HAMAP rule MF_01220
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01220 |
| Accession | MF_01220 |
| Dates | 13-AUG-2002 (Created)
3-SEP-2024 (Last updated, Version 32) |
| Name | PyrH |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P0A7E9 (PYRH_ECOLI); O31749 (PYRH_BACSU); Q9PPX6 (PYRH_UREPA); Q8U122 (PYRH_PYRFU); Q97ZE2 (PYRH_SACS2); Q97R83 (PYRH_STRPN); P65933 (PYRH_SALTY); P43890 (PYRH_HAEIN); P65932 (PYRH_NEIMB); Q831V1 (PYRH_ENTFA); Q2FZ22 (PYRH_STAA8); P65938 (PYRH_STRP1); O28237 (PYRH_ARCFU); Q9Z5K8 (PYRH_LACLM); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_01220_B (Get profile general information and statistics) end case
case c? <OC:Archaea>
HAMAP; MF_01220_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 | PYRH |
| Protein name | RecName: Full=Uridylate kinase; Short=UK; EC=2.7.4.22; AltName: Full=Uridine monophosphate kinase; Short=UMP kinase; Short=UMPK; |
| Gene name | Name=pyrH; |
Comments
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| FUNCTION | Catalyzes the reversible phosphorylation of UMP to UDP. |
| CATALYTIC ACTIVITY | Reaction=UMP + ATP = UDP + ADP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.22; |
| case <FT:3> | |
| ACTIVITY REGULATION | Allosterically activated by GTP. Inhibited by UTP. |
| else | |
| ACTIVITY REGULATION | Inhibited by UTP. |
| end case | |
| PATHWAY | Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. |
| SUBUNIT | Homohexamer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the UMP kinase family. |
Keywords
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| case <FT:3> | |
| Allosteric enzyme | |
| end case | |
| ATP-binding | |
| Cytoplasm | |
| Kinase | |
| Nucleotide-binding | |
| Pyrimidine biosynthesis | |
| Transferase | |
Gene Ontology
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| GO:0009041; Molecular function:UMP/dUMP kinase activity |
| GO:0044210; Biological process:'de novo' CTP biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| From: PYRH_ECOLI (P0A7E9) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Bacteria> | ||||||||||||
| BINDING | 15 | 18 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K-x-[SG]-G | ||||||||
| BINDING | 138 | 145 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
|||||||||
| REGION | 23 | 28 | /note="Involved in allosteric activation by GTP" | G-x-x-G-x-G | ||||||||
| BINDING | 57 | 57 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
G | ||||||||
| BINDING | 58 | 58 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G | ||||||||
| BINDING | 62 | 62 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
| BINDING | 77 | 77 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
D | ||||||||
| BINDING | 165 | 165 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
T | ||||||||
| BINDING | 166 | 166 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[NQ] | ||||||||
| BINDING | 171 | 171 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[YF] | ||||||||
| BINDING | 174 | 174 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[DE] | ||||||||
| end case | ||||||||||||
| From: PYRH_SACS2 (Q97ZE2) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Archaea> | ||||||||||||
| BINDING | 7 | 11 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K-x-[ST]-G-[KRS] | ||||||||
| BINDING | 114 | 120 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
|||||||||
| BINDING | 44 | 44 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
G | ||||||||
| BINDING | 66 | 66 | /ligand="UMP" /ligand_id="ChEBI:CHEBI:57865" |
D | ||||||||
| BINDING | 45 | 45 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G | ||||||||
| BINDING | 49 | 49 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
| BINDING | 140 | 140 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[TS] | ||||||||
| BINDING | 141 | 141 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
N | ||||||||
| BINDING | 146 | 146 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[YF] | ||||||||
| BINDING | 149 | 149 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[DE] | ||||||||
| end case | ||||||||||||
| From: PYRH_PYRFU (Q8U122) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Archaea> and not <FT:12> | ||||||||||||
| BINDING | 9 | 10 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-S | ||||||||
| end case | ||||||||||||
Additional information
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| Size range | 217-241 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Archaea (SACS2) and UREPA are shown not to be allosterically activated by GTP. This may be due to the absence of a little region containing the motif GXXGXG in the N-terminal part of the enzyme, which could be involved in activation by GTP (see PubMed:18021254). Thus, the activation is automatically annotated via the presence/absence of this region, but the motif GXXGXG is maybe too strict, since NEIMB, that possesses the motif GSDPFG is also shown to be activated by GTP. Two magnesium ions are seen in the catalytic site of PYRFU, but only one in that of SACS2, which binds the phosphate groups of both ATP and UMP. Magnesium 1 annotated in PYRFU could have a catalytic role in the phosphoryl group transfer, a role that could be taken in charge by a positively charged lysine residue in bacteria (Lys-15 in ECOLI) and some other archaea (included SACS2) (see PubMed:17297917). Since the exact catalytic mechanism is not very clear yet and the residues that bind magnesium are not well conserved, this is not annotated and propagated by the rule. Possible wrong start in DEIRA and SYNY3. Longer C-terminus in MALP2; sequence not taken into account in size range. |