ID PYRH_STRR6 Reviewed; 247 AA. AC Q8DQ50; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-FEB-2022, entry version 103. 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=spr0845; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). 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: Allosterically activated by GTP. Inhibited by UTP. CC {ECO:0000255|HAMAP-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; AE007317; AAK99649.1; -; Genomic_DNA. DR PIR; E97977; E97977. DR RefSeq; NP_358439.1; NC_003098.1. DR SMR; Q8DQ50; -. DR STRING; 171101.spr0845; -. DR EnsemblBacteria; AAK99649; AAK99649; spr0845. DR KEGG; spr:spr0845; -. DR PATRIC; fig|171101.6.peg.933; -. DR eggNOG; COG0528; Bacteria. DR HOGENOM; CLU_033861_0_0_9; -. DR OMA; PIIVFDM; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central. 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 Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1..247 FT /note="Uridylate kinase" FT /id="PRO_0000143893" FT NP_BIND 14..17 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT NP_BIND 137..144 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT REGION 22..27 FT /note="Involved in allosteric activation by GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 56 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 57 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 61 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 76 FT /note="UMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 165 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 171 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" FT BINDING 174 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220" SQ SEQUENCE 247 AA; 26693 MW; 6DEF633ED4EBFFD4 CRC64; MKMANPKYKR ILIKLSGEAL AGERGVGIDI QTVQTIAKEI QEVHSLGIEI ALVIGGGNLW RGEPAAEAGM DRVQADYTGM LGTVMNALVM ADSLQQVGVD TRVQTAIAMQ QVAEPYVRGR ALRHLEKGRI VIFGAGIGSP YFSTDTTAAL RAAEIEADAI LMAKNGVDGV YNADPKKDKT AVKFEELTHR DVINKGLRIM DSTASTLSMD NDIDLVVFNM NQSGNIKRVV FGENIGTTVS NNIEEKE //