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 12-AUG-2020, entry version 101. 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=TTE1407; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM OS 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., Chen Y., RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., RA 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 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}. 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 SMR; Q8RA23; -. DR STRING; 273068.TTE1407; -. DR EnsemblBacteria; AAM24629; AAM24629; TTE1407. DR KEGG; tte:TTE1407; -. DR eggNOG; COG0528; Bacteria. DR HOGENOM; CLU_033861_0_0_9; -. 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; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1..237 FT /note="Uridylate kinase" FT /id="PRO_0000143901" FT NP_BIND 12..15 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT NP_BIND 133..140 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 54 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 55 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 59 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 72 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 166 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 169 FT /note="ATP" FT /evidence="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 //