ID   ADK_PHYPA               Reviewed;         343 AA.
AC   O49923; A9SFV8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Adenosine kinase;
DE            Short=AK;
DE            EC=2.7.1.20;
DE   AltName: Full=Adenosine 5'-phosphotransferase;
GN   Name=ADK; ORFNames=PHYPADRAFT_184505;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=Cambridge;
RX   PubMed=9680981; DOI=10.1046/j.1365-313x.1998.00011.x;
RA   von Schwartzenberg K., Kruse S., Reski R., Moffatt B., Laloue M.;
RT   "Cloning and characterization of an adenosine kinase from Physcomitrella
RT   involved in cytokinin metabolism.";
RL   Plant J. 13:249-257(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
CC   -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC       nucleoside analogs to monophosphate derivatives. Can also act on the
CC       cytokinin isopentenyladenosine to produce isopentenyladenosine
CC       monophosphate. {ECO:0000269|PubMed:9680981}.
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   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenosine: step 1/1.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; Y15430; CAA75628.1; -; mRNA.
DR   EMBL; DS544963; EDQ69929.1; -; Genomic_DNA.
DR   RefSeq; XP_001765201.1; XM_001765149.1.
DR   AlphaFoldDB; O49923; -.
DR   SMR; O49923; -.
DR   STRING; 3218.PP1S74_140V6.1; -.
DR   EnsemblPlants; Pp3c3_10800V3.1; Pp3c3_10800V3.1; Pp3c3_10800.
DR   EnsemblPlants; Pp3c3_10800V3.2; Pp3c3_10800V3.2; Pp3c3_10800.
DR   Gramene; Pp3c3_10800V3.1; Pp3c3_10800V3.1; Pp3c3_10800.
DR   Gramene; Pp3c3_10800V3.2; Pp3c3_10800V3.2; Pp3c3_10800.
DR   eggNOG; KOG2854; Eukaryota.
DR   HOGENOM; CLU_045832_0_0_1; -.
DR   InParanoid; O49923; -.
DR   OMA; GGAAMNT; -.
DR   OrthoDB; 1226324at2759; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000006727; Chromosome 3.
DR   GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-EC.
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: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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..343
FT                   /note="Adenosine kinase"
FT                   /id="PRO_0000080059"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  37251 MW;  E29FEC383795E543 CRC64;
     MASEGVLLGM GNPLLDISCV VDDAFLEKYG LTLNNAILAE DKHLPMYKEL AANPDVEYIA
     GGATQNTIRI AQWMLGESNA TSYFGCVGKD EYGDRMFKLA SEGGVNIRYD VDEDLPTGTC
     GVLVVKGERS LVANLSAANK YKIDHLKKPE NWAFVEKAKY IYSAGFFLTV SPESMMTVAK
     HAAETGKYYM INLAAPFICQ FFKDPLMELF PYVDFIFGNE SEARAFAQVQ GWETEDTKVI
     AVKLAALPKA GGTHKRVAVI TQGTDPTIVA EDGKVTEFPV TPIPKEKLVD TNAAGDSFVG
     GFLSQLVLGK DIAQCVRAGN YAASVIIQRS GCTFPSKPSF ESQ