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Q2RRP5 (RBL2_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:Rru_A2400
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length466 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 – 466466Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_0000251412

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
Q2RRP5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 4D9F800450AB0155

FASTA46650,482
        10         20         30         40         50         60 
MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEVDEAREL TKIAYPVALF DRNITDGKAM IASFLTLTMG NNQGMGDVEY 

       130        140        150        160        170        180 
AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC 

       190        200        210        220        230        240 
HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI 

       250        260        270        280        290        300 
IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 

       310        320        330        340        350        360 
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM 

       370        380        390        400        410        420 
KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG 

       430        440        450        460 
VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC23200.1.
RefSeqYP_427487.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RRP5.
SMRQ2RRP5. Positions 2-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A2400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC23200; ABC23200; Rru_A2400.
GeneID3835834.
KEGGrru:Rru_A2400.
PATRIC23328526. VBIRhoRub82919_2502.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAAKEHREF.
OrthoDBEOG66QKT8.

Enzyme and pathway databases

BioCycRRUB269796:GCN1-2442-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_RHORT
AccessionPrimary (citable) accession number: Q2RRP5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 57 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