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UniProtKB/Swiss-Prot entry P27997


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

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Entry information
Entry name RBL1_RHOSH
Primary accession number P27997
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
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
Synonyms: cbbL1, rbcL
From
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides) [TaxID: 1063] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=HR;
PubMed=1907281 [NCBI, ExPASy, EBI, Israel, Japan]
Gibson J.L., Falcone D.L., Tabita F.R.;
"Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides.";
J. Biol. Chem. 266:14646-14653(1991).
[2]
KINETIC CHARACTERIZATION, AND MUTAGENESIS.
STRAIN=FI;
DOI=10.1006/abbi.1998.0979; PubMed=9882445 [NCBI, ExPASy, EBI, Israel, Japan]
Horken K.M., Tabita F.R.;
"Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities.";
Arch. Biochem. Biophys. 361:183-194(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 (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).
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=50 µM for ribulose 1,5-bisphosphate;
    KM=22 µM for CO2;
    Vmax=2.5 µmol/min/mg enzyme with CO2 as substrate;
    Note=The CO(2)/O(2) specificity factor (tau) is 56;
  • SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains (By similarity).
  • INDUCTION: Expression of this operon predominates when carbon dioxide is limiting.
  • 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
M64624; AAA26115.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D40767; RKRFAL.
3D structure databases
HSSP P09657; 1BXN. [HSSP ENTRY / PDB]
SMR P27997; 13-479.
ModBase P27997.
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.
BLOCKS P27997.
ProtoNet P27997.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   486  486     Ribulose bisphosphate carboxylase large chain. PRO_0000062647
ACT_SITE   177   177        Proton acceptor (By similarity). 
ACT_SITE   295   295        Proton acceptor (By similarity). 
METAL   203   203        Magnesium; via carbamate group (By similarity). 
METAL   205   205        Magnesium (By similarity). 
METAL   206   206        Magnesium (By similarity). 
BINDING   125   125        Substrate; in homodimeric partner (By similarity). 
BINDING   175   175        Substrate (By similarity). 
BINDING   179   179        Substrate (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   328   328        Substrate (By similarity). 
BINDING   380   380        Substrate (By similarity). 
SITE   335   335  1     Transition state stabilizer (By similarity). 
MOD_RES   203   203        N6-carboxylysine (By similarity). 
MUTAGEN   341   341        L->M: Increases KM for CO(2), decreases KM for ribulose 1,5-bisphosphate. 
Sequence information
Length: 486 AA [This is the length of the unprocessed precursor] Molecular weight: 53686 Da [This is the MW of the unprocessed precursor] CRC64: 82B91D700303C3C0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDTKTTEIKG KERYKAGVLK YAQMGYWDGD YVPKDTDVLA LFRITPQEGV DPVEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD SYRAKAYRVE PVPGTPGQYF CYVAYDLILF EEGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM RFPVAYVKTY KGPPTGIVGE RERLDKFGKP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGKNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LYVMEAVNLA SAQTGEVKGH 

       250        260        270        280        290        300 
YLNITAGTME EMYRRAEFAK SLGSVIVMVD LIIGYTAIQS ISEWCRQNDM ILHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC REPFNTVDLP 

       370        380        390        400        410        420 
RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLSLFGDDVV LQFGGGTIGH PMGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRNIDV EGPEILRAAA KWCKPLEAAL DTWGNITFNY TSTDTSDFVP 


TASVAM 

P27997 in FASTA format

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