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UniProtKB/Swiss-Prot entry O03042

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

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Entry information
Entry name RBL_ARATH
Primary accession number O03042
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 78)
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
OrderedLocusNames: AtCg00490
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Zhu G., Jensen R.G., Bohnert H.J.;
"DNA sequence of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit from Arabidopsis thaliana.";
(er) Plant Gene Register PGR97-074.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/6.5.283; PubMed=10574454 [NCBI, ExPASy, EBI, Israel, Japan]
Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
"Complete structure of the chloroplast genome of Arabidopsis thaliana.";
DNA Res. 6:283-290(1999).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
STRAIN=cv. Columbia;
DOI=10.1104/pp.114.2.623; PubMed=9193094 [NCBI, ExPASy, EBI, Israel, Japan]
Isono K., Niwa Y., Satoh K., Kobayashi H.;
"Evidence for transcriptional regulation of plastid photosynthesis genes in Arabidopsis thaliana roots.";
Plant Physiol. 114:623-630(1997).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-446.
Tsukaya H., Ikeda H., Yokoyama J., Matsuura K., Kuroiwa H., Kuroiwa T., Iwatsuki K.;
"Morphological, physiological and molecular genetic characterization of Arabidopsis himalaica, with reference to the analogous features of A. thaliana.";
J. Plant Res. 110:15-23(1997).
[5]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M300030-MCP200; PubMed=12766230 [NCBI, ExPASy, EBI, Israel, Japan]
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana.";
Mol. Cell. Proteomics 2:325-345(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 (By similarity).
  • 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 (By similarity).
  • SUBUNIT: 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: Plastid, chloroplast.
  • PTM: 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).
  • 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).
  • 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
U91966; AAB68400.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000423; BAA84393.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB003522; BAA20946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D88901; BAA19595.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_051067.1; -.
3D structure databases
HSSP P00880; 1RBL. [HSSP ENTRY / PDB]
SMR O03042; 11-475.
ModBase O03042.
2D gel databases
SWISS-2DPAGE O03042; -.
Organism-specific databases
TAIR AtCg00490; -.
Gene expression databases
GermOnline ATCG00490; Arabidopsis thaliana.
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 O03042.
Proteomic databases
ProMEX O03042; -.
Genome annotation databases
GeneID 844754; -.
GenomeReviews AP000423_GR; ATCG00490.
KEGG ath:ArthCp030; -.
NMPDR fig|3702.1.peg.29; -.
Other
ProtoNet O03042.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Complete proteome; 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     By similarity. PRO_0000031119
CHAIN   3   479  477     Ribulose bisphosphate carboxylase large chain. PRO_0000031120
ACT_SITE   175   175        Proton acceptor (By similarity). 
ACT_SITE   294   294        Proton acceptor (By similarity). 
METAL   201   201        Magnesium; via carbamate group (By similarity). 
METAL   203   203        Magnesium (By similarity). 
METAL   204   204        Magnesium (By similarity). 
BINDING   123   123        Substrate; in homodimeric partner (By similarity). 
BINDING   173   173        Substrate (By similarity). 
BINDING   177   177        Substrate (By similarity). 
BINDING   295   295        Substrate (By similarity). 
BINDING   327   327        Substrate (By similarity). 
BINDING   379   379        Substrate (By similarity). 
SITE   334   334  1     Transition state stabilizer (By similarity). 
MOD_RES   3     3        N-acetylproline (By similarity). 
MOD_RES   14    14        N6,N6,N6-trimethyllysine (By similarity). 
MOD_RES   201   201        N6-carboxylysine (By similarity). 
DISULFID   247   247        Interchain; in linked form (By similarity). 
Sequence information
Length: 479 AA [This is the length of the unprocessed precursor] Molecular weight: 52955 Da [This is the MW of the unprocessed precursor] CRC64: 3086705F3C8FEF75 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL AALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

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

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

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGDRE STLGFVDLLR DDYVEKDRSR 

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

       430        440        450        460        470 
RVALEACVQA RNEGRDLAVE GNEIIREACK WSPELAAACE VWKEITFNFP TIDKLDGQE
O03042 in FASTA format

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