ID PYRH_NOVAD Reviewed; 244 AA. AC Q2G8K8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 05-DEC-2018, entry version 84. 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=Saro_1371; OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP OS 105152 / NBRC 16084 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.; RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444."; RL Submitted (JAN-2006) 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 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; CP000248; ABD25815.1; -; Genomic_DNA. DR RefSeq; WP_011445029.1; NC_007794.1. DR ProteinModelPortal; Q2G8K8; -. DR SMR; Q2G8K8; -. DR STRING; 279238.Saro_1371; -. DR EnsemblBacteria; ABD25815; ABD25815; Saro_1371. DR KEGG; nar:Saro_1371; -. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR HOGENOM; HOG000047187; -. DR KO; K09903; -. DR OMA; PIIVFDM; -. DR OrthoDB; POG091H02JZ; -. DR BioCyc; NARO279238:G1G5T-1389-MONOMER; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000009134; 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; 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 1 244 Uridylate kinase. FT /FTId=PRO_1000053968. FT NP_BIND 16 19 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 139 146 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 58 58 UMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 59 59 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 63 63 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 78 78 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 166 166 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 172 172 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 175 175 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 244 AA; 26248 MW; FAF42119402C389F CRC64; MSLPSCVPGY RRILLKLSGE VLMGEQQFGI DTDYVARVAQ EVKDARDSGL EICLVIGGGN IFRGMAGAAK GMDRAQADYM GMLATVMNAL AMQSALEQLG VPTRVQSAIE MDKVCEPVIR RRAERHLEKG RIVIFAAGVG APYFTTDSGA ALRAAEMKCD ALLKGTSVDG VYNADPKKDP AAKRYETVDY DTVLADNLKV MDASAVALCR DNNIPIVVFS IRERGNLARV LAGEGTQTTV KKEA //