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UniProtKB/Swiss-Prot entry O99000


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

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Entry information
Entry name RBL_ADEOB
Primary accession number O99000
Secondary accession numbers None
Integrated into Swiss-Prot on November 2, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 51)
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
Adenium obesum (Desert rose) [TaxID: 69375] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Gentianales; Apocynaceae; Apocynoideae; Wrightieae; Adenium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Sennblad B., Endress M.E., Bremer B.;
"Morphology and molecular data in phylogenetic fraternity: the tribe Wrightieae (Apocynaceae) revisited.";
Am. J. Bot. 85:1143-1158(1998).
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
AJ002880; CAB38851.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P00876; 3RUB. [HSSP ENTRY / PDB]
SMR O99000; 2-466.
ModBase O99000.
Ontologies
GO
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 O99000.
ProtoNet O99000.
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_0000062340
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: 51650 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 17A0BA0A21D13F50 [This is a checksum on the sequence]
        10         20         30         40         50         60 
SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV 

        70         80         90        100        110        120 
WTDGLTSLDR YKGRCYHIEP VPGEEDQYIA YVAYPLDLFE EGSVTNMLTS IVGNVFGFKA 

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

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

       250        260        270        280        290        300 
MYKRAVFARE LGAPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM 

       310        320        330        340        350        360 
HFRVLAKALR MSGGDHIHAG TVVGKLEGER DITLGFVDLL RDDFIEKDRS RGIYFTQDWV 

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

       430        440        450        460 
ARNEGRDLAV EGNEIIREAS KWSPELAAAC EVWKEIRFNF KAVDTL 

O99000 in FASTA format

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