ID   PYRH_MYCSJ              Reviewed;         252 AA.
AC   A3PXZ4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=Mjls_1984;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) 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: Inhibited by UTP. {ECO:0000255|HAMAP-
CC       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; CP000580; ABN97771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PXZ4; -.
DR   SMR; A3PXZ4; -.
DR   STRING; 164757.Mjls_1984; -.
DR   KEGG; mjl:Mjls_1984; -.
DR   HOGENOM; CLU_033861_0_0_11; -.
DR   OMA; PIIVFDM; -.
DR   BioCyc; MSP164757:G1G8C-2004-MON; -.
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   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..252
FT                   /note="Uridylate kinase"
FT                   /id="PRO_0000323888"
FT   BINDING         27..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         68
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         88
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         149..156
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   252 AA;  26712 MW;  D608546E1509A346 CRC64;
     MSEPNSDHGA GAAVGETRPL YSRVLLKLGG EMFGGGAVGL DPDVVHLVAR QIAEVVRSGV
     QVAVVIGGGN FFRGAQLQQR GMERTRSDYM GMLGTVMNSL ALQDFLEKEG IDTRVQTAIT
     MGQVAEPYIP LRAVRHLEKG RVVIFGAGMG LPYFSTDTTA AQRALEIGAE VVLMAKAVDG
     VYTADPRKDP DAQLLTAITH REVIDRGLAV ADATAFSLCM DNGMPILVFN LLVDGNIARA
     VAGEKIGTLV TT