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P00877 (RBL_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

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.

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.

Subcellular location

Plastidchloroplast HAMAP-Rule MF_01338.

Post-translational modification

The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization. HAMAP-Rule MF_01338

The electron density found in the position of Thr-471 (Ref.6 only) suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing. 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".

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 HAMAP-Rule MF_01338
PRO_0000031175
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031176

Sites

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

Amino acid modifications

Modified residue31N-acetylproline Ref.3
Modified residue10414-hydroxyproline HAMAP-Rule MF_01338
Modified residue15114-hydroxyproline HAMAP-Rule MF_01338
Modified residue2011N6-carboxylysine HAMAP-Rule MF_01338
Modified residue2561S-methylcysteine HAMAP-Rule MF_01338
Modified residue3691S-methylcysteine HAMAP-Rule MF_01338
Disulfide bond247Interchain; in linked form HAMAP-Rule MF_01338

Natural variations

Natural variant461L → P in strain: 137c and CC-503.

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00877 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5A9BFD394CF7D4D4

FASTA47552,543
        10         20         30         40         50         60 
MVPQTETKAG AGFKAGVKDY RLTYYTPDYV VRDTDILAAF RMTPQLGVPP EECGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEDNQYIAY VAYPIDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYVKTFVG PPHGIQVERD KLNKYGRGLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKAQA ETGEVKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM MKRAVCAKEL GVPIIMHDYL TGGFTANTSL AIYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQRNHGIH FRVLAKALRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR DDYVEKDRSR 

       370        380        390        400        410        420 
GIYFTQDWCS MPGVMPVASG GIHVWHMPAL VEIFGDDACL QFGGGTLGHP WGNAPGAAAN 

       430        440        450        460        470 
RVALEACTQA RNEGRDLARE GGDVIRSACK WSPELAAACE VWKEIKFEFD TIDKL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes."
Dron M., Rahire M., Rochaix J.-D.
J. Mol. Biol. 162:775-793(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: addressing the mutational-hazard hypothesis."
Smith D.R., Lee R.W.
BMC Evol. Biol. 9:120-120(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC-503.
[3]"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 3-14, ACETYLATION AT PRO-3.
[4]"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats."
Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B.
Plant Cell 14:2659-2679(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
[5]"First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii."
Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.
J. Biol. Chem. 276:48159-48164(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP.
Strain: 2137.
[6]"Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate."
Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J., Kato K., Shibata N., Inoue T., Yokota A., Kai Y.
J. Mol. Biol. 316:679-691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP.
Strain: 137c / CC-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01399 Genomic DNA. Translation: AAA84449.1.
FJ423446 Genomic DNA. Translation: ACJ50136.1.
BK000554 Genomic DNA. Translation: DAA00950.1.
PIRRKKML. A01097.
RefSeqNP_958405.1. NC_005353.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK8X-ray1.40A/C/E/G1-475[»]
1IR2X-ray1.84A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z1-475[»]
1UW9X-ray2.05A/B/E/H/K/O/R/V1-475[»]
1UWAX-ray2.30A/B/E/H/K/O/R/V1-475[»]
1UZDX-ray2.40A/B/E/H/K/O/R/V1-475[»]
1UZHX-ray2.20A/B/E/H/K/O/R/V1-475[»]
2V63X-ray1.80A/B/C/D/E/F/G/H1-475[»]
2V67X-ray2.00A/B/C/D/E/F/G/H1-475[»]
2V68X-ray2.30A/B/C/D/E/F/G/H1-475[»]
2V69X-ray2.80A/B/C/D/E/F/G/H1-475[»]
2V6AX-ray1.50A/B/C/D/E/F/G/H1-475[»]
2VDHX-ray2.30A/B/C/D/E/F/G/H1-475[»]
2VDIX-ray2.65A/B/C/D/E/F/G/H1-475[»]
ProteinModelPortalP00877.
SMRP00877. Positions 7-475.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP00877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsDAA00950; DAA00950; DAA00950.
GeneID2717040.
KEGGcre:ChreCp049.

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycCHLAMY:CHRECP049-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...

Other

EvolutionaryTraceP00877.

Entry information

Entry nameRBL_CHLRE
AccessionPrimary (citable) accession number: P00877
Secondary accession number(s): B7U1I9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 117 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references