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UniProtKB/Swiss-Prot entry P28895

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

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Entry information
Entry name RBL1A_THIFE
Primary accession number P28895
Secondary accession number Q9X5Z0
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain 1
Synonyms RuBisCO large subunit 1
EC 4.1.1.39
Gene name
Name: cbbL1
Synonyms: rbcL1
From
Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans) [TaxID: 920] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Fe1;
PubMed=1718945 [NCBI, ExPASy, EBI, Israel, Japan]
Kusano T., Takeshima T., Inoue C., Sugawara K.;
"Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans.";
J. Bacteriol. 173:7313-7323(1991).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 23270 / CIP 104768 / DSM 14882 / NCIB 8455;
DOI=10.1007/s00284-002-3825-3; PubMed=12520366 [NCBI, ExPASy, EBI, Israel, Japan]
Cannon G.C., Baker S.H., Soyer F., Johnson D.R., Bradburne C.E., Mehlman J.L., Davies P.S., Jiang Q.L., Heinhorst S., Shively J.M.;
"Organization of carboxysome genes in the thiobacilli.";
Curr. Microbiol. 46:115-119(2003).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
STRAIN=Fe1;
PubMed=8432695 [NCBI, ExPASy, EBI, Israel, Japan]
Kusano T., Sugawara K.;
"Specific binding of Thiobacillus ferrooxidans RbcR to the intergenic sequence between the rbc operon and the rbcR gene.";
J. Bacteriol. 175:1019-1025(1993).
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).
  • 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.
  • CAUTION: In T.ferroxidans two similar set of genes code for RuBisCO large and small chains: the rbcL1-rbcS1 and the rbcL2-rbcS2 sets.
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
D90113; BAA14141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF129925; AAD30508.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D11141; BAA01916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41323; RKBCLT.
3D structure databases
HSSP P04718; 1RBA. [HSSP ENTRY / PDB]
SMR P28895; 6-468.
ModBase P28895.
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 P28895.
ProtoNet P28895.
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.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   473  473     Ribulose bisphosphate carboxylase large chain 1. PRO_0000062657
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). 
VARIANT   5     5  1     T -> K (in strain: ATCC 23270). 
VARIANT   12    12  1     D -> E (in strain: ATCC 23270). 
VARIANT   89    89  1     C -> S (in strain: ATCC 23270). 
VARIANT   94    94  1     V -> I (in strain: ATCC 23270). 
VARIANT   205   206  2     IA -> MR (in strain: ATCC 23270). 
VARIANT   280   282  3     NGV -> TGT (in strain: ATCC 23270). 
VARIANT   308   308  1     A -> V (in strain: ATCC 23270). 
VARIANT   334   334  1     A -> S (in strain: ATCC 23270). 
VARIANT   351   352  2     AG -> RS (in strain: ATCC 23270). 
VARIANT   382   382  1     A -> S (in strain: ATCC 23270). 
VARIANT   392   392  1     I -> V (in strain: ATCC 23270). 
Sequence information
Length: 473 AA [This is the length of the unprocessed precursor] Molecular weight: 52501 Da [This is the MW of the unprocessed precursor] CRC64: 0185458526EA7D84 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAVKTYEAGV KDYRQTYWAP EYVPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED VRFPLAYVKT CNGPPHGIQV ERDKMNKYGR PMLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFIAWRDR FLFVADAIHT AEAETGERKG HYLNVTAPSP 

       250        260        270        280        290        300 
EEMYERAEFA KELNMPIIMH DFLTGGFCAN TGLARWCRKN GVLLHIHRAM HAVVDRNPHH 

       310        320        330        340        350        360 
GIHFRVLAKA LRLSGGDHLH TGTVVGKLEG DRAATQGWVD LLRESFVPED AGRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGVFAV ASGGIHVWHM PALLAIFGDD AIFQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNEGRDL EREGKDILTN AAKDSPELKI ALETWKEIKF EFDTVDKLDV VNR
P28895 in FASTA format

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