AC   MF_00583;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00583_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00583_A; -; 1; level=0
XX
Names: RibP_PPkinase
XX
ID   KPRS
case <OC:Bacteria> and not <FTTag:Div>
DE   RecName: Full=Putative ribose-phosphate pyrophosphokinase;
DE            Short=RPPK;
DE            EC=2.7.6.1;
else
DE   RecName: Full=Ribose-phosphate pyrophosphokinase;
DE            Short=RPPK;
DE            EC=2.7.6.1;
end case
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase;
DE   AltName: Full=Phosphoribosyl diphosphate synthase;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase;
DE            Short=P-Rib-PP synthase;
DE            Short=PRPP synthase;
DE            Short=PRPPase;
GN   Name=prs;
XX
CC   -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC       phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC       pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC       5-P).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1;
case <OC:Bacteria> and not <FTTag:Metal>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
else
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 Mg(2+) ions per subunit.;
end case
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route I): step 1/1.
case <OC:Bacteria>
CC   -!- SUBUNIT: Homohexamer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <OC:Archaea>
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       Class III (archaeal) subfamily.
else
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       Class I subfamily.
end case
case <OC:Bacteria> and not <FTTag:Div>
CC   -!- CAUTION: Part of a set of proteins in which some residues (ACT_SITE,
CC       NP_BIND, REGION and BINDING) are not conserved.
end case
XX
DR   Pfam; PF00156; Pribosyltran; 1; trigger=no
DR   NCBIfam; TIGR01251; RibP_PPkin; 1; trigger=no
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1; trigger=no
XX
KW   ATP-binding
KW   Cytoplasm
KW   Kinase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Nucleotide biosynthesis
KW   Transferase
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004749; F:ribose phosphate diphosphokinase activity
GO   GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: KPRS_BACSU (P14193)
case <OC:Bacteria>
FT   BINDING         43..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [DN]-x-[EN]
FT   BINDING         102..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: R-Q
FT   BINDING         228..232
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: [DN]-[TS]-[AG]-x-[TS]
FT   ACT_SITE        198
FT   Tag: Div; Condition: K
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="#"
FT   Condition: H
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="#"
FT   Tag: Metal; Condition: D
FT   BINDING         200
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: R
FT   BINDING         224
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: D
end case
FT   From: KPRS_THEVO (Q97CA5)
case <OC:Archaea>
FT   BINDING         34..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: D-x-E
FT   BINDING         91..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: R-Q
FT   BINDING         214..218
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: S-T-G-x-T
FT   ACT_SITE        184
FT   Condition: K
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         186
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: R
FT   BINDING         210
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT   Condition: D
end case
XX
case <OC:Bacteria>
Size: 309-344;
end case
case <OC:Archaea>
Size: 271-300;
end case
Related: None;
Template: P14193; P0A717; Q97CA5; Q58761; P9WKE3;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARCFU, ENTFA, LACLA, LACPL, LISIN, LISMO, LISMF, STRP8, STRA3,
 STRA5, STRMU, STRPN, STRP1, STRP3, STRP6, STRP8, STRPQ, STRR6
Plasmid: None
Comments: None
XX
# Revision 1.42 2024/01/19
//