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UniProtKB/Swiss-Prot entry P22859


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

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Entry information
Entry name RBL1B_CHRVI
Primary accession number P22859
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain 2
Synonyms RuBisCO large subunit 2
EC 4.1.1.39
Gene name
Name: cbbL2
Synonyms: rbcL
From
Chromatium vinosum (Allochromatium vinosum) [TaxID: 1049] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae; Allochromatium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 17899 / DSM 180 / D;
DOI=10.1016/0378-1119(91)90009-Z; PubMed=1899846 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M.;
"Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum.";
Gene 97:55-62(1991).
[2]
PROTEIN SEQUENCE OF 2-26.
PubMed=2211708 [NCBI, ExPASy, EBI, Israel, Japan]
Viale A.M., Kobayashi H., Akazawa T.;
"Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum.";
J. Biol. Chem. 265:18386-18392(1990).
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 (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).
  • 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.
  • CAUTION: In C.vinosum two similar set of genes code for RuBisCO large and small chains: the rbcL-rbcS and the rbcA-rbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.
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
D90204; BAA14229.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0586; RKKRL2.
3D structure databases
HSSP O93627; 1GEH. [HSSP ENTRY / PDB]
SMR P22859; 5-467, 6-468.
ModBase P22859.
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 P22859.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Direct protein sequencing; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   471  470     Ribulose bisphosphate carboxylase large chain 2. PRO_0000062622
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). 
DISULFID   240   240        Interchain; in linked form (By similarity). 
Sequence information
Length: 471 AA [This is the length of the unprocessed precursor] Molecular weight: 52394 Da [This is the MW of the unprocessed precursor] CRC64: FB79F09C6C33B885 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL FEEGSIVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED IRFPLHYVKT CGGPRNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYEMLRGGL DFTKDDENVN SQPFMRWQNR FEFVSEAVRK AREETGERKG HYLNVTAPTC 

       250        260        270        280        290        300 
EEMFKRAEFA KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRHPKH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED RSRGLFFDQD 

       370        380        390        400        410        420 
WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVATEAC 

       430        440        450        460        470 
VKARNEGVEI EKHAREVLSD AARHSPELAV AMETWKEIKF EFDVVDKLDA A 

P22859 in FASTA format

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