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P04717 (RBL_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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:rbcL
Encoded onPlastid; Chloroplast
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

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

Subcellular location

Plastidchloroplast 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.

Sequence similarities

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

Sequence caution

The sequence CAA27483.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 HAMAP-Rule MF_01338
PRO_0000031333
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031334

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 Ref.2
Modified residue141N6,N6,N6-trimethyllysine Ref.2
Modified residue2011N6-carboxylysine By similarity
Disulfide bond247Interchain; in linked form By similarity

Secondary structure

......................................................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04717 [UniParc].

Last modified December 1, 1992. Version 3.
Checksum: 1F673855DD921DF9

FASTA47552,763
        10         20         30         40         50         60 
MSPQTETKAK VGFKAGVKDY KLTYYTPDYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYEIEPV PGEDNQFIAY VAYPLDLFEE GSVTNMFTSI 

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

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

       250        260        270        280        290        300 
NATAGTCEEM LKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDYIKKDRSR 

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

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNAIIREACK WSPELAAACE VWKEIKFEFP AMDTL 

« Hide

References

[1]"Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from pea chloroplasts."
Zurawski G., Whitfeld P.R., Bottomley W.
Nucleic Acids Res. 14:3975-3976(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species."
Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.
Plant Physiol. 98:1170-1174(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, ACETYLATION AT PRO-3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03853 Genomic DNA. Translation: CAA27483.1. Different initiation.
PIRRKPMLC. A24471.
RefSeqYP_003587524.1. NC_014057.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HHHX-ray2.20A/B/C/D1-475[»]
4MKVX-ray2.15A/B/C/D12-469[»]
ProteinModelPortalP04717.
SMRP04717. Positions 9-475.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP04717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9073048.

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_PEA
AccessionPrimary (citable) accession number: P04717
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 97 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references