AC   MF_01220;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01220_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_01220_A; -; 1; level=0
XX
Names: PyrH
XX
ID   PYRH
DE   RecName: Full=Uridylate kinase;
DE            Short=UK;
DE            EC=2.7.4.22;
DE   AltName: Full=Uridine monophosphate kinase;
DE            Short=UMP kinase;
DE            Short=UMPK;
GN   Name=pyrH;
XX
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.22;
case <FT:3>
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP.
else
CC   -!- ACTIVITY REGULATION: Inhibited by UTP.
end case
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       UDP from UMP (UMPK route): step 1/1.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the UMP kinase family.
XX
DR   Pfam; PF00696; AA_kinase; 1; trigger=no
DR   NCBIfam; TIGR02075; PyrH_bact; 1; trigger=no
DR   NCBIfam; TIGR02076; PyrH_arch; 1; trigger=no
XX
case <FT:3>
KW   Allosteric enzyme
end case
KW   ATP-binding
KW   Cytoplasm
KW   Kinase
KW   Nucleotide-binding
KW   Pyrimidine biosynthesis
KW   Transferase
XX
GO   GO:0009041; F:UMP/dUMP kinase activity
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PYRH_ECOLI (P0A7E9)
case <OC:Bacteria>
FT   BINDING         15..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K-x-[SG]-G
FT   BINDING         138..145
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   REGION          23..28
FT                   /note="Involved in allosteric activation by GTP"
FT   Optional; Condition: G-x-x-G-x-G
FT   BINDING         57
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   Condition: G
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         77
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   Condition: D
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: T
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [NQ]
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [YF]
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DE]
end case
FT   From: PYRH_SACS2 (Q97ZE2)
case <OC:Archaea>
FT   BINDING         7..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: K-x-[ST]-G-[KRS]
FT   BINDING         114..120
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   BINDING         44
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   Condition: G
FT   BINDING         66
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT   Condition: D
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [TS]
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: N
FT   BINDING         146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [YF]
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DE]
end case
FT   From: PYRH_PYRFU (Q8U122)
case <OC:Archaea> and not <FT:12>
FT   BINDING         9..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-S
end case
XX
case <OC:Bacteria>
Size: 231-266;
end case
case <OC:Archaea>
Size: 217-241;
end case
Related: None;
Template: P0A7E9; O31749; Q9PPX6; Q8U122; Q97ZE2; Q97R83; P65933; P43890; P65932; Q831V1; Q2FZ22; P65938; O28237; Q9Z5K8;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.30 2023/06/01
//