AC   MF_01987;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
TR   HAMAP; MF_01987; -; 1; level=0
XX
Names: Ribokinase
XX
ID   RBSK
DE   RecName: Full=Ribokinase;
DE            Short=RK;
DE            EC=2.7.1.15;
GN   Name=rbsK;
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.
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   Potassium
KW   Transferase
XX
GO   GO:0005737; C:cytoplasm
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_ECOLI (P0A9J6)
FT   BINDING         223..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: x(2)-G-x(2)-G
FT   BINDING         254..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-D
FT   BINDING         14..16
FT                   /ligand="substrate"
FT   Condition: x(2)-D
FT   BINDING         42..46
FT                   /ligand="substrate"
FT   Condition: G-[KR]-[GAS]-x-[NR]
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT   Condition: D
FT   BINDING         249
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: [DN]
FT   BINDING         251
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         285
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         288
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   BINDING         290
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: G
FT   BINDING         294
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Optional; Condition: S
FT   BINDING         143
FT                   /ligand="substrate"
FT   Optional; Condition: E
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   BINDING         255
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [HN]
XX
Size: 259-382;
Related: None;
Template: P0A9J6; A0A0H2WZY4;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/06/01
//