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K0DP73 (K0DP73_9BURK) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 9. 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 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:BUPH_00547 EMBL AFT88011.1
OrganismBurkholderia phenoliruptrix BR3459a [Complete proteome] EMBL AFT88011.1
Taxonomic identifier1229205 [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
K0DP73 [UniParc].

Last modified November 28, 2012. Version 1.
Checksum: 6991FFC279364257

FASTA49955,251
        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 DIRHEGSDIL EAAARWCGPL KQALDTWRDV 

       490 
TFNYASTDSP DFAATPTAA 

« Hide

References

[1]"Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa."
de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G., Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I., Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M., Ribeiro de Vasconcelos A.T.
J. Bacteriol. 194:6675-6676(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BR3459a EMBL AFT88011.1.
[2]Cunha C.O., Zuleta L.F.G., Almeida L.G.P., Ciapina L.P., Borges W.L., Pitard R.M., Baldani J.I., Rosangela S.R., Faria S.M., Hungria M., Cavada B.S., Mercante F.M., Vasconcelos A.T.R.
Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BR3459a EMBL AFT88011.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003864 Genomic DNA. Translation: AFT88011.1.
RefSeqYP_006792994.1. NC_018672.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFT88011; AFT88011; BUPH_00547.
GeneID13735304.
KEGGbpx:BUPH_00547.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameK0DP73_9BURK
AccessionPrimary (citable) accession number: K0DP73
Entry history
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: June 11, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)