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Q44176 (RBL_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SYNPCC7002_A1798
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 caution

The sequence ACA99786.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062650

Sites

Active site1701Proton acceptor By similarity
Active site2891Proton acceptor By similarity
Metal binding1961Magnesium; via carbamate group By similarity
Metal binding1981Magnesium By similarity
Metal binding1991Magnesium By similarity
Binding site1181Substrate; in homodimeric partner By similarity
Binding site1681Substrate By similarity
Binding site1721Substrate By similarity
Binding site2901Substrate By similarity
Binding site3221Substrate By similarity
Binding site3741Substrate By similarity
Site3291Transition state stabilizer By similarity

Amino acid modifications

Modified residue1961N6-carboxylysine By similarity
Disulfide bond242Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q44176 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: 7D43456FD17D9775

FASTA47052,159
        10         20         30         40         50         60 
MQTKSAGFNA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPPEECAA AVAAESSTGT 

        70         80         90        100        110        120 
WTTVWTDGLT DLDRYKGRCY NVEPVPGEDN QYFCFVAYPL DLFEEGSVTN VLTSLVGNVF 

       130        140        150        160        170        180 
GFKALRALRL EDIRFPVALI KTYQGPPHGI TVERDLLNKY GRPLLGCTIK PKLGLSAKNY 

       190        200        210        220        230        240 
GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKSQAETNEV KGHYLNVTAG 

       250        260        270        280        290        300 
TCEEMLKRAE FAKEIGTPII MHDFLTGGFT ANTTLAKWCR DNGVLLHIHR AMHAVIDRQK 

       310        320        330        340        350        360 
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGDRAATLGF VDLMREDYVE EDRSRGVFFT 

       370        380        390        400        410        420 
QDYASLPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE 

       430        440        450        460        470 
ACVQARNEGR SLAREGNDVL REAGKWSPEL AAALDLWKEI KFEFDTVDTL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of RubisCO large subunit and small subunit from Synechococcus sp. PCC7002."
Akiyama H., Kanai S., Hirano M., Sugimoto M., Kiyohara M.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13971 Genomic DNA. Translation: BAA03076.1.
CP000951 Genomic DNA. Translation: ACA99786.1. Different initiation.
RefSeqYP_001735042.1. NC_010475.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PEMX-ray2.95R459-465[»]
ProteinModelPortalQ44176.
SMRQ44176. Positions 5-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING32049.SYNPCC7002_A1798.

PTM databases

PhosSiteP13051899.

Proteomic databases

PRIDEQ44176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA99786; ACA99786; SYNPCC7002_A1798.
GeneID6056494.
KEGGsyp:SYNPCC7002_A1798.
PATRIC23818226. VBISynSp37135_2054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycSSP32049:GKF7-1799-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_SYNP2
AccessionPrimary (citable) accession number: Q44176
Secondary accession number(s): B1XPS2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 14, 2014
This is version 85 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references