ID   PYRH_CALS4              Reviewed;         237 AA.
AC   Q8RA23;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAY-2019, entry version 98.
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};
GN   OrderedLocusNames=TTE1407;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 /
OS   JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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
CC       pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP-
CC       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; AE008691; AAM24629.1; -; Genomic_DNA.
DR   RefSeq; WP_009611037.1; NC_003869.1.
DR   SMR; Q8RA23; -.
DR   STRING; 273068.TTE1407; -.
DR   EnsemblBacteria; AAM24629; AAM24629; TTE1407.
DR   KEGG; tte:TTE1407; -.
DR   eggNOG; ENOG4105C41; Bacteria.
DR   eggNOG; COG0528; LUCA.
DR   HOGENOM; HOG000047187; -.
DR   KO; K09903; -.
DR   OMA; PIIVFDM; -.
DR   OrthoDB; 1043239at2; -.
DR   BioCyc; TTEN273068:G1FZJ-1506-MONOMER; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000000555; Chromosome.
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   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; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    237       Uridylate kinase.
FT                                /FTId=PRO_0000143901.
FT   NP_BIND      12     15       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   NP_BIND     133    140       UMP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      54     54       UMP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      55     55       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      59     59       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING      72     72       UMP. {ECO:0000255|HAMAP-Rule:MF_01220}.
FT   BINDING     166    166       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01220}.
FT   BINDING     169    169       ATP. {ECO:0000255|HAMAP-Rule:MF_01220}.
SQ   SEQUENCE   237 AA;  25789 MW;  93F6E495E73EEB6A CRC64;
     MSSVVYKRVV LKISGEALAG DKEFGIDFNV VNRIADEIKE VRDLGVQIGL VVGGGNIWRG
     RDAVGMDRTT ADHMGMLATV INALALQDAL EQRGVPTRVQ TAIEMRAIAE PYIRRRAIRH
     LEKGRVVIFA AGTGNPFFST DTAASLRAAE IDAEVILLAK KVDGVYDKDP LKHKDAVKFK
     ELSYLDVLNK GLGVMDSTAT SLCMDNKIPI IVFDLTTYGN IKKVVMGNDI GTIVKEG
//