HAMAP rule MF_01987
General rule information
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Accession | MF_01987 |
Dates | 29-FEB-2016 (Created) 1-JUN-2023 (Last updated, Version 10) |
Name | Ribokinase |
Scope | Bacteria
Archaea |
Templates | P0A9J6 (RBSK_ECOLI); A0A0H2WZY4 (RBSK_STAAC): [Recover all] |
case <OC:Bacteria> or <OC:Archaea>
Triggered by |
end case
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 phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. |
Catalytic activity | RHEA:13697: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
EC 2.7.1.15 |
Cofactor | Mg(2+) Note: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. |
Activity regulation | Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity. |
Pathway | Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. |
Subunit | Homodimer. |
Subcellular location | Cytoplasm. |
Similarity | Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily. |
Keywords
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ATP-binding
Carbohydrate metabolism
Cytoplasm
Kinase
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Transferase
Carbohydrate metabolism
Cytoplasm
Kinase
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Transferase
Gene Ontology
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GO:0005737; Cellular component: cytoplasm.
GO:0005524; Molecular function: ATP binding.
GO:0004747; Molecular function: ribokinase activity.
GO:0046835; Biological process: carbohydrate phosphorylation.
GO:0019303; Biological process: D-ribose catabolic process.
GO:0005524; Molecular function: ATP binding.
GO:0004747; Molecular function: ribokinase activity.
GO:0046835; Biological process: carbohydrate phosphorylation.
GO:0019303; Biological process: D-ribose catabolic process.
Cross-references
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PROSITE | PS00584; PFKB_KINASES_2; 1; |
Pfam | PF00294; PfkB; 1; |
PRINTS | PR00990; RIBOKINASE; 1; |
NCBIfam | TIGR02152; D_ribokin_bact; 1; |
Features
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From: RBSK_ECOLI (P0A9J6) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 223 | 228 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | x(2)-G-x(2)-G | ||||||||
BINDING | 254 | 255 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | G-D | ||||||||
BINDING | 14 | 16 | /ligand="substrate | x(2)-D | ||||||||
BINDING | 42 | 46 | /ligand="substrate | G-[KR]-[GAS]-x-[NR] | ||||||||
ACT_SITE | 255 | 255 | Proton acceptor | D | ||||||||
BINDING (Optional) | 249 | 249 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | [DN] | ||||||||
BINDING | 251 | 251 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | |||||||||
BINDING | 285 | 285 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | |||||||||
BINDING | 288 | 288 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | |||||||||
BINDING (Optional) | 290 | 290 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | G | ||||||||
BINDING (Optional) | 294 | 294 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103 | S | ||||||||
BINDING (Optional) | 143 | 143 | /ligand="substrate | E | ||||||||
BINDING | 187 | 187 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | N | ||||||||
BINDING | 255 | 255 | /ligand="substrate | D | ||||||||
BINDING (Optional) | 279 | 279 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | [HN] |
Additional information
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Size range | 259-382 amino acids |
Related rules | None |
Fusion | None |