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B9KQ06 (RBL_RHOSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. 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:RSKD131_2681
OrganismRhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]
Taxonomic identifier557760 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length486 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 – 486486Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_1000166262

Sites

Active site1771Proton acceptor By similarity
Active site2951Proton acceptor By similarity
Metal binding2031Magnesium; via carbamate group By similarity
Metal binding2051Magnesium By similarity
Metal binding2061Magnesium By similarity
Binding site1251Substrate; in homodimeric partner By similarity
Binding site1751Substrate By similarity
Binding site1791Substrate By similarity
Binding site2961Substrate By similarity
Binding site3281Substrate By similarity
Binding site3801Substrate By similarity
Site3351Transition state stabilizer By similarity

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9KQ06 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 82B91D700303C3C0

FASTA48653,686
        10         20         30         40         50         60 
MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV DPVEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF CYVAYDLILF EEGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM RFPVAYVKTY KGPPTGIVGE RERLDKFGKP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGKNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH 

       250        260        270        280        290        300 
YLNITAGTME EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC REPFNTVDLP 

       370        380        390        400        410        420 
RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV LQFGGGTIGH PMGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRNIDV EGPEILRAAA KWCKPLEAAL DTWGNITFNY TSTDTSDFVP 


TASVAM 

« Hide

References

[1]"Complete genome sequence of Rhodobacter sphaeroides KD131."
Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001150 Genomic DNA. Translation: ACM02541.1.
RefSeqYP_002527042.1. NC_011963.1.

3D structure databases

ProteinModelPortalB9KQ06.
SMRB9KQ06. Positions 6-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557760.RSKD131_2681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM02541; ACM02541; RSKD131_2681.
GeneID7358468.
KEGGrsk:RSKD131_2681.
PATRIC23184494. VBIRhoSph125910_4087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycRSPH557760:GH1P-2714-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_RHOSK
AccessionPrimary (citable) accession number: B9KQ06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 32 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