ID   KAD1_SOLTU              Reviewed;         288 AA.
AC   Q8HSW1;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Adenylate kinase;
DE            Short=AK;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate monophosphate kinase;
GN   Name=ADK;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Regierer B., Fernie A.R., Springer F., Perez A., Willmitzer L.,
RA   Geigenberger P., Kossmann J.;
RT   "StpADK (adenylate kinase, plastidial).";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Plays an important role in cellular energy
CC       homeostasis and in adenine nucleotide metabolism.
CC       {ECO:0000250|UniProtKB:P69441}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000250|UniProtKB:P69441};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69441}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR   EMBL; AF411937; AAN76661.1; -; mRNA.
DR   AlphaFoldDB; Q8HSW1; -.
DR   SMR; Q8HSW1; -.
DR   STRING; 4113.PGSC0003DMT400071737; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   InParanoid; Q8HSW1; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q8HSW1; baseline.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048364; P:root development; IEA:EnsemblPlants.
DR   GO; GO:0048367; P:shoot system development; IEA:EnsemblPlants.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..288
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000016556"
FT   REGION          85..114
FT                   /note="NMP"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   REGION          178..226
FT                   /note="LID"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         65..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         86
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         91
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         112..114
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         142..145
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         149
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         223
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         234
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
SQ   SEQUENCE   288 AA;  31433 MW;  1A8BE3898C5B7160 CRC64;
     MAAMIRLFRS SSSSSSNSIS LISRSLSTAA ASETVKSQSY PHNPHSTSVD PKAKTVQWVF
     LGCPGVGKGT YASRLSTLLG VPHIATGDLV RDELKSSGPL SKQLAEIVNQ GKLVSDEIIL
     NLLSKRLESG EAKGEAGFIL DGFPRTVRQA EILTEVTDID LVVNLKLPER VLVEKCLGRR
     ICSECGKNFN VASIDVAGEN GAPRISMARL NPPFTVCFKL ITRADDTEAI VKERLSIYWD
     KSQPVEDFYR SQGKLLEFDL PGGIPESWPK LLEVLNLDEQ EYKLSPAA