HAMAP rule MF_03215
General rule information
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Accession | MF_03215 |
Dates | 29-FEB-2016 (Created)
1-JUN-2023 (Last updated, Version 9) |
Name | Ribokinase_euk |
Scope(s) |
Eukaryota |
Template(s) | Q9H477 (RBSK_HUMAN); P0A9J6 (RBSK_ECOLI); [ Recover all ] |
Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01987 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | RBSK |
Protein name | RecName: Full=Ribokinase; Short=RK; EC=2.7.1.15; |
case <OC:Vertebrata> | |
Gene name | Name=RBKS; |
else case <OC:Saccharomycotina> | |
Gene name | Name=RBK1; |
end case |
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 | Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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. Nucleus. |
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 |
Nucleus |
Potassium |
Transferase |
Gene Ontology
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GO:0005737; Cellular component:cytoplasm |
GO:0005634; Cellular component:nucleus |
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_HUMAN (Q9H477) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 235 | 240 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
x(2)-G-x(2)-G | ||||||||
BINDING | 268 | 269 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-D | ||||||||
BINDING | 25 | 27 | /ligand="substrate" | x(2)-D | ||||||||
BINDING | 53 | 57 | /ligand="substrate" | G-[KR]-[GAS]-x-[NR] | ||||||||
ACT_SITE | 269 | 269 | /note="Proton acceptor" | D | ||||||||
BINDING | 263 | 263 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
[DN] | ||||||||
BINDING | 265 | 265 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
|||||||||
BINDING | 301 | 301 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
|||||||||
BINDING | 304 | 304 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
|||||||||
BINDING | 306 | 306 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
G | ||||||||
BINDING | 310 | 310 | /ligand="K(+)" /ligand_id="ChEBI:CHEBI:29103" |
S | ||||||||
BINDING | 154 | 154 | /ligand="substrate" | E | ||||||||
BINDING | 199 | 199 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
N | ||||||||
BINDING | 256 | 256 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
T | ||||||||
BINDING | 269 | 269 | /ligand="substrate" | D | ||||||||
BINDING | 295 | 295 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[HN] |
Additional information
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Size range | 280-470 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |