ID   PYRH_PARZE              Reviewed;         241 AA.
AC   P59005;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UK {ECO:0000255|HAMAP-Rule:MF_01220};
DE            EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220};
DE   AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE            Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220};
GN   Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220};
OS   Paracoccus zeaxanthinifaciens.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=187400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R114;
RA   Huembelin M.;
RT   "Genetics of isoprenoid biosynthesis in Paracoccus zeaxanthinifaciens.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000255|HAMAP-Rule:MF_01220}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01220};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP.
CC       {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}.
CC   -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01220}.
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DR   EMBL; AJ431698; CAD24428.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59005; -.
DR   SMR; P59005; -.
DR   UniPathway; UPA00159; UER00275.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04254; AAK_UMPK-PyrH-Ec; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01220_B; PyrH_B; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR011817; Uridylate_kinase.
DR   InterPro; IPR015963; Uridylate_kinase_bac.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF005650; Uridylate_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR02075; pyrH_bact; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..241
FT                   /note="Uridylate kinase"
FT                   /id="PRO_0000143869"
FT   REGION          23..28
FT                   /note="Involved in allosteric activation by GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         15..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         57
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         77
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         138..145
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   241 AA;  26076 MW;  97B4C7198449AA96 CRC64;
     MTSETPKQYG RVMLKISGEA LMGDQGFGLN PPTVARIANE VDSVAKMGVE VCMVIGGGNI
     FRGLQGSAQG MERTTADYMG MLATVMNALA MQSALEALGH HCRVISAIRM DEVCEPYIRR
     RAIRHLEKKR IVIFAAGTGN PYFTTDTAAT LRASEMNCEA IFKGTKVDGV YDKDPVKHAD
     AKRYGDVSYD EVLQKHLGVM DASAIALARD NKLPIIVFSL DAPGGFRSIL AGSGTYTRVH
     V