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UniProtKB/Swiss-Prot entry P00875


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RBL_SPIOL
Primary accession number P00875
Secondary accession number Q9M3L8
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 96)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain [Precursor]
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: rbcL
From
Spinacia oleracea (Spinach) [TaxID: 3562] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; Caryophyllales; Amaranthaceae; Spinacia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/9.14.3251; PubMed=6269077 [NCBI, ExPASy, EBI, Israel, Japan]
Zurawski G., Perrot B., Bottomley W., Whitfeld P.R.;
"The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA.";
Nucleic Acids Res. 9:3251-3270(1981).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Geant d'hiver, and cv. Monatol;
DOI=10.1023/A:1006478403810; PubMed=11292076 [NCBI, ExPASy, EBI, Israel, Japan]
Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R.;
"The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization.";
Plant Mol. Biol. 45:307-315(2001).
[3]
PROTEIN SEQUENCE OF 3-18, AND LACK OF METHYLATION.
PubMed=2928307 [NCBI, ExPASy, EBI, Israel, Japan]
Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.;
"Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989).
[4]
PROTEIN SEQUENCE OF 8-14 AND 466-475.
PubMed=3422748 [NCBI, ExPASy, EBI, Israel, Japan]
Mulligan R.M., Houtz R.L., Tolbert N.E.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 85:1513-1517(1988).
[5]
ACTIVE SITE.
DOI=10.1016/0006-291X(78)91351-7; PubMed=637859 [NCBI, ExPASy, EBI, Israel, Japan]
Stringer C.D., Hartman F.C.;
"Sequences of two active-site peptides from spinach ribulosebisphosphate carboxylase/oxygenase.";
Biochem. Biophys. Res. Commun. 80:1043-1048(1978).
[6]
ACTIVATION.
Lorimer G.H.;
Submitted (OCT-1982) to the PIR data bank.
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Knight S., Andersson I., Braenden C.-I.;
"Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants.";
Science 244:702-705(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1016/S0022-2836(05)80100-7; PubMed=2118958 [NCBI, ExPASy, EBI, Israel, Japan]
Knight S., Andersson I., Braenden C.-I.;
"Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4-A resolution. Subunit interactions and active site.";
J. Mol. Biol. 215:113-160(1990).
[9]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1006/jmbi.1996.0310; PubMed=8648644 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson I.;
"Large structures at high resolution: the 1.6-A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.";
J. Mol. Biol. 259:160-174(1996).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITORS 4-CABP AND XUBP.
DOI=10.1074/jbc.271.51.32894; PubMed=8955130 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.C., Fothergill M.D., Andersson I.;
"A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate.";
J. Biol. Chem. 271:32894-32899(1996).
[11]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1021/bi962818w; PubMed=9092835 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.C., Andersson I.;
"Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.";
Biochemistry 36:4041-4046(1997).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1006/jmbi.1996.0738; PubMed=9034362 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.C., Andersson I.;
"The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.";
J. Mol. Biol. 265:432-444(1997).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/j.jmb.2003.09.025; PubMed=14596800 [NCBI, ExPASy, EBI, Israel, Japan]
Karkehabadi S., Taylor T.C., Andersson I.;
"Calcium supports loop closure but not catalysis in Rubisco.";
J. Mol. Biol. 334:65-73(2003).
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.
  • CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
  • CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.
  • COFACTOR: Binds 1 magnesium ion per subunit.
  • SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.
  • SUBCELLULAR LOCATION: Plastid, chloroplast.
  • PTM: 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.
  • 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".
  • SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.
  • WEB RESOURCE: Name=Protein Spotlight; Note=The Plant Kingdom's sloth - Issue 38 of September 2003; URL="http://www.expasy.org/spotlight/back_issues/sptlt038.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V00168; CAA23473.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ400848; CAB88737.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01094; RKSPL.
A28965; A28965.
RefSeq NP_054944.1; -.
3D structure databases
PDB
1AA1; X-ray; 2.20 A; B/E/H/L=1-475.[ExPASy / RCSB / EBI]
1AUS; X-ray; 2.20 A; L/M/N/O=1-475.[ExPASy / RCSB / EBI]
1IR1; X-ray; 1.80 A; A/B/C/D=1-475.[ExPASy / RCSB / EBI]
1RBO; X-ray; 2.30 A; B/E/H/L=1-475.[ExPASy / RCSB / EBI]
1RCO; X-ray; 2.30 A; B/E/H/K/L/O/R/V=1-475.[ExPASy / RCSB / EBI]
1RCX; X-ray; 2.40 A; B/E/H/K/L/O/R/V=1-475.[ExPASy / RCSB / EBI]
1RXO; X-ray; 2.20 A; B/E/H/L=1-475.[ExPASy / RCSB / EBI]
1UPM; X-ray; 2.30 A; B/E/H/K/L/O/R/V=1-475.[ExPASy / RCSB / EBI]
1UPP; X-ray; 2.30 A; A/C/E/G=1-475.[ExPASy / RCSB / EBI]
8RUC; X-ray; 1.60 A; A/C/E/G=1-475.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AA1; -.
1AUS; -.
1IR1; -.
1RBO; -.
1RCO; -.
1RCX; -.
1RXO; -.
1UPM; -.
1UPP; -.
8RUC; -.
ModBase P00875.
Protein-protein interaction databases
DIP DIP:27641N; -.
Ontologies
GO
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01338; -; 1.
PBIL [Tree]
InterPro IPR000685; RuBisCO_lsu_C.
IPR017443; RuBisCO_lsu_fd_N.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.110; RuBisCO_large; 1.
G3DSA:3.30.70.150; RuBisCO_large; 1.
Pfam PF00016; RuBisCO_large; 1.
PF02788; RuBisCO_large_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00157; RUBISCO_LARGE; 1.
BLOCKS P00875.
Genome annotation databases
GeneID 2715621; -.
Other
LinkHub P00875; -.
ProtoNet P00875.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2      PRO_0000031415
CHAIN   3   475  473     Ribulose bisphosphate carboxylase large chain. PRO_0000031416
ACT_SITE   175   175        Proton acceptor. 
ACT_SITE   294   294        Proton acceptor. 
METAL   201   201        Magnesium; via carbamate group. 
METAL   203   203        Magnesium. 
METAL   204   204        Magnesium. 
BINDING   123   123        Substrate; in homodimeric partner. 
BINDING   173   173        Substrate. 
BINDING   177   177        Substrate. 
BINDING   295   295        Substrate. 
BINDING   327   327        Substrate. 
BINDING   379   379        Substrate. 
SITE   14    14  1     Not N6-methylated. 
SITE   334   334  1     Transition state stabilizer. 
MOD_RES   3     3        N-acetylproline. 
MOD_RES   201   201        N6-carboxylysine. 
DISULFID   247   247        Interchain; in linked form. 
CONFLICT   12    12        E -> G (in Ref. 2; CAB88737). 
TURN   22    24  3      
STRAND   36    44  9      
HELIX   50    60  11      
HELIX   70    74  5      
HELIX   77    79  3      
STRAND   83    89  7      
STRAND   97   103  7      
HELIX   105   107  3      
HELIX   113   121  9      
HELIX   124   126  3      
STRAND   130   139  10      
HELIX   142   145  4      
HELIX   155   162  8      
STRAND   169   173  5      
STRAND   175   179  5      
HELIX   182   194  13      
STRAND   198   201  4      
STRAND   207   209  3      
HELIX   214   232  19      
STRAND   237   241  5      
HELIX   247   260  14      
STRAND   263   268  6      
HELIX   269   272  4      
HELIX   274   287  14      
STRAND   290   294  5      
HELIX   298   302  5      
STRAND   305   309  5      
HELIX   311   321  11      
STRAND   324   327  4      
HELIX   339   350  12      
STRAND   352   354  3      
HELIX   358   360  3      
STRAND   375   381  7      
HELIX   384   386  3      
HELIX   387   394  8      
STRAND   399   401  3      
HELIX   404   407  4      
HELIX   413   432  20      
HELIX   437   449  13      
HELIX   453   462  10      
Sequence information
Length: 475 AA [This is the length of the unprocessed precursor] Molecular weight: 52740 Da [This is the MW of the unprocessed precursor] CRC64: 484FFFFD36BB1238 [This is a checksum on the sequence]
        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 

P00875 in FASTA format

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