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G1D766 (G1D766_RICCO) Unreviewed, UniProtKB/TrEMBL

Last modified March 6, 2013. Version 11. Feed History...

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

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:rbcL HAMAP-Rule MF_01338
ORF Names:RCOM_ORF00051 EMBL AEJ82563.1
Encoded onPlastid; Chloroplast EMBL AEJ82563.1
OrganismRicinus communis (Castor bean) [Complete proteome]
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length475 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. HAMAP-Rule MF_01338

Subcellular location

Plastid › chloroplast By similarity RuleBase RU000303 HAMAP-Rule MF_01338.

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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 By similarity HAMAP-Rule MF_01338

Sites

Active site1751Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2941Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2011Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium By similarity HAMAP-Rule MF_01338
Binding site1231Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1731Substrate By similarity HAMAP-Rule MF_01338
Binding site1771Substrate By similarity HAMAP-Rule MF_01338
Binding site2951Substrate By similarity HAMAP-Rule MF_01338
Binding site3271Substrate By similarity HAMAP-Rule MF_01338
Binding site3791Substrate By similarity HAMAP-Rule MF_01338
Site3341Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue31N-acetylproline By similarity HAMAP-Rule MF_01338
Modified residue141N6,N6,N6-trimethyllysine By similarity HAMAP-Rule MF_01338
Modified residue2011N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond247Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
G1D766 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: E3685F131A17C4E6

FASTA47552,638
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEENQFIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

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

       250        260        270        280        290        300 
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR 

       370        380        390        400        410        420 
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIREAGK WSPELAAACE VWKEIKFEFP AMDTL

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References

[1]"Castor bean organelle genome sequencing and worldwide genetic diversity analysis."
Rivarola M., Foster J.T., Chan A.P., Williams A.L., Rice D.W., Liu X., Melake-Berhan A., Huot Creasy H., Puiu D., Rosovitz M.J., Khouri H.M., Beckstrom-Sternberg S.M., Allan G.J., Keim P., Ravel J., Rabinowicz P.D.
PLoS ONE 6:E21743-E21743(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Hale.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		JF937588 Genomic DNA. Translation: AEJ82563.1.
RefSeqYP_005090186.1. NC_016736.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11542325.
KEGGrcu:RCOM_ORF00051.

Phylogenomic databases

KOK01601.

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 nameG1D766_RICCO
AccessionPrimary (citable) accession number: G1D766
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: March 6, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info