ID   ADK2_ARATH              Reviewed;         345 AA.
AC   Q9LZG0;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Adenosine kinase 2 {ECO:0000303|PubMed:11115893};
DE            Short=AK 2 {ECO:0000305};
DE            EC=2.7.1.20 {ECO:0000269|PubMed:11115893};
DE   AltName: Full=Adenosine 5'-phosphotransferase 2 {ECO:0000303|PubMed:11115893};
GN   Name=ADK2 {ECO:0000303|PubMed:11115893};
GN   OrderedLocusNames=At5g03300 {ECO:0000312|Araport:AT5G03300};
GN   ORFNames=F12E4.30 {ECO:0000312|EMBL:CAB83286.1},
GN   MOK16.21 {ECO:0000312|EMBL:BAB08390.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11115893; DOI=10.1104/pp.124.4.1775;
RA   Moffatt B.A., Wang L., Allen M.S., Stevens Y.Y., Qin W., Snider J.,
RA   von Schwartzenberg K.;
RT   "Adenosine kinase of Arabidopsis. Kinetic properties and gene expression.";
RL   Plant Physiol. 124:1775-1785(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS AL2 AND BEET CURLY TOP VIRUS
RP   L2, AND ACTIVITY REGULATION.
RX   PubMed=14615595; DOI=10.1105/tpc.015180;
RA   Wang H., Hao L., Shung C.-Y., Sunter G., Bisaro D.M.;
RT   "Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins.";
RL   Plant Cell 15:3020-3032(2003).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17272833; DOI=10.1093/jxb/erl275;
RA   Pereira L.A.R., Todorova M., Cai X., Makaroff C.A., Emery R.J.N.,
RA   Moffatt B.A.;
RT   "Methyl recycling activities are co-ordinately regulated during plant
RT   development.";
RL   J. Exp. Bot. 58:1083-1098(2007).
RN   [8]
RP   INTERACTION WITH KIN11, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=24498147; DOI=10.1371/journal.pone.0087592;
RA   Mohannath G., Jackel J.N., Lee Y.H., Buchmann R.C., Wang H., Patil V.,
RA   Adams A.K., Bisaro D.M.;
RT   "A complex containing SNF1-related kinase (SnRK1) and adenosine kinase in
RT   Arabidopsis.";
RL   PLoS ONE 9:E87592-E87592(2014).
CC   -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC       nucleoside analogs to monophosphate derivatives (PubMed:11115893).
CC       Essential to sustain methyl recycling (PubMed:17272833).
CC       {ECO:0000269|PubMed:11115893, ECO:0000269|PubMed:17272833}.
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:11115893};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20825;
CC         Evidence={ECO:0000269|PubMed:11115893};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P55263};
CC   -!- ACTIVITY REGULATION: Inactivated by the begomovirus AL2 protein or the
CC       curtovirus L2 protein. {ECO:0000269|PubMed:14615595}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 uM for adenosine {ECO:0000269|PubMed:11115893};
CC         KM=370 uM for ATP {ECO:0000269|PubMed:11115893};
CC         Vmax=6.7 umol/min/mg enzyme with adenosine as substrate
CC         {ECO:0000269|PubMed:11115893};
CC         Vmax=7.8 umol/min/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:11115893};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenosine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with the begomovirus AL2 protein and the curtovirus
CC       L2 protein (PubMed:14615595). Interacts with KIN11 (PubMed:24498147).
CC       {ECO:0000269|PubMed:14615595, ECO:0000269|PubMed:24498147}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24498147}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11115893,
CC       ECO:0000269|PubMed:17272833}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during the lignification process in
CC       inflorescence stems. {ECO:0000269|PubMed:17272833}.
CC   -!- PTM: Phosphorylated by KIN11. {ECO:0000269|PubMed:24498147}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; AF180895; AAG45247.1; -; mRNA.
DR   EMBL; AF180897; AAG45249.1; -; Genomic_DNA.
DR   EMBL; AB005240; BAB08390.1; -; Genomic_DNA.
DR   EMBL; AL162751; CAB83286.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90582.1; -; Genomic_DNA.
DR   EMBL; AY042855; AAK68795.1; -; mRNA.
DR   EMBL; AY072485; AAL66900.1; -; mRNA.
DR   PIR; T48351; T48351.
DR   RefSeq; NP_195950.1; NM_120408.4.
DR   AlphaFoldDB; Q9LZG0; -.
DR   SMR; Q9LZG0; -.
DR   BioGRID; 17158; 1.
DR   IntAct; Q9LZG0; 1.
DR   STRING; 3702.AT5G03300.1; -.
DR   iPTMnet; Q9LZG0; -.
DR   MetOSite; Q9LZG0; -.
DR   PaxDb; Q9LZG0; -.
DR   PRIDE; Q9LZG0; -.
DR   ProteomicsDB; 244701; -.
DR   EnsemblPlants; AT5G03300.1; AT5G03300.1; AT5G03300.
DR   GeneID; 831882; -.
DR   Gramene; AT5G03300.1; AT5G03300.1; AT5G03300.
DR   KEGG; ath:AT5G03300; -.
DR   Araport; AT5G03300; -.
DR   TAIR; locus:2142609; AT5G03300.
DR   eggNOG; KOG2854; Eukaryota.
DR   HOGENOM; CLU_045832_0_0_1; -.
DR   InParanoid; Q9LZG0; -.
DR   OMA; MYEEMTK; -.
DR   OrthoDB; 1226324at2759; -.
DR   PhylomeDB; Q9LZG0; -.
DR   BioCyc; MetaCyc:AT5G03300-MON; -.
DR   BRENDA; 2.7.1.20; 399.
DR   UniPathway; UPA00588; UER00659.
DR   PRO; PR:Q9LZG0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZG0; baseline and differential.
DR   Genevisible; Q9LZG0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0004001; F:adenosine kinase activity; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0006169; P:adenosine salvage; TAS:TAIR.
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; IBA:GO_Central.
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; Cytoplasm; Host-virus interaction; Kinase; Magnesium;
KW   Nucleotide-binding; Phosphoprotein; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..345
FT                   /note="Adenosine kinase 2"
FT                   /id="PRO_0000080058"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000250|UniProtKB:P55263"
SQ   SEQUENCE   345 AA;  37846 MW;  0834B163049F740E CRC64;
     MASSSNYDGI LLGMGNPLLD ISAVVDDEFL TKYDIKLNNA ILAEDKHLPM YDEMSSKFNV
     EYIAGGATQN SIKVAQWMLQ IPGATSYMGS IGKDKYGEAM KKDATAAGVN VHYYEDESAP
     TGTCGVCVVG GERSLIANLS AANCYKVDHL KKPENWALVE KAKFYYIAGF FLTVSPESIQ
     LVSEHAAANN KVFTMNLSAP FICEFFKDVQ EKFLPYMDFV FGNETEARTF SRVHGWETED
     VEQIAIKISQ LPKATGTYKR TTVITQGADP VVVAEDGKVK KYPVIPLPKE KLVDTNGAGD
     AFVGGFMSQL VKEKSIEECV KAGCYASNVV IQRSGCTYPE KPDFN