HAMAP rule MF_00583
General rule information
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Accession | MF_00583 |
Dates | 19-OCT-2002 (Created)
19-JAN-2024 (Last updated, Version 42) |
Name | RibP_PPkinase |
Scope(s) |
Bacteria Archaea |
Template(s) | P14193 (KPRS_BACSU); P0A717 (KPRS_ECOLI); Q97CA5 (KPRS_THEVO); Q58761 (KPRS_METJA); P9WKE3 (KPRS_MYCTU); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00583_B (Get profile general information and statistics) end case
case c? <OC:Archaea>
HAMAP; MF_00583_A (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | KPRS |
case <OC:Bacteria> and not <FTTag:Div> | |
Protein name | RecName: Full=Putative ribose-phosphate pyrophosphokinase; Short=RPPK; EC=2.7.6.1; |
else | |
Protein name | RecName: Full=Ribose-phosphate pyrophosphokinase; Short=RPPK; EC=2.7.6.1; |
end case | |
Protein name | AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase; AltName: Full=Phosphoribosyl diphosphate synthase; AltName: Full=Phosphoribosyl pyrophosphate synthase; Short=P-Rib-PP synthase; Short=PRPP synthase; Short=PRPPase; |
Gene name | Name=prs; |
Comments
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FUNCTION | Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P). |
CATALYTIC ACTIVITY | Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1- diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; |
case <OC:Bacteria> and not <FTTag:Metal> | |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
else | |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 Mg(2+) ions per subunit.; |
end case | |
PATHWAY | Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. |
case <OC:Bacteria> | |
SUBUNIT | Homohexamer. |
end case | |
SUBCELLULAR LOCATION | Cytoplasm. |
case <OC:Archaea> | |
SIMILARITY | Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily. |
else | |
SIMILARITY | Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily. |
end case | |
case <OC:Bacteria> and not <FTTag:Div> | |
CAUTION | Part of a set of proteins in which some residues (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved. |
end case |
Keywords
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ATP-binding |
Cytoplasm |
Kinase |
Magnesium |
Metal-binding |
Nucleotide-binding |
Nucleotide biosynthesis |
Transferase |
Gene Ontology
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GO:0000287; Molecular function:magnesium ion binding |
GO:0004749; Molecular function:ribose phosphate diphosphokinase activity |
GO:0006015; Biological process:5-phosphoribose 1-diphosphate biosynthetic process |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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From: KPRS_BACSU (P14193) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <OC:Bacteria> | ||||||||||||
BINDING | 43 | 45 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[DN]-x-[EN] | ||||||||
BINDING | 102 | 103 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R-Q | ||||||||
BINDING | 228 | 232 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
[DN]-[TS]-[AG]-x-[TS] | ||||||||
ACT_SITE | 198 | 198 | Div | K | ||||||||
BINDING | 136 | 136 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="#" |
H | ||||||||
BINDING | 175 | 175 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="#" |
Metal | D | |||||||
BINDING | 200 | 200 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
R | ||||||||
BINDING | 224 | 224 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
D | ||||||||
end case | ||||||||||||
From: KPRS_THEVO (Q97CA5) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <OC:Archaea> | ||||||||||||
BINDING | 34 | 36 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
D-x-E | ||||||||
BINDING | 91 | 92 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R-Q | ||||||||
BINDING | 214 | 218 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
S-T-G-x-T | ||||||||
ACT_SITE | 184 | 184 | K | |||||||||
BINDING | 124 | 124 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
H | ||||||||
BINDING | 161 | 161 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
BINDING | 186 | 186 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
R | ||||||||
BINDING | 210 | 210 | /ligand="D-ribose 5-phosphate" /ligand_id="ChEBI:CHEBI:78346" |
D | ||||||||
end case |
Additional information
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Size range | 271-300 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |