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UniProtKB/Swiss-Prot entry P22849


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

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Entry information
Entry name RBL1A_CHRVI
Primary accession number P22849
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 62)
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: rbcA
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].
PubMed=2708310 [NCBI, ExPASy, EBI, Israel, Japan]
Viale A.M., Kobayashi H., Akazawa T.;
"Expressed genes for plant-type ribulose 1,5-bisphosphate carboxylase/oxygenase in the photosynthetic bacterium Chromatium vinosum, which possesses two complete sets of the genes.";
J. Bacteriol. 171:2391-2400(1989).
[2]
PROTEIN SEQUENCE OF 2-25.
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).
[3]
PROTEIN SEQUENCE OF 2-21.
DOI=10.1016/0003-9861(87)90081-6; PubMed=3579306 [NCBI, ExPASy, EBI, Israel, Japan]
Torres-Ruiz J., McFadden B.A.;
"The nature of L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase from Chromatium vinosum.";
Arch. Biochem. Biophys. 254:63-68(1987).
[4]
PROTEIN SEQUENCE OF 2-12.
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).
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 (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
M26396; AAA23328.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32303; RKKRL1.
3D structure databases
HSSP O93627; 1GEH. [HSSP ENTRY / PDB]
SMR P22849; 5-467.
ModBase P22849.
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 P22849.
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   472  471     Ribulose bisphosphate carboxylase large chain 1. PRO_0000062621
ACT_SITE   167   167        Proton acceptor (By similarity). 
ACT_SITE   286   286        Proton acceptor (By similarity). 
METAL   193   193        Magnesium; via carbamate group (By similarity). 
METAL   195   195        Magnesium (By similarity). 
METAL   196   196        Magnesium (By similarity). 
BINDING   115   115        Substrate; in homodimeric partner (By similarity). 
BINDING   165   165        Substrate (By similarity). 
BINDING   169   169        Substrate (By similarity). 
BINDING   287   287        Substrate (By similarity). 
BINDING   319   319        Substrate (By similarity). 
BINDING   371   371        Substrate (By similarity). 
SITE   326   326  1     Transition state stabilizer (By similarity). 
MOD_RES   193   193        N6-carboxylysine (By similarity). 
Sequence information
Length: 472 AA [This is the length of the unprocessed precursor] Molecular weight: 52524 Da [This is the MW of the unprocessed precursor] CRC64: 2512B82C3A8D1895 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKTYSAGVK EYRETYWMPN YTPKDTDILA CFKITPQAGV PREEAAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYAIE DVPGDDTCFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AVRALRLEDV RFPIAYVMTC NGPPHAIQVE RDIMNKYGRP MLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRQRF DFVMDAIDKA ERETGERKGH YLNVTAPTPE 

       250        260        270        280        290        300 
EMYKRAEYAK EIGAPIIMHD YITGGFCANT GLAQWCRDNG VLLHIHRAMH AVLDRNPHHG 

       310        320        330        340        350        360 
IHFRVLTKIL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIKEDR SRGLFFDQDW 

       370        380        390        400        410        420 
GSMPGAFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTLG HPWGNAAGAC ANRVALEACV 

       430        440        450        460        470 
EARNQGVAIE KEGKDVLTKA AASSPELKIA METWKEIKFE FDTVDKLDIA HK 

P22849 in FASTA format

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View entry in raw text format (no links)
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