hide

References

[1]"Complete sequence of chromosome2 of Burkholderia sp. CCGE1001."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Martinez-Romero E. expand/collapse author list , Rogel M.A., Auchtung J., Tiedje J., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CCGE1001 EMBL ADX57374.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002520 Genomic DNA. Translation: ADX57374.1.
RefSeqYP_004230434.1. NC_015137.1.

3D structure databases

ProteinModelPortalE8YSE3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX57374; ADX57374; BC1001_3963.
GeneID10225554.
KEGGbug:BC1001_3963.
PATRIC46900954. VBIBurSp1058_4154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycBSP640510:GI28-4031-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 nameE8YSE3_9BURK
AccessionPrimary (citable) accession number: E8YSE3
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 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)