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Q31NB3 (RBL_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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
Synonyms:rbcL
Ordered Locus Names:Synpcc7942_1426
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length472 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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. HAMAP-Rule MF_01338

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 – 472472Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251463

Sites

Active site1721Proton acceptor By similarity
Active site2911Proton acceptor By similarity
Metal binding1981Magnesium; via carbamate group By similarity
Metal binding2001Magnesium By similarity
Metal binding2011Magnesium By similarity
Binding site1201Substrate; in homodimeric partner By similarity
Binding site1701Substrate By similarity
Binding site1741Substrate By similarity
Binding site2921Substrate By similarity
Binding site3241Substrate By similarity
Binding site3761Substrate By similarity
Site3311Transition state stabilizer By similarity

Amino acid modifications

Modified residue1981N6-carboxylysine By similarity
Disulfide bond244Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31NB3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CDD8519AA9D493C9

FASTA47252,448
        10         20         30         40         50         60 
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST 

        70         80         90        100        110        120 
GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN 

       130        140        150        160        170        180 
VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK 

       190        200        210        220        230        240 
NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT 

       250        260        270        280        290        300 
APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR 

       310        320        330        340        350        360 
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF 

       370        380        390        400        410        420 
FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA 

       430        440        450        460        470 
LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000100 Genomic DNA. Translation: ABB57456.1.
RefSeqYP_400443.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ31NB3.
SMRQ31NB3. Positions 6-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1426.

Proteomic databases

PRIDEQ31NB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB57456; ABB57456; Synpcc7942_1426.
GeneID3773598.
KEGGsyf:Synpcc7942_1426.
PATRIC23788203. VBISynElo51371_1628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1426-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_SYNE7
AccessionPrimary (citable) accession number: Q31NB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 53 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