| Accession |
MF_01338 |
| Dates |
5-AUG-2005 (Created) 7-JUN-2008 (Last updated, Version 25) |
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; |
|
end case
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; |
|
end case
case <OC:Cyanobacteria>
| Protein name |
| RecName: |
Full=Ribulose bisphosphate carboxylase large chain; Short=RuBisCO large subunit; EC=4.1.1.39; |
|
end case
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; |
|
end case
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).
end case
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.
case <FT:15>
end case
case <FTGroup:1>
end case
case <FT:16>
end case
case <OG:Chloroplast> or <OC:Cyanobacteria>
end case
case <OG:Chloroplast> or <Property:PHOTOSYN>
end case
case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity.
case <OG:Chloroplast>
end case
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 |
|
|
| Size range: |
463-499 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
Plastid |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
in BRASB, BRASO, CHRVI, HYDMR, METPP, NITSX, RALEU, THIFE |
| Plasmid encoded: |
in OLICA, RALEU, RHIME |
View rule in raw text format (no links)