HAMAP rule MF_01133
General rule information
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Accession | MF_01133 |
Dates | 25-SEP-2003 (Created) 1-JUN-2023 (Last updated, Version 35) |
Name | RuBisCO_L_type3 |
Scope | Archaea |
Templates | O93627 (RBL_THEKO); Q58632 (RBL_METJA); O28635 (RBL_ARCFU); Q8THG2 (RBL_METAC): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase. |
Catalytic activity | RHEA:23124: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC 4.1.1.39 |
RHEA:36631: D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+) |
case <FTGroup:1>
Cofactor | Mg(2+) Note: Binds 1 Mg(2+) ion per subunit. |
end case
Subunit | Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits. |
Miscellaneous | Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O(2) to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains. |
Similarity | Belongs to the RuBisCO large chain family. Type III subfamily. |
Keywords
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case <FTGroup:1>
end case
Gene Ontology
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case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity.
GO:0006196; Biological process: AMP catabolic process.
GO:0006196; Biological process: AMP catabolic process.
Cross-references
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Features
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From: RBL_THEKO (O93627) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 367 | 369 | /ligand="substrate | S-x-G | ||||||||
BINDING | 389 | 392 | /ligand="substrate | Q-x-G-G | ||||||||
ACT_SITE | 163 | 163 | Proton acceptor | K | ||||||||
ACT_SITE | 281 | 281 | Proton acceptor | H | ||||||||
BINDING | 189 | 189 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /note="via carbamate group | K | 1 | |||||||
BINDING | 191 | 191 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 | D | 1 | |||||||
BINDING | 192 | 192 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 | E | 1 | |||||||
BINDING | 165 | 165 | /ligand="substrate | K | ||||||||
BINDING | 282 | 282 | /ligand="substrate | R | ||||||||
BINDING | 314 | 314 | /ligand="substrate | H | ||||||||
SITE | 322 | 322 | Transition state stabilizer | K | ||||||||
MOD_RES | 189 | 189 | N6-carboxylysine | K |
Additional information
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