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Q2J1J9 (RBL2_RHOP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:RPB_0951
OrganismRhodopseudomonas palustris (strain HaA2) [Complete proteome] [HAMAP]
Taxonomic identifier316058 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length461 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 – 461461Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
PRO_0000251409

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
Q2J1J9 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 78A84C7343DE90E9

FASTA46150,522
        10         20         30         40         50         60 
MDQSSRYANL NLKESDLIAG GRHVLCAYIM KPKDGFGNFL QTAAHFSAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTRGVDA LVYEIDEANN VMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE 

       130        140        150        160        170        180 
YAKMHDFYVP PAYLRLFDGP STTIRDLWRV LGRPVVDGGF IVGTIIKPKL GLRPQPFADA 

       190        200        210        220        230        240 
CYDFWLGGDF IKNDEPQGNQ VFAPFKETVR AVNEAMRRAQ DKTGEPKLFS FNITADDHYE 

       250        260        270        280        290        300 
MVARGEYILE TFADNADHVA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 

       310        320        330        340        350        360 
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAM AYMITEDSAD GPFFHQEWLG 

       370        380        390        400        410        420 
MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH IDGGAAGAKS LRQAEQCWKA 

       430        440        450        460 
GADPVEFAKD HREFARAFES FPHDADALYP NWRNSLKLAA A 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris HaA2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A. expand/collapse author list , Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HaA2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000250 Genomic DNA. Translation: ABD05661.1.
RefSeqYP_484572.1. NC_007778.1.

3D structure databases

ProteinModelPortalQ2J1J9.
SMRQ2J1J9. Positions 2-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316058.RPB_0951.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD05661; ABD05661; RPB_0951.
GeneID3909306.
KEGGrpb:RPB_0951.
PATRIC23296397. VBIRhoPal125544_0994.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAAKEHREF.
OrthoDBEOG66QKT8.

Enzyme and pathway databases

BioCycRPAL316058:GHF1-966-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_RHOP2
AccessionPrimary (citable) accession number: Q2J1J9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 54 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