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Q479W5 (RBL2_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:Daro_3637
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length459 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_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_0000251406

Sites

Active site1661Proton acceptor By similarity
Active site2871Proton acceptor By similarity
Metal binding1911Magnesium; via carbamate group By similarity
Metal binding1931Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site1111Substrate; in homodimeric partner By similarity
Binding site1681Substrate By similarity
Binding site2881Substrate By similarity
Binding site3211Substrate By similarity
Binding site3681Substrate By similarity
Site3291Transition state stabilizer By similarity

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q479W5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 813D3C3753EE1C0F

FASTA45950,788
        10         20         30         40         50         60 
MDQSNRYADL SLTEAELIAG GQHILCAYKM KPKAGHRYLE AAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DEFTKGVDAL VYHIDEASED MRIAYPLDLF DRNMTDGRMM MASFLTLTIG NNQGMGDIEH 

       130        140        150        160        170        180 
AKMVDFYVPR RGIELFDGPS KDISDLWRML GRPVKDGGYI AGTIIKPKLG LRPEPFARAA 

       190        200        210        220        230        240 
YEFWLGGDFI KNDEPQGNQV FAPLKKVIPL VYDSMKRAMD ETGEAKLFSM NITADDHFEM 

       250        260        270        280        290        300 
CARADFALEA FGPDADKLAF LVDGYVGGPG MITTARRQYP NQYLHYHRAG HGAVTSPSSK 

       310        320        330        340        350        360 
RGYTAYVLAK MSRLQGASGI HVGTMGYGKM EGDKDDRACA YIIERDSYTG PVYHQEWYGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGAYGHI DSPAAGARSL RQAYDCWKAG 

       430        440        450 
ADPVEWARDH YEFARAFESF PQDADQLYPG WRHKLRPAA 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ48366.1.
RefSeqYP_286836.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ479W5.
SMRQ479W5. Positions 2-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ48366; AAZ48366; Daro_3637.
GeneID3568282.
KEGGdar:Daro_3637.
PATRIC21605954. VBIDecAro89105_3619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.
OrthoDBEOG66QKT8.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycDARO159087:GI5B-3713-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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 nameRBL2_DECAR
AccessionPrimary (citable) accession number: Q479W5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 56 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