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Q07N61 (RBL2_RHOP5) 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

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:RPE_2686
OrganismRhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP]
Taxonomic identifier316055 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length460 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 – 460460Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_1000067650

Sites

Active site1671Proton acceptor By similarity
Active site2881Proton acceptor By similarity
Metal binding1921Magnesium; via carbamate group By similarity
Metal binding1941Magnesium By similarity
Metal binding1951Magnesium By similarity
Binding site1121Substrate; in homodimeric partner By similarity
Binding site1691Substrate By similarity
Binding site2891Substrate By similarity
Binding site3221Substrate By similarity
Binding site3691Substrate By similarity
Site3301Transition state stabilizer By similarity

Amino acid modifications

Modified residue1921N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07N61 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 4AED8610E910F883

FASTA46050,252
        10         20         30         40         50         60 
MDQSSRYANL NLKEKDLIAG GRHVLCAYIV KPKAGFGDFL QTAAHFAAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTRGVDA LVYEIDESKE LMKIAYPVEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 

       130        140        150        160        170        180 
YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFANA 

       190        200        210        220        230        240 
CFDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DATGQAKLFS FNITADDHYE 

       250        260        270        280        290        300 
MLARGEYILE TFGENADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 

       310        320        330        340        350        360 
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AFMITEDSAD GPYFHQEWLG 

       370        380        390        400        410        420 
MNPTTPIISG GMNALRMPGF FTNLGHSNLI MTAGGGAFGH LDGGAAGAKS LRQAEQCWKL 

       430        440        450        460 
GADPVQFAKE HHEFARAFES FSHDADKLFP GWRGQLGLAA 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisA53."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisA53.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000463 Genomic DNA. Translation: ABJ06623.1.
RefSeqYP_781603.1. NC_008435.1.

3D structure databases

ProteinModelPortalQ07N61.
SMRQ07N61. Positions 2-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316055.RPE_2686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ06623; ABJ06623; RPE_2686.
GeneID4360364.
KEGGrpe:RPE_2686.
PATRIC23259930. VBIRhoPal93214_2710.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRPAL316055:GHR9-2711-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_RHOP5
AccessionPrimary (citable) accession number: Q07N61
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 31, 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