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A1B2Q2 (RBL_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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 large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:Pden_1699
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length487 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_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000299967

Sites

Active site1791Proton acceptor By similarity
Active site2971Proton acceptor By similarity
Metal binding2051Magnesium; via carbamate group By similarity
Metal binding2071Magnesium By similarity
Metal binding2081Magnesium By similarity
Binding site1271Substrate; in homodimeric partner By similarity
Binding site1771Substrate By similarity
Binding site1811Substrate By similarity
Binding site2981Substrate By similarity
Binding site3301Substrate By similarity
Binding site3821Substrate By similarity
Site3371Transition state stabilizer By similarity

Amino acid modifications

Modified residue2051N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1B2Q2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 07BD6810EEA63615

FASTA48753,971
        10         20         30         40         50         60 
MNEMSKSEIT DKKKRYAAGV LKYAQMGYWD GDYQPKDTDI LALFRITPQD GVDPIEAAAA 

        70         80         90        100        110        120 
VAGESSTATW TVVWTDRLTA CDQYRAKAYK VEPVPGQEGQ YFCYVAYDLI LFEEGSIANV 

       130        140        150        160        170        180 
TASIIGNVFS FKPLLAARLE DMRFPVAYMK TFAGPPTGIV VERERLDKFG RPLLGATTKP 

       190        200        210        220        230        240 
KLGLSGKNYG RVVYEGLKGG LDFMKDDENI NSQPFMHWRD RFLYCMEAVN KATAVTGEVK 

       250        260        270        280        290        300 
GHYLNITAGT MEEMYRRAEL AKELGSVIVM VDLIVGWTAI QSISNWCRQN DMILHMHRAG 

       310        320        330        340        350        360 
HGTYTRQKNH GISFRVIAKW LRMAGVDHLH CGTAVGKLEG DPLTVQGYYN TCREMVNEVD 

       370        380        390        400        410        420 
LPRGIFFEQD WGNLKKVMPV ASGGIHAGQM HQLLDLFGDD VVLQFGGGTI GHPMGIQAGA 

       430        440        450        460        470        480 
TANRVALEAM VLARNEGVDL KTEGPEVLRR AAKWCKPLEA ALDVWGNITF NYTSTDTSDF 


VPTASVS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000489 Genomic DNA. Translation: ABL69796.1.
RefSeqYP_915492.1. NC_008686.1.

3D structure databases

ProteinModelPortalA1B2Q2.
SMRA1B2Q2. Positions 12-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_1699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL69796; ABL69796; Pden_1699.
GeneID4581325.
KEGGpde:Pden_1699.
PATRIC22854475. VBIParDen97112_1626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-1717-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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 nameRBL_PARDP
AccessionPrimary (citable) accession number: A1B2Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 47 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