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UniProtKB/Swiss-Prot entry P00876


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

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Entry information
Entry name RBL_TOBAC
Primary accession number P00876
Secondary accession number Q32716
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 1, 2001 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 87)
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
Synonyms: rbcA
From
Nicotiana tabacum (Common tobacco) [TaxID: 4097] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; Nicotiana.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(82)90090-7; PubMed=7160620 [NCBI, ExPASy, EBI, Israel, Japan]
Shinozaki K., Sugiura M.;
"The nucleotide sequence of the tobacco chloroplast gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
Gene 20:91-102(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Bright Yellow 4;
PubMed=16453699 [NCBI, ExPASy, EBI, Israel, Japan]
Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N., Matsubayashi T., Zaita N., Chunwongse J., Obokata J., Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M., Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A., Tohdoh N., Shimada H., Sugiura M.;
"The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression.";
EMBO J. 5:2043-2049(1986).
[3]
PROTEIN SEQUENCE OF 5-477, AND VARIANTS VAL-394 AND MET-405.
Amiri I., Salnikow J., Vater J.;
"Amino-acid sequence of the large subunit of D-ribulose bisphosphate carboxylase/oxygenase from Nicotiana tabacum.";
Biochim. Biophys. Acta 784:116-123(1984).
[4]
PROTEIN SEQUENCE OF 3-18, AND METHYLATION AT LYS-14.
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
DOI=10.1016/0022-2836(87)90129-X; PubMed=3681999 [NCBI, ExPASy, EBI, Israel, Japan]
Suh S.W., Cascio D., Chapman M.S., Eisenberg D.;
"A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state.";
J. Mol. Biol. 197:363-365(1987).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=1512238 [NCBI, ExPASy, EBI, Israel, Japan]
Curmi P.M.G., Cascio D., Sweet R.M., Eisenberg D., Schreuder H.;
"Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0-A resolution.";
J. Biol. Chem. 267:16980-16989(1992).
[7]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-477.
DOI=10.1006/jmbi.2000.3724; PubMed=10801357 [NCBI, ExPASy, EBI, Israel, Japan]
Duff A.P., Andrews T.J., Curmi P.M.G.;
"The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate.";
J. Mol. Biol. 298:903-916(2000).
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 3RUB and 4RUB 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.
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
J01450; AAD15025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z00044; CAA77361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01095; RKNTL.
RefSeq NP_054507.1; -.
3D structure databases
PDB
1EJ7; X-ray; 2.45 A; L=3-477.[ExPASy / RCSB / EBI]
1RLC; X-ray; 2.70 A; L=1-477.[ExPASy / RCSB / EBI]
1RLD; X-ray; 2.50 A; A/B=22-467.[ExPASy / RCSB / EBI]
3RUB; X-ray; 2.00 A; L=1-477.[ExPASy / RCSB / EBI]
4RUB; X-ray; 2.70 A; A/B/C/D=1-477.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EJ7; -.
1RLC; -.
1RLD; -.
3RUB; -.
4RUB; -.
ModBase P00876.
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 P00876.
Genome annotation databases
GeneID 800513; -.
Other
LinkHub P00876; -.
ProtoNet P00876.
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; Methylation; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2      PRO_0000031427
CHAIN   3   477  475     Ribulose bisphosphate carboxylase large chain. PRO_0000031428
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   334   334  1     Transition state stabilizer. 
MOD_RES   3     3        N-acetylproline. 
MOD_RES   14    14        N6,N6,N6-trimethyllysine. 
MOD_RES   201   201        N6-carboxylysine. 
DISULFID   247   247        Interchain; in linked form. 
VARIANT   394   394  1     F -> V. 
VARIANT   405   405  1     G -> M. 
CONFLICT   284   284        C -> G (in Ref. 3; AA sequence). 
CONFLICT   377   377        V -> E (in Ref. 1; AAD15025). 
HELIX   21    24  4      
STRAND   36    44  9      
HELIX   50    60  11      
TURN   61    63  3      
HELIX   70    73  4      
HELIX   77    80  4      
STRAND   83    89  7      
STRAND   91    95  5      
STRAND   97   103  7      
HELIX   105   107  3      
HELIX   113   121  9      
HELIX   124   126  3      
STRAND   130   139  10      
HELIX   142   145  4      
STRAND   151   153  3      
HELIX   155   162  8      
STRAND   169   173  5      
STRAND   175   178  4      
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   338   350  13      
STRAND   352   354  3      
HELIX   358   360  3      
STRAND   375   381  7      
HELIX   384   386  3      
HELIX   387   394  8      
STRAND   399   403  5      
TURN   404   408  5      
HELIX   413   432  20      
HELIX   437   450  14      
HELIX   453   458  6      
HELIX   460   466  7      
Sequence information
Length: 477 AA [This is the length of the unprocessed precursor] Molecular weight: 52898 Da [This is the MW of the unprocessed precursor] CRC64: 232D54E42263198F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI 

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

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

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

       310        320        330        340        350        360 
IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR 

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

       430        440        450        460        470 
RVALEACVKA RNEGRDLAQE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK 

P00876 in FASTA format

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