ADK_YEAST
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 03-AUG-2022, entry version 184.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + ATP = ADP + AMP + 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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}.
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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; 247.
DR DIP; DIP-4681N; -.
DR IntAct; P47143; 4.
DR MINT; P47143; -.
DR STRING; 4932.YJR105W; -.
DR iPTMnet; P47143; -.
DR MaxQB; P47143; -.
DR PaxDb; P47143; -.
DR PRIDE; P47143; -.
DR EnsemblFungi; YJR105W_mRNA; YJR105W; YJR105W.
DR GeneID; 853569; -.
DR KEGG; sce:YJR105W; -.
DR SGD; S000003866; ADO1.
DR VEuPathDB; FungiDB:YJR105W; -.
DR eggNOG; KOG2854; Eukaryota.
DR GeneTree; ENSGT00390000014320; -.
DR HOGENOM; CLU_045832_1_0_1; -.
DR InParanoid; P47143; -.
DR OMA; APFIAQF; -.
DR BioCyc; YEAST:YJR105W-MON; -.
DR Reactome; R-SCE-74217; Purine salvage.
DR UniPathway; UPA00588; UER00659.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IMP:SGD.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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; PTHR45769; 1.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00989; ADENOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..340
FT /note="Adenosine kinase"
FT /id="PRO_0000080062"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
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
