ID   ADK_CRIGR               Reviewed;         361 AA.
AC   P55262; G3GWQ3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Adenosine kinase;
DE            Short=AK;
DE            EC=2.7.1.20 {ECO:0000269|PubMed:8917457};
DE   AltName: Full=Adenosine 5'-phosphotransferase;
GN   Name=ADK;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP   AND FUNCTION.
RC   TISSUE=Liver, and Ovary;
RX   PubMed=8917457; DOI=10.1111/j.1432-1033.1996.00564.x;
RA   Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.;
RT   "Cloning and characterization of cDNA for adenosine kinase from mammalian
RT   (Chinese hamster, mouse, human and rat) species. High frequency mutants of
RT   Chinese hamster ovary cells involve structural alterations in the gene.";
RL   Eur. J. Biochem. 241:564-571(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the purine nucleoside
CC       adenosine at the 5' position in an ATP-dependent manner. Serves as a
CC       potential regulator of concentrations of extracellular adenosine and
CC       intracellular adenine nucleotides. {ECO:0000269|PubMed:8917457}.
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         Evidence={ECO:0000269|PubMed:8917457};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20825;
CC         Evidence={ECO:0000305|PubMed:8917457};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P55263};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P55263};
CC   -!- ACTIVITY REGULATION: Activity is inhibited by 5-iodotubercidin and 5'-
CC       amino-5'-deoxyadenosine. {ECO:0000250|UniProtKB:P55263}.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenosine: step 1/1.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55263}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA91648.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U26588; AAA91648.1; ALT_FRAME; mRNA.
DR   EMBL; JH000053; EGV97815.1; -; Genomic_DNA.
DR   PIR; JC7368; JC7368.
DR   RefSeq; NP_001231779.1; NM_001244850.1.
DR   STRING; 10029.NP_001231779.1; -.
DR   Ensembl; ENSCGRT00001020046; ENSCGRP00001015803; ENSCGRG00001016316.
DR   Ensembl; ENSCGRT00015024907; ENSCGRP00015020238; ENSCGRG00015015437.
DR   GeneID; 100736551; -.
DR   KEGG; cge:100736551; -.
DR   CTD; 132; -.
DR   eggNOG; KOG2854; Eukaryota.
DR   GeneTree; ENSGT00390000014320; -.
DR   InParanoid; P55262; -.
DR   OMA; APFIAQF; -.
DR   OrthoDB; 1226324at2759; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004001; F:adenosine kinase activity; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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: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; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..361
FT                   /note="Adenosine kinase"
FT                   /id="PRO_0000080052"
FT   MOTIF           7..15
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   ACT_SITE        316
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         34
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   BINDING         305
FT                   /ligand="adenosine"
FT                   /ligand_id="ChEBI:CHEBI:16335"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
SQ   SEQUENCE   361 AA;  40246 MW;  B4A727B30264B080 CRC64;
     MAAAEEPKPK KLKVEAPQAL SENVLFGMGN PLLDISAVVD KDFLDKYSLK PNDQILAEEK
     HKELFDELVR KFKVEYHAGG STQNSIKVAQ WMIQKPHKAA TFFGCIGIDK FGEILKSKAA
     EAHVDAHYYE QNEQPTGTCA ACITGDNRSL VANLAAANCY KKEKHLDLEN NWVLVEKARV
     YYIAGFFLTV SPESVLKVAR YAAENNRIFT LNLSAPFISQ FFKESLMEVM PYVDILFGNE
     TEAATFAREQ GFETKDIKEI AKKAQALAKV NSKRPRTVVF TQGRDDTVVA TENEVMAFAV
     LDQNQKEIID TNGAGDAFVG GFLSQLVYNK PLTECIRAGH YAASVIIRRT GCTFPEKPDF
     H