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B0JVL8 (RBL_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:MAE_47890
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis

Protein attributes

Sequence length471 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 – 471471Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000355751

Sites

Active site1711Proton acceptor By similarity
Active site2901Proton acceptor By similarity
Metal binding1971Magnesium; via carbamate group By similarity
Metal binding1991Magnesium By similarity
Metal binding2001Magnesium By similarity
Binding site1191Substrate; in homodimeric partner By similarity
Binding site1691Substrate By similarity
Binding site1731Substrate By similarity
Binding site2911Substrate By similarity
Binding site3231Substrate By similarity
Binding site3751Substrate By similarity
Site3301Transition state stabilizer By similarity

Amino acid modifications

Modified residue1971N6-carboxylysine By similarity
Disulfide bond243Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
B0JVL8 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 0758222DD0F46B6C

FASTA47152,544
        10         20         30         40         50         60 
MVQAKSKGFQ AGVKDYRLTY YTPDYTPKDT DLLACFRVTP QPGVPPEEAG AAVAAESSTG 

        70         80         90        100        110        120 
TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQFFCFVAYP LDLFEEGSVT NILTSIVGNV 

       130        140        150        160        170        180 
FGFKALRGLR LEDIRFPVAL IKTFQGPPHG ITVERDKLNK YGRPLLGCTI KPKLGLSAKN 

       190        200        210        220        230        240 
YGRAVYECLR GGLDFTKDDE NINSQPFMRW RDRFLFVQEA IVKSQAETNE VKGHYLNVTA 

       250        260        270        280        290        300 
PTCEQMMQRA EFAAEIKTPI IMHDYLTGGF TANTTLAKFC RDKGLLLHIH RAMHAVIDRQ 

       310        320        330        340        350        360 
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV EEDRARGIFF 

       370        380        390        400        410        420 
TQDYASLPGV MPVASGGIHV WHMPALVEIF GDDSCLQFGG GTLGHPWGNA PGATANRVAL 

       430        440        450        460        470 
EACIQARNEG RSLAREGNDV IREACRWSPE LAAACELWKE IKFEFEAMDT L 

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009552 Genomic DNA. Translation: BAG04611.1.
RefSeqYP_001659803.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JVL8.
SMRB0JVL8. Positions 8-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING449447.MAE_47890.

Proteomic databases

PaxDbB0JVL8.
PRIDEB0JVL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG04611; BAG04611; MAE_47890.
GeneID5865621.
KEGGmar:MAE_47890.
PATRIC22634095. VBIMicAer59304_4356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycMAER449447:GHO8-4825-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_MICAN
AccessionPrimary (citable) accession number: B0JVL8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 42 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