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G8MDQ6 (G8MDQ6_9BURK) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 16. 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:BYI23_B014300 EMBL AET92037.1
OrganismBurkholderia sp. YI23 [Complete proteome] EMBL AET92037.1
Taxonomic identifier1097668 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length497 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 site1881Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3061Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2141Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2161Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2171Magnesium By similarity HAMAP-Rule MF_01338
Binding site1361Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1861Substrate By similarity HAMAP-Rule MF_01338
Binding site1901Substrate By similarity HAMAP-Rule MF_01338
Binding site3071Substrate By similarity HAMAP-Rule MF_01338
Binding site3391Substrate By similarity HAMAP-Rule MF_01338
Binding site3911Substrate By similarity HAMAP-Rule MF_01338
Site3461Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2141N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
G8MDQ6 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: 370A0F2ADDB00C72

FASTA49755,048
        10         20         30         40         50         60 
MNDFSKAAVE AARNPSDPRS RYAAGVMKYR EMGYWQPDYT PKDTDVIALF RITPQAGVEP 

        70         80         90        100        110        120 
EEAAAAVAGE SSTATWTVVW TDRLTACDMY RAKAYRVDPV PNQRADEPQY FAYIAYELDL 

       130        140        150        160        170        180 
FEEGSVANLT ASIIGNVFGF KPLKALRLED MRIPVAYLKT FQGPPTGIIV ERERLDKYGR 

       190        200        210        220        230        240 
PLLGATVKPK LGLSGKNYGR VVYEGLKGGL DFLKDDENIN SQAFMHWRDR YLFAMEAVSR 

       250        260        270        280        290        300 
AQAETGEVKG HYLNVTAGTM EDMYERAEFA KELGSCIVMI DLVIGWTAIQ SMSKWARRND 

       310        320        330        340        350        360 
MILHLHRAGH GTYTRQRNHG ISFRVIAKWL RMAGVDHAHA GTAVGKLEGD PLSVQGYYNV 

       370        380        390        400        410        420 
CREARNEPDL SRGIFFDQPW AGLRKVMPVA SGGIHAGQMH QLLDLFGDDC ILQFGGGTIG 

       430        440        450        460        470        480 
HPQGIQAGAT ANRVALEAMV KARNEGRDIV NEGLDVLDAA ARFCTPLKLA LDTWRDVTFN 

       490 
YASTDTPDFA VTPSVAV 

« Hide

References

[1]"Complete Genome Sequence of the Fenitrothion-Degrading Burkholderia sp. Strain YI23."
Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y., Ka J.O.
J. Bacteriol. 194:896-896(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: YI23 EMBL AET92037.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003088 Genomic DNA. Translation: AET92037.1.
RefSeqYP_005042924.1. NC_016625.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAET92037; AET92037; BYI23_B014300.
GeneID11558245.
KEGGbyi:BYI23_B014300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycBSP1097668:GKEO-5926-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 nameG8MDQ6_9BURK
AccessionPrimary (citable) accession number: G8MDQ6
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 11, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)