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HAMAP annotation rule: MF_01338

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General rule information

Accession MF_01338
Dates 5-AUG-2005 (Created)
13-OCT-2008 (Last updated, Version 28)
Data class Protein
Predictors HAMAP; MF_01338; [distribution of match scores in UniProtKB];[seed alignment for MF_01338]


Propagated annotation

Identifier, protein and gene names
Identifier RBL

case <OG:Chloroplast> and <OC:Viridiplantae>
Protein name
RecName: Full=Ribulose bisphosphate carboxylase large chain;
Short=RuBisCO large subunit;
EC=4.1.1.39;
Flags: Precursor;
Gene name rbcL

else case <OG:Chloroplast> and not <OC:Viridiplantae>
Protein name
RecName: Full=Ribulose bisphosphate carboxylase large chain;
Short=RuBisCO large subunit;
EC=4.1.1.39;
Gene name rbcL

else case <OC:Cyanobacteria>
Protein name
RecName: Full=Ribulose bisphosphate carboxylase large chain;
Short=RuBisCO large subunit;
EC=4.1.1.39;
Gene name cbbL, rbcL

else case not <OC:Cyanobacteria> and not <OG:Chloroplast>
Protein name
RecName: Full=Ribulose bisphosphate carboxylase large chain;
Short=RuBisCO large subunit;
EC=4.1.1.39;
Gene name cbbL
end case

Comments

case <OG:Chloroplast> or <OC:Cyanobacteria>
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).

else case not <OC:Cyanobacteria> and not <OG:Chloroplast>
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).
end case

CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O.
CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2).

case <FTGroup:1>
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
end case


case <FT:18>
SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity).

else
SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains (By similarity).
end case


case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case


case <FT:18>
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).
end case

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.
Cross-references
PROSITE PS00157; RUBISCO_LARGE; 1;
Pfam PF00016; RuBisCO_large; 1;
PF02788; RuBisCO_large_N; 1;
Keywords

case <FT:15>
Acetylation.
end case

Calvin cycle, Carbon dioxide fixation, Lyase.

case <FTGroup:1>
Magnesium, Metal-binding.
end case


case <FT:16>
Methylation.
end case

Monooxygenase, Oxidoreductase.

case <OG:Chloroplast> or <OC:Cyanobacteria>
Photorespiration.
end case


case <OG:Chloroplast> or <Property:PHOTOSYN>
Photosynthesis.
end case

Gene Ontology

case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case

GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity.

case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Features

case <OC:Viridiplantae>
From: RBL_TOBAC (P00876)
Key     From     To       Description   Condition   FTGroup
PROPEP     1     2       By similarity      
CHAIN     3     Cter       Ribulose bisphosphate carboxylase large chain      
end case

Key     From     To       Description   Condition   FTGroup
SITE     334     334       Transition state stabilizer (By similarity)   K  
ACT_SITE     175     175       Proton acceptor (By similarity)   K  
ACT_SITE     294     294       Proton acceptor (By similarity)   H  
 
METAL     201     201       Magnesium; via carbamate group (By similarity)   K   1
METAL     203     203       Magnesium (By similarity)   D   1
METAL     204     204       Magnesium (By similarity)   E   1
 
BINDING     123     123       Substrate; in homodimeric partner (By similarity)   N  
BINDING     173     173       Substrate (By similarity)   T  
BINDING     177     177       Substrate (By similarity)   K  
BINDING     295     295       Substrate (By similarity)   R  
BINDING     327     327       Substrate (By similarity)   H  
BINDING     379     379       Substrate (By similarity)   S  
case <OC:Viridiplantae>
Key     From     To       Description   Condition   FTGroup
MOD_RES     3     3       N-acetylproline (By similarity)   P  
MOD_RES     14     14       N6,N6,N6-trimethyllysine (By similarity)   K  
end case

Key     From     To       Description   Condition   FTGroup
MOD_RES     201     201       N6-carboxylysine (By similarity)   K  
DISULFID (Optional)     247     247       Interchain; in linked form (By similarity)   C  


Additional information

Size range: 463-501 amino acids
Related UniRules: MF_01133 (RBL); MF_01339 (RBL2)
Template: P00876 (RBL_TOBAC); P0C2C2 (RBL1C_RALEU); P00880 (RBL_SYNP6); P00877 (RBL_CHLRE); P0C512 (RBL_ORYSJ); P00875 (RBL_SPIOL): [Recover all]
Scope: Bacteria; Cyanobacteria
Bacteria; Alphaproteobacteria
Bacteria; Betaproteobacteria
Bacteria; Acidithiobacillales
Bacteria; Chromatiales
Bacteria; Methylococcales
Bacteria; Thiotrichales
Bacteria; sulfur-oxidizing symbionts
Bacteria; Verrucomicrobia
Plastid
Fusion: Nter: None; Cter: None
Duplicate: in BRASB, BRASO, CHRVI, HYDMR, METPP, NITSX, RALEU, RHOS5, THIFE
Plasmid encoded: in BURP8, OLICA, RALEU, RHIME, RHOS5

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UniProtKB rule member sequences



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