ID Q636K1_BACCZ Unreviewed; 240 AA. AC Q636K1; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 08-MAY-2019, entry version 120. 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., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., 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., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA 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, ECO:0000256|SAAS:SAAS01087336}. 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:0000256|HAMAP- CC Rule:MF_01220, ECO:0000256|SAAS:SAAS01122072}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by CC UTP. {ECO:0000256|HAMAP-Rule:MF_01220}. CC -!- ACTIVITY REGULATION: Inhibited by UTP. CC {ECO:0000256|SAAS:SAAS01071959}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01220, ECO:0000256|SAAS:SAAS00056421}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220, CC ECO:0000256|SAAS:SAAS01087343}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220, CC ECO:0000256|SAAS:SAAS00056429}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000256|HAMAP- CC Rule:MF_01220, ECO:0000256|SAAS:SAAS01087340}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 KEGG; bcz:BCE33L3584; -. DR PATRIC; fig|288681.22.peg.1827; -. DR KO; K09903; -. 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 ECO:0000256|SAAS:SAAS00056455}; KW Complete proteome {ECO:0000313|Proteomes:UP000002612}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220, KW ECO:0000256|SAAS:SAAS00056495}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01220, KW ECO:0000256|SAAS:SAAS00056414, ECO:0000313|EMBL:AAU16682.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220, KW ECO:0000256|SAAS:SAAS00056462}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01220, KW ECO:0000256|SAAS:SAAS00056469}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01220, KW ECO:0000256|SAAS:SAAS00056481, ECO:0000313|EMBL:AAU16682.1}. FT DOMAIN 7 217 AA_kinase. {ECO:0000259|Pfam:PF00696}. FT NP_BIND 12 15 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}. FT NP_BIND 135 142 UMP. {ECO:0000256|HAMAP-Rule:MF_01220}. FT REGION 20 25 Involved in allosteric activation by GTP. FT {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 54 54 UMP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 55 55 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 59 59 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 74 74 UMP. {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 163 163 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}. FT BINDING 169 169 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01220}. FT BINDING 172 172 ATP. {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 //