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 15-FEB-2017, 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}; 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: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- ENZYME 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE008691; AAM24629.1; -; Genomic_DNA. DR RefSeq; WP_009611037.1; NC_003869.1. DR ProteinModelPortal; Q8RA23; -. DR STRING; 273068.TTE1407; -. DR PRIDE; Q8RA23; -. DR EnsemblBacteria; AAM24629; AAM24629; TTE1407. DR KEGG; tte:TTE1407; -. DR PATRIC; 23897528; VBITheTen82880_1417. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR HOGENOM; HOG000047187; -. DR KO; K09903; -. DR OMA; KGLKVMD; -. DR OrthoDB; POG09170047; -. 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 Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_B; PyrH_B; 1. 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 //