ID Q636K1_BACCZ Unreviewed; 240 AA. AC Q636K1; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 25-MAY-2022, entry version 129. DE RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UK {ECO:0000256|HAMAP-Rule:MF_01220}; DE EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220}; DE AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220}; DE Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220}; GN Name=smbA {ECO:0000313|EMBL:AAU16682.1}; GN Synonyms=pyrH {ECO:0000256|HAMAP-Rule:MF_01220}; GN OrderedLocusNames=BCE33L3584 {ECO:0000313|EMBL:AAU16682.1}; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU16682.1, ECO:0000313|Proteomes:UP000002612}; RN [1] {ECO:0000313|Proteomes:UP000002612} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612}; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001018, ECO:0000256|HAMAP- CC Rule:MF_01220}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP. CC {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CC UDP from UMP (UMPK route): step 1/1. {ECO:0000256|ARBA:ARBA00004791, CC ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- SIMILARITY: Belongs to the UMP kinase family. CC {ECO:0000256|ARBA:ARBA00007614, ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000001; AAU16682.1; -; Genomic_DNA. DR RefSeq; WP_000042663.1; NZ_CP009968.1. DR SMR; Q636K1; -. DR EnsemblBacteria; AAU16682; AAU16682; BCE33L3584. DR GeneID; 59155678; -. DR GeneID; 64199164; -. DR KEGG; bcz:BCE33L3584; -. DR PATRIC; fig|288681.22.peg.1827; -. DR OMA; PIIVFDM; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000002612; 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 Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01220}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01220}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01220}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000313|EMBL:AAU16682.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01220}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000313|EMBL:AAU16682.1}. FT DOMAIN 7..217 FT /note="AA_kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT NP_BIND 12..15 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT NP_BIND 135..142 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT REGION 20..25 FT /note="Involved in allosteric activation by GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 54 FT /note="UMP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 55 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 59 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 74 FT /note="UMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 163 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 169 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" FT BINDING 172 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220" SQ SEQUENCE 240 AA; 25870 MW; 38F617B1244D4B9D CRC64; MSKPKYNRVV LKLSGEALAG EQGFGINPAV IKSVAEQVKE IAELDVEVAV VVGGGNIWRG KIGSEMGMDR AGADYMGMLA TVMNSLALQD SLENIGIQTR VQTSIEMRQV AEPYIRRKAV RHLEKKRVVI FAAGTGNPYF STDTTAALRA AEIEADVILM AKNNVDGVYN ADPSIDPTAT KYETLTYLDV LKEGLGVMDS TASSLCMDND IPLIVFSVME KGNIKRAVLG ENIGTVVRGK //