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UniProtKB/Swiss-Prot entry P0C2C2


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

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Entry information
Entry name RBL1C_RALEU
Primary accession number P0C2C2
Secondary accession numbers P09657 P77811
Integrated into Swiss-Prot on January 23, 2007
Sequence was last modified on January 23, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 16)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain, chromosomal
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: cbbL1
Synonyms: cbbL, cbxLC, cfxLC
From
Ralstonia eutropha (Alcaligenes eutrophus) [TaxID: 106590] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
PubMed=2820933 [NCBI, ExPASy, EBI, Israel, Japan]
Andersen K., Caton J.;
"Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products.";
J. Bacteriol. 169:4547-4558(1987).
[2]
SEQUENCE REVISION.
Andersen K.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
STRAIN=ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R;
DOI=10.1006/jmbi.1999.2701; PubMed=10329167 [NCBI, ExPASy, EBI, Israel, Japan]
Hansen S., Vollan V.B., Hough E., Andersen K.;
"The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits.";
J. Mol. Biol. 288:609-621(1999).
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. 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.
  • PTM: The disulfide bond which can form between Cys-278 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".
  • 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
M17744; AAC28129.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26954; RKALLE.
3D structure databases
PDB
1BXN; X-ray; 2.70 A; A/C/E/G=1-486.[ExPASy / RCSB / EBI]
PDBsum 1BXN; -.
ModBase P0C2C2.
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 P0C2C2.
Other
ProtoNet P0C2C2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   486  486     Ribulose bisphosphate carboxylase large chain, chromosomal. PRO_0000062641
ACT_SITE   178   178        Proton acceptor. 
ACT_SITE   296   296        Proton acceptor. 
METAL   204   204        Magnesium; via carbamate group. 
METAL   206   206        Magnesium. 
METAL   207   207        Magnesium. 
BINDING   126   126        Substrate; in homodimeric partner. 
BINDING   176   176        Substrate. 
BINDING   180   180        Substrate. 
BINDING   297   297        Substrate. 
BINDING   329   329        Substrate. 
BINDING   381   381        Substrate. 
SITE   336   336  1     Transition state stabilizer. 
MOD_RES   204   204        N6-carboxylysine. 
TURN   25    27  3      
STRAND   38    47  10      
HELIX   53    62  10      
TURN   63    66  4      
HELIX   75    78  4      
HELIX   81    83  3      
STRAND   86    92  7      
STRAND   100   107  8      
HELIX   108   110  3      
HELIX   116   124  9      
HELIX   127   129  3      
STRAND   133   135  3      
STRAND   137   142  6      
HELIX   145   148  4      
HELIX   158   165  8      
STRAND   172   176  5      
HELIX   185   197  13      
STRAND   201   204  4      
HELIX   217   235  19      
STRAND   240   244  5      
HELIX   250   262  13      
STRAND   266   271  6      
HELIX   272   274  3      
HELIX   276   287  12      
TURN   288   290  3      
STRAND   292   296  5      
TURN   298   300  3      
HELIX   301   304  4      
STRAND   309   311  3      
HELIX   313   323  11      
STRAND   326   329  4      
STRAND   335   338  4      
HELIX   341   352  12      
STRAND   354   356  3      
HELIX   360   362  3      
STRAND   377   383  7      
HELIX   386   388  3      
HELIX   389   396  8      
STRAND   401   404  4      
HELIX   406   409  4      
HELIX   414   435  22      
HELIX   439   453  15      
HELIX   455   463  9      
Sequence information
Length: 486 AA [This is the length of the unprocessed precursor] Molecular weight: 53840 Da [This is the MW of the unprocessed precursor] CRC64: 66EAB4A11982FAB5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG VDPVEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG 

       250        260        270        280        290        300 
SYLNVTAGTM EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTQTDL 

       370        380        390        400        410        420 
TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCAPLRAA LDTWGDITFN YTPTDTSDFV 


PTASVA 

P0C2C2 in FASTA format

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