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UniProtKB/Swiss-Prot entry P28378


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

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Entry information
Entry name RBL_ADOMO
Primary accession number P28378
Secondary accession numbers None
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 59)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain [Fragment]
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: rbcL
From
Adoxa moschatellina (Moschatel) [TaxID: 4208] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; campanulids; Dipsacales; Adoxaceae; Adoxa.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1523408 [NCBI, ExPASy, EBI, Israel, Japan]
Albert V.A., Williams S.E., Chase M.W.;
"Carnivorous plants: phylogeny and structural evolution.";
Science 257:1491-1495(1992).
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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity).
  • SUBCELLULAR LOCATION: Plastid, chloroplast.
  • 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.
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
L01883; AAA83213.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P00875; 1AUS. [HSSP ENTRY / PDB]
SMR P28378; 3-466.
ModBase P28378.
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:0009853; Biological process: photorespiration (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 P28378.
ProtoNet P28378.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   <1   466  >466     Ribulose bisphosphate carboxylase large chain. PRO_0000062342
ACT_SITE   166   166        Proton acceptor (By similarity). 
ACT_SITE   285   285        Proton acceptor (By similarity). 
METAL   192   192        Magnesium; via carbamate group (By similarity). 
METAL   194   194        Magnesium (By similarity). 
METAL   195   195        Magnesium (By similarity). 
BINDING   114   114        Substrate; in homodimeric partner (By similarity). 
BINDING   164   164        Substrate (By similarity). 
BINDING   168   168        Substrate (By similarity). 
BINDING   286   286        Substrate (By similarity). 
BINDING   318   318        Substrate (By similarity). 
BINDING   370   370        Substrate (By similarity). 
SITE   325   325  1     Transition state stabilizer (By similarity). 
MOD_RES   5     5        N6,N6,N6-trimethyllysine (By similarity). 
MOD_RES   192   192        N6-carboxylysine (By similarity). 
DISULFID   238   238        Interchain; in linked form (By similarity). 
NON_TER   1     1         
Sequence information
Length: 466 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 51736 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: F8D728DFCA3F43A8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
SAGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV 

        70         80         90        100        110        120 
WTDGLTNLDR YKGRCYHIEP VAGEETQFIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA 

       130        140        150        160        170        180 
LRALRLEDLR IPVAYVKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV 

       190        200        210        220        230        240 
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTCEE 

       250        260        270        280        290        300 
MMKRAIFARE LGVPIVMHDY LTGGFTANTT LAHYCRDNGL LLHIHRAMHA VIDRQKNHGI 

       310        320        330        340        350        360 
HFRVLAKALR MSGGDHIHSG TVVGKLEGER EITLGFVDLL RDDFIEKDRS RGIYFTQDWV 

       370        380        390        400        410        420 
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ 

       430        440        450        460 
ARNEGRXXAR EGNEIIREAS KWSPELAAAC EVWKEIKFEF EAMDTL 

P28378 in FASTA format

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