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Q0P3J3 (RBL_OSTTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:rbcL
Ordered Locus Names:OtCpg00590
Encoded onPlastid; Chloroplast
OrganismOstreococcus tauri [Complete proteome]
Taxonomic identifier70448 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Mamiellophyceae › Mamiellales › Ostreococcus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

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

Subcellular location

Plastid › chloroplast 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. HAMAP-Rule MF_01338

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 By similarity
PRO_0000251427
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251428

Sites

Active site1751Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2011Magnesium; via carbamate group By similarity
Metal binding2031Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site1231Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site1771Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue31N-acetylproline By similarity
Modified residue2011N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0P3J3 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: 90EFD83EA2992B11

FASTA47552,520
        10         20         30         40         50         60 
MAPQTETKTG TGFQAGVKDY RLTYYTPDYQ VKETDILAAF RMTPQPGVPA EECGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTQLDRY KGRCYDLEPV PGEDNQFIAY VAYPLDLFEE GSVTNLFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PVAYCKTFQG APHGIQTERD KLNKYGRGLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKSQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGNVDQM LKRAQVAKEL GMPIIMHDYL TAGFTANTTL ATYCREEGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQRNHGIH FRVLAKALRL SGGDHLHSGT VVGKLEGERN VTLGFVDLMR DAYVEKDRDR 

       370        380        390        400        410        420 
GIYFSQDWAS LPGVMPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP WGNAPGASAN 

       430        440        450        460        470 
RVALEACTQA RNEGRDLARE GGDVIRAACK WSPELAAACE VWKEIKFEFD TVDTL

« Hide

References

[1]"The complete chloroplast and mitochondrial DNA sequence of Ostreococcus tauri: organelle genomes of the smallest eukaryote are examples of compaction."
Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.
Mol. Biol. Evol. 24:956-968(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OTTH0595.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR954199 Genomic DNA. Translation: CAL36384.1.
RefSeqYP_717262.1. NC_008289.1.

3D structure databases

ProteinModelPortalQ0P3J3.
SMRQ0P3J3. Positions 12-470.
ModBaseSearch...

Protein-protein interaction databases

STRING70448.Q0P3J3.

Proteomic databases

PRIDEQ0P3J3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4238788.
KEGGota:OstapCp59.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
ProtClustDBCHL00040.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_OSTTA
AccessionPrimary (citable) accession number: Q0P3J3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 19, 2006
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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