ID Q1GBC1_LACDA Unreviewed; 217 AA. AC Q1GBC1; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Uridine kinase {ECO:0000256|ARBA:ARBA00021478, ECO:0000256|HAMAP-Rule:MF_00551}; DE EC=2.7.1.48 {ECO:0000256|ARBA:ARBA00012137, ECO:0000256|HAMAP-Rule:MF_00551}; DE AltName: Full=Cytidine monophosphokinase {ECO:0000256|HAMAP-Rule:MF_00551}; DE AltName: Full=Uridine monophosphokinase {ECO:0000256|HAMAP-Rule:MF_00551}; GN Name=udk1 {ECO:0000313|EMBL:CAI97347.1}; GN Synonyms=udk {ECO:0000256|HAMAP-Rule:MF_00551}; GN OrderedLocusNames=Ldb0516 {ECO:0000313|EMBL:CAI97347.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM OS 00102 / Lb 14). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97347.1, ECO:0000313|Proteomes:UP000001259}; RN [1] {ECO:0000313|EMBL:CAI97347.1, ECO:0000313|Proteomes:UP000001259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14 RC {ECO:0000313|Proteomes:UP000001259}; RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P., RA Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive RT and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00000503, CC ECO:0000256|RuleBase:RU003825}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00000734, ECO:0000256|HAMAP- CC Rule:MF_00551, ECO:0000256|RuleBase:RU003825}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CC CTP from cytidine: step 1/3. {ECO:0000256|ARBA:ARBA00004784, CC ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; CC UMP from uridine: step 1/1. {ECO:0000256|ARBA:ARBA00004690, CC ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551, CC ECO:0000256|RuleBase:RU003825}. CC -!- SIMILARITY: Belongs to the uridine kinase family. CC {ECO:0000256|ARBA:ARBA00005408, ECO:0000256|HAMAP-Rule:MF_00551, CC ECO:0000256|RuleBase:RU003825}. 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; CR954253; CAI97347.1; -; Genomic_DNA. DR RefSeq; WP_003622588.1; NZ_JQAV01000001.1. DR AlphaFoldDB; Q1GBC1; -. DR STRING; 390333.Ldb0516; -. DR KEGG; ldb:Ldb0516; -. DR PATRIC; fig|390333.13.peg.281; -. DR eggNOG; COG0572; Bacteria. DR HOGENOM; CLU_021278_1_2_9; -. DR BioCyc; LDEL390333:LDB_RS02205-MONOMER; -. DR UniPathway; UPA00574; UER00637. DR UniPathway; UPA00579; UER00640. DR Proteomes; UP000001259; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0043771; F:cytidine kinase activity; IEA:RHEA. DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR CDD; cd02023; UMPK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00551; Uridine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006083; PRK/URK. DR InterPro; IPR026008; Uridine_kinase. DR InterPro; IPR000764; Uridine_kinase-like. DR NCBIfam; TIGR00235; udk; 1. DR PANTHER; PTHR10285; URIDINE KINASE; 1. DR PANTHER; PTHR10285:SF226; URIDINE KINASE; 1. DR Pfam; PF00485; PRK; 1. DR PRINTS; PR00988; URIDINKINASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00551, KW ECO:0000256|RuleBase:RU003825}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00551, ECO:0000256|RuleBase:RU003825}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00551}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00551}; Reference proteome {ECO:0000313|Proteomes:UP000001259}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00551}. FT DOMAIN 9..195 FT /note="Phosphoribulokinase/uridine kinase" FT /evidence="ECO:0000259|Pfam:PF00485" FT BINDING 14..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00551" SQ SEQUENCE 217 AA; 24866 MW; 5413C0746D7A734B CRC64; MSKKQHPIII GIAGGSGSGK TTIAHELYDQ FKTDRIRIIT EDSYYKNHPE MSMAERNKIN FDHPDAFDTE LLISQLQDLL NGKAIEMPIY DFTTHLRSPE TVHVEPADII ILEGILVLAS EELRNLMDIK IFVDTDDDIR LIRRQRRDMA ERGRSFDSII DQYLATVKPS YHQFVEPSKR YANIIVPEGG ANDVALDMLI TKVRDILRRN DLAEKEA //