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P00875 (RBL_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

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 bonds reported in 1RBO may be the result of oxidation during crystallization. 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_0000031415
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031416

Sites

Active site1751Proton acceptor Ref.5
Active site2941Proton acceptor Ref.5
Metal binding2011Magnesium; via carbamate group
Metal binding2031Magnesium
Metal binding2041Magnesium
Binding site1231Substrate; in homodimeric partner
Binding site1731Substrate
Binding site1771Substrate
Binding site2951Substrate
Binding site3271Substrate
Binding site3791Substrate
Site141Not N6-methylated
Site3341Transition state stabilizer

Amino acid modifications

Modified residue31N-acetylproline HAMAP-Rule MF_01338
Modified residue2011N6-carboxylysine HAMAP-Rule MF_01338
Disulfide bond247Interchain; in linked form HAMAP-Rule MF_01338

Experimental info

Sequence conflict121E → G in CAB88737. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00875 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 484FFFFD36BB1238

FASTA47552,740
        10         20         30         40         50         60 
MSPQTETKAS VEFKAGVKDY KLTYYTPEYE TLDTDILAAF RVSPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTNLDRY KGRCYHIEPV AGEENQYICY VAYPLDLFEE GSVTNMFTSI 

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

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

       250        260        270        280        290        300 
NATAGTCEDM MKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDYTEKDRSR 

       370        380        390        400        410        420 
GIYFTQSWVS TPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNTIIREATK WSPELAAACE VWKEIKFEFP AMDTV 

« Hide

References

« Hide 'large scale' references
[1]"The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA."
Zurawski G., Perrot B., Bottomley W., Whitfeld P.R.
Nucleic Acids Res. 9:3251-3270(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization."
Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R.
Plant Mol. Biol. 45:307-315(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Geant d'hiver and cv. Monatol.
[3]"Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase."
Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-18, LACK OF METHYLATION.
[4]"Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: the amino-terminal residue of the large subunit is acetylated proline."
Mulligan R.M., Houtz R.L., Tolbert N.E.
Proc. Natl. Acad. Sci. U.S.A. 85:1513-1517(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-14 AND 466-475.
[5]"Sequences of two active-site peptides from spinach ribulosebisphosphate carboxylase/oxygenase."
Stringer C.D., Hartman F.C.
Biochem. Biophys. Res. Commun. 80:1043-1048(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[6]Lorimer G.H.
Submitted (OCT-1982) to the PIR data bank
Cited for: ACTIVATION.
[7]"Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants."
Knight S., Andersson I., Braenden C.-I.
Science 244:702-705(1989)
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]"Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4-A resolution. Subunit interactions and active site."
Knight S., Andersson I., Braenden C.-I.
J. Mol. Biol. 215:113-160(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[9]"Large structures at high resolution: the 1.6-A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate."
Andersson I.
J. Mol. Biol. 259:160-174(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[10]"A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate."
Taylor T.C., Fothergill M.D., Andersson I.
J. Biol. Chem. 271:32894-32899(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITORS 4-CABP AND XUBP.
[11]"Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase."
Taylor T.C., Andersson I.
Biochemistry 36:4041-4046(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[12]"The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate."
Taylor T.C., Andersson I.
J. Mol. Biol. 265:432-444(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[13]"Calcium supports loop closure but not catalysis in Rubisco."
Karkehabadi S., Taylor T.C., Andersson I.
J. Mol. Biol. 334:65-73(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Protein Spotlight

The Plant Kingdom's sloth - Issue 38 of September 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00168 Genomic DNA. Translation: CAA23473.1.
AJ400848 Genomic DNA. Translation: CAB88737.1.
PIRRKSPL. A01094.
A28965.
RefSeqNP_054944.1. NC_002202.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA1X-ray2.20B/E/H/L1-475[»]
1AUSX-ray2.20L/M/N/O1-475[»]
1IR1X-ray1.80A/B/C/D1-475[»]
1RBOX-ray2.30B/E/H/L1-475[»]
1RCOX-ray2.30B/E/H/K/L/O/R/V1-475[»]
1RCXX-ray2.40B/E/H/K/L/O/R/V1-475[»]
1RXOX-ray2.20B/E/H/L1-475[»]
1UPMX-ray2.30B/E/H/K/L/O/R/V1-475[»]
1UPPX-ray2.30A/C/E/G1-475[»]
8RUCX-ray1.60A/C/E/G1-475[»]
ProteinModelPortalP00875.
SMRP00875. Positions 9-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-27641N.
MINTMINT-1522611.

Protein family/group databases

Allergome3814. Spi o RuBisCO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2715621.

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

EvolutionaryTraceP00875.

Entry information

Entry nameRBL_SPIOL
AccessionPrimary (citable) accession number: P00875
Secondary accession number(s): Q9M3L8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 125 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references