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A1VNQ9 (RBL2_POLNA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Pnap_1978
OrganismPolaromonas naphthalenivorans (strain CJ2) [Complete proteome] [HAMAP]
Taxonomic identifier365044 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

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_1000067649

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
A1VNQ9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6FEEDE1CB0783D9D

FASTA45950,571
        10         20         30         40         50         60 
MDQSNRYADL SLKEEDLIAG GRHILVAYKM KPKAGHGYLE AAAHFAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DEFTKGVDAL VYLIDEATEE MRIAFPMDLF DRNILDGRMM IVSFLTLVIG NNQGMGDIQH 

       130        140        150        160        170        180 
AKIYDFFMPP RAIQLFDGPS KDISDMWRIL GRPVKDGGYI AGTIIKPKLG LRPEPFAQAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQT FAPMNKVMPL VHDAMKRAMD ETGEAKLFSA NITADDHYEM 

       250        260        270        280        290        300 
LARGDYILRT FGPDADKVAF LVDGYVGGPG MITTARRAFP NQYLHYHRAG HGAVTSPSAK 

       310        320        330        340        350        360 
RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGTHDDRAIA YIIERDSYTG PAYHQEWYGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGAYGHI DSPAAGATSL RQAYECWKAK 

       430        440        450 
ADPIEWAKEH PEFARAFASF PGDADMLFPG WRDKLASHR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Polaromonas naphthalenivorans CJ2."
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., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Madsen E.L., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CJ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000529 Genomic DNA. Translation: ABM37287.1.
RefSeqYP_982208.1. NC_008781.1.

3D structure databases

ProteinModelPortalA1VNQ9.
SMRA1VNQ9. Positions 2-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING365044.Pnap_1978.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM37287; ABM37287; Pnap_1978.
GeneID4688038.
KEGGpna:Pnap_1978.
PATRIC22948612. VBIPolNap76733_2845.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAAKEHREF.
OrthoDBEOG66QKT8.

Enzyme and pathway databases

BioCycPNAP365044:GJ8X-2009-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_POLNA
AccessionPrimary (citable) accession number: A1VNQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 49 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