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B2JX50 (RBL_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:Bphy_6497
Encoded onPlasmid pBPHY01
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length501 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.

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.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000355748

Sites

Active site1931Proton acceptor By similarity
Active site3111Proton acceptor By similarity
Metal binding2191Magnesium; via carbamate group By similarity
Metal binding2211Magnesium By similarity
Metal binding2221Magnesium By similarity
Binding site1411Substrate; in homodimeric partner By similarity
Binding site1911Substrate By similarity
Binding site1951Substrate By similarity
Binding site3121Substrate By similarity
Binding site3441Substrate By similarity
Binding site3961Substrate By similarity
Site3511Transition state stabilizer By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2JX50 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: E8238E2EFE685A2D

FASTA50155,176
        10         20         30         40         50         60 
MNDFSKEAVK PADSATAAAK AEKRSRYAAG VMKYREMGYW QPDYTPKDTD VIALFRITPQ 

        70         80         90        100        110        120 
PGVEPEEAAA AVAGESSTAT WTVVWTDRLT ACDMYRAKAF RVEPVPNPAE GEPQYFAFIA 

       130        140        150        160        170        180 
YELDLFEEGS VANLTASIIG NVFGFKPLKA LRLEDMRIPV AYLKTFQGPP TGIVVERERL 

       190        200        210        220        230        240 
DKYGRPLLGA TVKPKLGLSG KNYGRVVYEG LKGGLDFLKD DENINSQPFM HWRDRYLFAM 

       250        260        270        280        290        300 
EAVHRAQAET GEVKGHYLNV TAGTMEDMYE RAEFAKELGS CIVMIDLVIG WTAITSMGRW 

       310        320        330        340        350        360 
ARKNDMILHL HRAGHGTYTR QRNHGISFRV IAKWLRMAGV DHAHAGTAVG KLDGDPLSVQ 

       370        380        390        400        410        420 
GYYNVLRESH NSVDLTRGIF FDQHWAGLRK VMPVASGGIH AGQMHQLLDL FGDDAILQFG 

       430        440        450        460        470        480 
GGTIGHPSGI QAGATANRVA LETMVKARNE GRDIANEGSD LLEAAARHCT PLKQALDTWG 

       490        500 
DVTFNYTPTD SPDFAVTPSV A 

« Hide

References

[1]"Complete sequence of plasmid 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001045 Genomic DNA. Translation: ACC75527.1.
RefSeqYP_001862573.1. NC_010625.1.

3D structure databases

ProteinModelPortalB2JX50.
SMRB2JX50. Positions 22-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391038.Bphy_6497.

Proteomic databases

PRIDEB2JX50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC75527; ACC75527; Bphy_6497.
GeneID6248036.
KEGGbph:Bphy_6497.
PATRIC19199896. VBIBurPhy25146_6827.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycBPHY391038:GI4Z-6575-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 nameRBL_BURP8
AccessionPrimary (citable) accession number: B2JX50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families