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Q13QV1 (RBL_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Bxeno_B0570
ORF Names:Bxe_B2453
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [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.

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 – 499499Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251445

Sites

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

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q13QV1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 5F82AF41666CDB74

FASTA49955,239
        10         20         30         40         50         60 
MNDFSQPVID SIHKPRDAAN PRERYAAGVM KYREMGYWQP DYAPKDTDVI ALFRITPQPG 

        70         80         90        100        110        120 
VDPEEAAAAV AGESSTATWT VVWTDRLTAC DIYRAKAYRV DPVPASNAAE PQYFAYIAYE 

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

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

       250        260        270        280        290        300 
VNRAQAETGE VKGHYLNVTA GTMEDMYERA EFAKELGSCI VMIDLVIGWT AIQSMARWAR 

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

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

       430        440        450        460        470        480 
TIGHPAGIQA GAVANRVALE AMVKARNEGR DIVHEGPDIL EAAARWCTPL KQALDTWRDV 

       490 
TFNYASTDTP DFAATPTAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000271 Genomic DNA. Translation: ABE33538.1.
RefSeqYP_552888.1. NC_007952.1.

3D structure databases

ProteinModelPortalQ13QV1.
SMRQ13QV1. Positions 34-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266265.Bxe_B2453.

Proteomic databases

PRIDEQ13QV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE33538; ABE33538; Bxe_B2453.
GeneID4007051.
KEGGbxe:Bxe_B2453.
PATRIC19335974. VBIBurXen52548_5256.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBXEN266265:GJII-5191-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_BURXL
AccessionPrimary (citable) accession number: Q13QV1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 52 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