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 23-FEB-2022, entry version 92. 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=Saro_1371; OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG OS 56034 / CIP 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 / CCUG 56034 / CIP 105152 / NBRC 16084 / RC 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 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; CP000248; ABD25815.1; -; Genomic_DNA. DR RefSeq; WP_011445029.1; NC_007794.1. DR SMR; Q2G8K8; -. DR STRING; 279238.Saro_1371; -. DR PRIDE; Q2G8K8; -. DR EnsemblBacteria; ABD25815; ABD25815; Saro_1371. DR KEGG; nar:Saro_1371; -. DR eggNOG; COG0528; Bacteria. DR HOGENOM; CLU_033861_0_0_5; -. DR OMA; PIIVFDM; -. DR OrthoDB; 1043239at2; -. 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 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..244 FT /note="Uridylate kinase" FT /id="PRO_1000053968" FT NP_BIND 16..19 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT NP_BIND 139..146 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 58 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 59 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 63 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 78 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 166 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 172 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 175 FT /note="ATP" FT /evidence="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 //