URK1_YEAST
ID URK1_YEAST Reviewed; 501 AA.
AC P27515; D6W1I7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Uridine kinase;
DE EC=2.7.1.48 {ECO:0000305|PubMed:10501935, ECO:0000305|PubMed:2169608};
DE AltName: Full=Uridine monophosphokinase;
GN Name=URK1; OrderedLocusNames=YNR012W; ORFNames=N2050;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=2169608; DOI=10.1093/nar/18.17.5279;
RA Kern L.;
RT "The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase.";
RL Nucleic Acids Res. 18:5279-5279(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10501935; DOI=10.1007/s002940050482;
RA Kurtz J.-E., Exinger F., Erbs P., Jund R.;
RT "New insights into the pyrimidine salvage pathway of Saccharomyces
RT cerevisiae: requirement of six genes for cytidine metabolism.";
RL Curr. Genet. 36:130-136(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the conversion of uridine into UMP and cytidine
CC into CMP in the pyrimidine salvage pathway.
CC {ECO:0000269|PubMed:10501935, ECO:0000269|PubMed:2169608}.
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:0000305|PubMed:2169608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16826;
CC Evidence={ECO:0000305|PubMed:2169608};
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:0000305|PubMed:10501935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24675;
CC Evidence={ECO:0000305|PubMed:10501935};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000305|PubMed:10501935}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000305|PubMed:2169608}.
CC -!- INTERACTION:
CC P27515; Q12084: DAS2; NbExp=4; IntAct=EBI-20151, EBI-35824;
CC P27515; P18562: FUR1; NbExp=3; IntAct=EBI-20151, EBI-20122;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; X53998; CAA37946.1; -; Genomic_DNA.
DR EMBL; X77395; CAA54580.1; -; Genomic_DNA.
DR EMBL; Z71627; CAA96289.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10553.1; -; Genomic_DNA.
DR PIR; S29374; S29374.
DR RefSeq; NP_014409.1; NM_001183189.1.
DR AlphaFoldDB; P27515; -.
DR SMR; P27515; -.
DR BioGRID; 35837; 88.
DR DIP; DIP-1720N; -.
DR IntAct; P27515; 7.
DR MINT; P27515; -.
DR STRING; 4932.YNR012W; -.
DR iPTMnet; P27515; -.
DR MaxQB; P27515; -.
DR PaxDb; P27515; -.
DR PRIDE; P27515; -.
DR EnsemblFungi; YNR012W_mRNA; YNR012W; YNR012W.
DR GeneID; 855746; -.
DR KEGG; sce:YNR012W; -.
DR SGD; S000005295; URK1.
DR VEuPathDB; FungiDB:YNR012W; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_0_2_1; -.
DR InParanoid; P27515; -.
DR OMA; RTKTMYG; -.
DR BioCyc; MetaCyc:YNR012W-MON; -.
DR BioCyc; YEAST:YNR012W-MON; -.
DR Reactome; R-SCE-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:P27515; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P27515; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; IMP:SGD.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008655; P:pyrimidine-containing compound salvage; IMP:SGD.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR000764; Uridine_kinase-like.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..501
FT /note="Uridine kinase"
FT /id="PRO_0000164462"
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 501 AA; 56296 MW; 30A0592899BCD040 CRC64;
MSHRIAPSKE RSSSFISILD DETRDTLKAN AVMDGEVDVK KTKGKSSRYI PPWTTPYIIG
IGGASGSGKT SVAAKIVSSI NVPWTVLISL DNFYNPLGPE DRARAFKNEY DFDEPNAINL
DLAYKCILNL KEGKRTNIPV YSFVHHNRVP DKNIVIYGAS VVVIEGIYAL YDRRLLDLMD
LKIYVDADLD VCLARRLSRD IVSRGRDLDG CIQQWEKFVK PNAVKFVKPT MKNADAIIPS
MSDNATAVNL IINHIKSKLE LKSNEHLREL IKLGSSPSQD VLNRNIIHEL PPTNQVLSLH
TMLLNKNLNC ADFVFYFDRL ATILLSWALD DIPVAHTNII TPGEHTMENV IACQFDQVTA
VNIIRSGDCF MKSLRKTIPN ITIGKLLIQS DSQTGEPQLH CEFLPPNIEK FGKVFLMEGQ
IISGAAMIMA IQVLLDHGID LEKISVVVYL ATEVGIRRIL NAFDNKVNIF AGMIISREKL
QNHQYKWALT RFFDSKYFGC D
