URK_STRP3
ID URK_STRP3 Reviewed; 208 AA.
AC P0DH36; P67416; Q99Z70;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Uridine kinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE EC=2.7.1.48 {ECO:0000255|HAMAP-Rule:MF_00551};
DE AltName: Full=Cytidine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE AltName: Full=Uridine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
GN Name=udk {ECO:0000255|HAMAP-Rule:MF_00551}; OrderedLocusNames=SpyM3_1042;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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:0000255|HAMAP-Rule:MF_00551};
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:0000255|HAMAP-Rule:MF_00551};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00551}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00551}.
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DR EMBL; AE014074; AAM79649.1; -; Genomic_DNA.
DR RefSeq; WP_002984060.1; NC_004070.1.
DR AlphaFoldDB; P0DH36; -.
DR SMR; P0DH36; -.
DR EnsemblBacteria; AAM79649; AAM79649; SpyM3_1042.
DR GeneID; 57852870; -.
DR KEGG; spg:SpyM3_1042; -.
DR HOGENOM; CLU_021278_1_2_9; -.
DR OMA; TTLKPMH; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000000564; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
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; -; 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 Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..208
FT /note="Uridine kinase"
FT /id="PRO_0000164502"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
SQ SEQUENCE 208 AA; 23816 MW; 510007D58B379DB6 CRC64;
MLKKPIIIGV TGGSGGGKTS VSRAILDSFP NARIAMIQHD SYYKDQSHMS FEERVKTNYD
HPLAFDTDFM IQQLKELLAG RPVDIPIYDY KKHTRSNTTF RQDPQDVIIV EGILVLEDER
LRDLMDIKLF VDTDDDIRII RRIKRDMMER GRSLESIIDQ YTSVVKPMYH QFIEPSKRYA
DIVIPEGVSN VVAIDVINSK IASILGEV