ADK1_ARATH
ID ADK1_ARATH Reviewed; 344 AA.
AC Q9SF85; B3LFB3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Adenosine kinase 1 {ECO:0000303|PubMed:11115893};
DE Short=AK 1 {ECO:0000305};
DE EC=2.7.1.20 {ECO:0000269|PubMed:11115893};
DE AltName: Full=Adenosine 5'-phosphotransferase 1 {ECO:0000303|PubMed:11115893};
GN Name=ADK1 {ECO:0000303|PubMed:11115893};
GN OrderedLocusNames=At3g09820 {ECO:0000312|Araport:AT3G09820};
GN ORFNames=F8A24.13 {ECO:0000312|EMBL:AAF23253.1};
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] (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS AL2 AND BEET CURLY TOP VIRUS
RP L2.
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).
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:0000250|UniProtKB:Q9LZG0}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for adenosine {ECO:0000269|PubMed:11115893};
CC KM=350 uM for ATP {ECO:0000269|PubMed:11115893};
CC Vmax=2.7 umol/min/mg enzyme with adenosine as substrate
CC {ECO:0000269|PubMed:11115893};
CC Vmax=3.5 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. {ECO:0000269|PubMed:14615595}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SF85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SF85-2; Sequence=VSP_040515, VSP_040516;
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 -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AF180896; AAG45248.1; -; Genomic_DNA.
DR EMBL; AF180894; AAG45246.1; -; mRNA.
DR EMBL; AC015985; AAF23253.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74816.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74817.1; -; Genomic_DNA.
DR EMBL; AF375451; AAK53035.1; -; mRNA.
DR EMBL; BT033101; ACF16163.1; -; mRNA.
DR RefSeq; NP_187593.1; NM_111817.4. [Q9SF85-1]
DR RefSeq; NP_974269.1; NM_202540.1. [Q9SF85-2]
DR AlphaFoldDB; Q9SF85; -.
DR SMR; Q9SF85; -.
DR BioGRID; 5474; 5.
DR IntAct; Q9SF85; 1.
DR STRING; 3702.AT3G09820.1; -.
DR MetOSite; Q9SF85; -.
DR PaxDb; Q9SF85; -.
DR PRIDE; Q9SF85; -.
DR ProMEX; Q9SF85; -.
DR ProteomicsDB; 244755; -. [Q9SF85-1]
DR EnsemblPlants; AT3G09820.1; AT3G09820.1; AT3G09820. [Q9SF85-1]
DR EnsemblPlants; AT3G09820.2; AT3G09820.2; AT3G09820. [Q9SF85-2]
DR GeneID; 820140; -.
DR Gramene; AT3G09820.1; AT3G09820.1; AT3G09820. [Q9SF85-1]
DR Gramene; AT3G09820.2; AT3G09820.2; AT3G09820. [Q9SF85-2]
DR KEGG; ath:AT3G09820; -.
DR Araport; AT3G09820; -.
DR TAIR; locus:2085079; AT3G09820.
DR eggNOG; KOG2854; Eukaryota.
DR HOGENOM; CLU_045832_0_0_1; -.
DR InParanoid; Q9SF85; -.
DR OMA; GGAAMNT; -.
DR OrthoDB; 1226324at2759; -.
DR PhylomeDB; Q9SF85; -.
DR BioCyc; MetaCyc:AT3G09820-MON; -.
DR BRENDA; 2.7.1.20; 399.
DR UniPathway; UPA00588; UER00659.
DR PRO; PR:Q9SF85; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF85; baseline and differential.
DR Genevisible; Q9SF85; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
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:0009506; C:plasmodesma; 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: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 GO; GO:0080094; P:response to trehalose-6-phosphate; IEP:TAIR.
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 Alternative splicing; ATP-binding; Host-virus interaction; Kinase;
KW Magnesium; Nucleotide-binding; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..344
FT /note="Adenosine kinase 1"
FT /id="PRO_0000080057"
FT ACT_SITE 299
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040515"
FT VAR_SEQ 43..49
FT /note="EDKHLPM -> MIIGMFR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040516"
SQ SEQUENCE 344 AA; 37836 MW; 771C789CD1D2D2E6 CRC64;
MASSDFDGIL LGMGNPLLDV SAVVDQQFLD KYDIKLNNAI LAEDKHLPMY DEMSQKFNVE
YIAGGATQNS IKVAQWMLQV PGATSYMGSI GKDKYGEAMK KDATAAGVYV HYYEDEATPT
GTCGVCVLGG ERSLIANLSA ANCYKVEHLK KPENWALVEK AKFYYIAGFF LTVSPESIQL
VREHAAANNK VFTMNLSAPF ICEFFKDVQE KCLPYMDYIF GNETEARTFS RVHGWETDDV
EQIAIKMSQL PKASGTYKRT TVITQGADPV VVAEDGKVKK YPVIPLPKEK LVDTNGAGDA
FVGGFLSQLV HGKGIEECVR AGCYASNVVI QRSGCTYPEK PDFN
