ID   ADK_YEAST               Reviewed;         340 AA.
AC   P47143; D6VWS4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 200.
DE   RecName: Full=Adenosine kinase {ECO:0000303|PubMed:11223943};
DE            EC=2.7.1.20 {ECO:0000269|PubMed:11223943};
GN   Name=ADO1 {ECO:0000303|PubMed:11223943}; OrderedLocusNames=YJR105W;
GN   ORFNames=J1973;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=11223943;
RX   DOI=10.1002/1097-0061(20010315)18:4<335::aid-yea674>3.0.co;2-x;
RA   Lecoq K., Belloc I., Desgranges C., Daignan-Fornier B.;
RT   "Role of adenosine kinase in Saccharomyces cerevisiae: identification of
RT   the ADO1 gene and study of the mutant phenotypes.";
RL   Yeast 18:335-342(2001).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14558146; DOI=10.1002/yea.1039;
RA   Barrado P., Rodriguez M.J., Jimenez A., Lobato M.F.;
RT   "Expression in Escherichia coli of a recombinant adenosine kinase from
RT   Saccharomyces cerevisiae: purification, kinetics and substrate analyses.";
RL   Yeast 20:1145-1150(2003).
CC   -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC       nucleoside analogs to monophosphate derivatives. ADO1 does not play a
CC       major role in adenine utilization in yeast. Its physiological role
CC       could primarily be to recycle adenosine produced by the methyl cycle.
CC       {ECO:0000269|PubMed:14558146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + ATP = AMP + ADP + H(+); Xref=Rhea:RHEA:20824,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20;
CC         Evidence={ECO:0000269|PubMed:14558146};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P55263};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.84 mM for ATP {ECO:0000269|PubMed:14558146};
CC         KM=0.003 mM for adenosine {ECO:0000269|PubMed:14558146};
CC         KM=1.84 mM for 3'-deoxyadenosine {ECO:0000269|PubMed:14558146};
CC         KM=0.26 mM for 3'-amino-3'-deoxyadenosine
CC         {ECO:0000269|PubMed:14558146};
CC         Vmax=0.18 mmol/min/mg enzyme towards ATP
CC         {ECO:0000269|PubMed:14558146};
CC         Vmax=0.17 mmol/min/mg enzyme towards adenosine
CC         {ECO:0000269|PubMed:14558146};
CC         Vmax=0.71 umol/min/mg enzyme towards 3'-deoxyadenosine
CC         {ECO:0000269|PubMed:14558146};
CC         Vmax=0.06 mmol/min/mg enzyme towards 3'-amino-3'-deoxyadenosine
CC         {ECO:0000269|PubMed:14558146};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenosine: step 1/1.
CC   -!- DISRUPTION PHENOTYPE: Results in a severe reduction of adenosine kinase
CC       activity. {ECO:0000269|PubMed:11223943}.
CC   -!- MISCELLANEOUS: Present with 22200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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; Z49605; CAA89635.1; -; Genomic_DNA.
DR   EMBL; AY558082; AAS56408.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08890.1; -; Genomic_DNA.
DR   PIR; S57126; S57126.
DR   RefSeq; NP_012639.1; NM_001181763.1.
DR   AlphaFoldDB; P47143; -.
DR   SMR; P47143; -.
DR   BioGRID; 33861; 259.
DR   DIP; DIP-4681N; -.
DR   FunCoup; P47143; 1567.
DR   IntAct; P47143; 6.
DR   MINT; P47143; -.
DR   STRING; 4932.YJR105W; -.
DR   iPTMnet; P47143; -.
DR   PaxDb; 4932-YJR105W; -.
DR   PeptideAtlas; P47143; -.
DR   EnsemblFungi; YJR105W_mRNA; YJR105W; YJR105W.
DR   GeneID; 853569; -.
DR   KEGG; sce:YJR105W; -.
DR   AGR; SGD:S000003866; -.
DR   SGD; S000003866; ADO1.
DR   VEuPathDB; FungiDB:YJR105W; -.
DR   eggNOG; KOG2854; Eukaryota.
DR   HOGENOM; CLU_045832_1_0_1; -.
DR   InParanoid; P47143; -.
DR   OMA; RTMCTYL; -.
DR   OrthoDB; 432447at2759; -.
DR   BioCyc; YEAST:YJR105W-MONOMER; -.
DR   Reactome; R-SCE-74217; Purine salvage.
DR   Reactome; R-SCE-9755088; Ribavirin ADME.
DR   UniPathway; UPA00588; UER00659.
DR   BioGRID-ORCS; 853569; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P47143; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47143; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004001; F:adenosine kinase activity; IDA:SGD.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IMP:SGD.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR   CDD; cd01168; adenosine_kinase; 1.
DR   Gene3D; 3.30.1110.10; -; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR001805; Adenokinase.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR45769; ADENOSINE KINASE; 1.
DR   PANTHER; PTHR45769:SF3; ADENOSINE KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00989; ADENOKINASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..340
FT                   /note="Adenosine kinase"
FT                   /id="PRO_0000080062"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         10
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         64
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         68
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         293
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
SQ   SEQUENCE   340 AA;  36372 MW;  F0F18B5831F025A5 CRC64;
     MTAPLVVLGN PLLDFQADVT AEYLAKYSLK ENDAILVDAK SGDAKMAIFD ELLQMPETKL
     VAGGAAQNTA RGAAYVLGAG QVVYFGSVGK DKFSERLLNE NEKAGVKSMY QVQNDIGTGK
     CAALITGHNR SLVTDLGAAN FFTPDHLDKH WDLVEAAKLF YIGGFHLTVS PDAIVKLGQH
     AKENSKPFVL NFSAPFIPHV FKDALARVLP YATVIIANES EAEAFCDAFQ LDCANTDLEA
     IAQRIVKDSP VEKTVIFTHG VEPTVVVSSK GTSTYPVKPL DSSKIVDTNG AGDAFAGGFM
     AGLTKGEDLE TSIDMGQWLA ALSIQEVGPS YPSEKISYSK
//