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UniProtKB/Swiss-Prot entry O85040


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

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Entry information
Entry name RBL1_THINE
Primary accession number O85040
Secondary accession numbers None
Integrated into Swiss-Prot on November 22, 2005
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 49)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: cbbL
From
Thiobacillus neapolitanus (Halothiobacillus neapolitanus) [TaxID: 927] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Halothiobacillaceae; Halothiobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND EXPRESSION.
STRAIN=ATCC 23641;
PubMed=9696760 [NCBI, ExPASy, EBI, Israel, Japan]
Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
"Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth.";
J. Bacteriol. 180:4133-4139(1998).
[2]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K., Yeates T.O.;
"The structure of Halothiobacillus neapolitanus Rubisco.";
Submitted (APR-2005) to the PDB data bank.
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 (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 (By similarity).
  • INDUCTION: Produced when grown in air or in air supplemented with 5% CO(2).
  • 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
AF038430; AAC32549.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1SVD; X-ray; 1.80 A; A=1-473.[ExPASy / RCSB / EBI]
PDBsum 1SVD; -.
ModBase O85040.
Ontologies
GO
GO:0009573; Cellular component: chloroplast ribulose bisphosphate carboxylase complex (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004497; Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253; Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet O85040.
Other
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   473  473     Ribulose bisphosphate carboxylase large chain. PRO_0000062660
ACT_SITE   168   168        Proton acceptor (By similarity). 
ACT_SITE   287   287        Proton acceptor (By similarity). 
METAL   194   194        Magnesium; via carbamate group (By similarity). 
METAL   196   196        Magnesium (By similarity). 
METAL   197   197        Magnesium (By similarity). 
BINDING   116   116        Substrate; in homodimeric partner (By similarity). 
BINDING   166   166        Substrate (By similarity). 
BINDING   170   170        Substrate (By similarity). 
BINDING   288   288        Substrate (By similarity). 
BINDING   320   320        Substrate (By similarity). 
BINDING   372   372        Substrate (By similarity). 
SITE   327   327  1     Transition state stabilizer (By similarity). 
MOD_RES   194   194        N6-carboxylysine (By similarity). 
STRAND   28    37  10      
HELIX   43    53  11      
TURN   54    56  3      
HELIX   63    67  5      
TURN   70    72  3      
STRAND   76    83  8      
STRAND   86    96  11      
HELIX   98   100  3      
HELIX   106   114  9      
HELIX   117   119  3      
STRAND   123   132  10      
HELIX   135   138  4      
HELIX   148   155  8      
STRAND   162   166  5      
STRAND   170   172  3      
HELIX   175   187  13      
STRAND   191   194  4      
STRAND   200   202  3      
HELIX   207   225  19      
STRAND   230   234  5      
HELIX   240   253  14      
STRAND   257   261  5      
TURN   262   265  4      
HELIX   267   280  14      
STRAND   283   287  5      
HELIX   291   295  5      
STRAND   300   302  3      
HELIX   304   314  11      
STRAND   317   320  4      
HELIX   329   331  3      
HELIX   333   343  11      
STRAND   345   347  3      
HELIX   351   353  3      
STRAND   368   374  7      
HELIX   377   379  3      
HELIX   380   387  8      
STRAND   389   394  6      
HELIX   397   400  4      
HELIX   406   425  20      
TURN   430   433  4      
HELIX   434   442  9      
HELIX   446   455  10      
Sequence information
Length: 473 AA [This is the length of the unprocessed precursor] Molecular weight: 52636 Da [This is the MW of the unprocessed precursor] CRC64: B84D2EDE46CAF7D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRGLRLED VRFPLAYVKT CGGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNQGRDI EKEGKEILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDT QNR 

O85040 in FASTA format

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