ID Q636K1_BACCZ Unreviewed; 240 AA. AC Q636K1; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 05-MAY-2009, entry version 42. DE SubName: Full=Uridylate kinase; DE EC=2.7.4.-; GN Name=smbA; OrderedLocusNames=BCE33L3584; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; YP_085166.1; -. DR GeneID; 3025654; -. DR GenomeReviews; CP000001_GR; BCE33L3584. DR KEGG; bcz:BCZK3584; -. DR HOGENOM; Q636K1; -. DR OMA; Q636K1; HMGMLAT. DR BioCyc; BCER288681:BCE33L3584-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR015963; Uridylate_kinase_bac. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR TIGRFAMs; TIGR02075; pyrH_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Transferase. 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 //