AC   MF_03215;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01987; -; 1; level=0
XX
Names: Ribokinase_euk
XX
ID   RBSK
DE   RecName: Full=Ribokinase;
DE            Short=RK;
DE            EC=2.7.1.15;
case <OC:Vertebrata>
GN   Name=RBKS;
else case <OC:Saccharomycotina>
GN   Name=RBK1;
end case
XX
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC       requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC       then be used either for sythesis of nucleotides, histidine, and
CC       tryptophan, or as a component of the pentose phosphate pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC         EC=2.7.1.15;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC       electrophilic catalyst to aid phosphoryl group transfer. It is the
CC       chelate of the metal and the nucleotide that is the actual substrate.;
CC   -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC       but not in, the active site. The most likely occupant of the site in
CC       vivo is potassium. Ion binding induces a conformational change that may
CC       alter substrate affinity.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC       subfamily.
XX
DR   PROSITE; PS00584; PFKB_KINASES_2; 1; trigger=no
DR   Pfam; PF00294; PfkB; 1; trigger=no
DR   PRINTS; PR00990; RIBOKINASE; 1; trigger=no
DR   NCBIfam; TIGR02152; D_ribokin_bact; 1; trigger=no
XX
KW   ATP-binding
KW   Carbohydrate metabolism
KW   Cytoplasm
KW   Kinase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Nucleus
KW   Potassium
KW   Transferase
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0005634; C:nucleus
GO   GO:0005524; F:ATP binding
GO   GO:0004747; F:ribokinase activity
GO   GO:0046835; P:carbohydrate phosphorylation
GO   GO:0019303; P:D-ribose catabolic process
XX
FT   From: RBSK_HUMAN (Q9H477)
FT   BINDING         235..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: x(2)-G-x(2)-G
FT   BINDING         268..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-D
FT   BINDING         25..27
FT                   /ligand="substrate"
FT   Condition: x(2)-D
FT   BINDING         53..57
FT                   /ligand="substrate"
FT   Condition: G-[KR]-[GAS]-x-[NR]
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT   Condition: D
FT   BINDING         263
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: [DN]
FT   BINDING         265
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         301
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         304
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         306
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: G
FT   BINDING         310
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: S
FT   BINDING         154
FT                   /ligand="substrate"
FT   Optional; Condition: E
FT   BINDING         199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   BINDING         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: T
FT   BINDING         269
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [HN]
XX
Size: 280-470;
Related: None;
Template: Q9H477; P0A9J6;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.9 2023/06/01
//