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HAMAP rule MF_03215

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General rule information [?]

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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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 REGULATIONActivated 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.
PATHWAYCarbohydrate metabolism; D-ribose degradation; D-ribose 5- phosphate from beta-D-ribopyranose: step 2/2.
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm. Nucleus.
SIMILARITYBelongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.

Keywords [?]


Gene Ontology [?]

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 [?]

PROSITE PS00584; PFKB_KINASES_2; 1;
Pfam PF00294; PfkB; 1;
PRINTS PR00990; RIBOKINASE; 1;
NCBIfam TIGR02152; D_ribokin_bact; 1;

Features [?]

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 [?]

Size range 280-470 amino acids
Related rules None
Fusion Nter: None Cter: None



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