HAMAP rule MF_00583
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00583 |
| Accession | MF_00583 |
| Dates | 28-FEB-2005 (Created)
03-SEP-2024 (Last updated, Version 37) |
| Name | RibP_PPkinase |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P14193; P0A717; Q97CA5; Q58761; P9WKE3; [ 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=D-ribose 5-phosphate + ATP = 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 |