ID   KAD_ENTHI               Reviewed;         193 AA.
AC   O96907;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 79.
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;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RA   Sanchez L.B., Muller M.;
RT   "Nucleotide kinases from Entamoeba histolytica.";
RL   Submitted (JAN-1997) 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; U83615; AAD00546.1; -; Genomic_DNA.
DR   AlphaFoldDB; O96907; -.
DR   SMR; O96907; -.
DR   STRING; 5759.rna_EHI_135470-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_093160; -.
DR   VEuPathDB; AmoebaDB:EHI7A_057040; -.
DR   VEuPathDB; AmoebaDB:EHI8A_060050; -.
DR   VEuPathDB; AmoebaDB:EHI_135470; -.
DR   VEuPathDB; AmoebaDB:KM1_112550; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   OMA; KLDMVIN; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
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   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..193
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158935"
FT   REGION          34..63
FT                   /note="NMP"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   REGION          127..137
FT                   /note="LID"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         35
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         40
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         61..63
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         88..91
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         95
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         134
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
SQ   SEQUENCE   193 AA;  21102 MW;  F13157678200182B CRC64;
     MAKVFLIMLG GPGAGKGTQC ANIEKHLNSS AHISTGDLLR AEIKNKTEIG LKVEDIIRNG
     QLVSDEIICN MVNNFIAKNE KEVIVFDGYP RAVSQLEALL KEATAETKIC VINLEIPDEI
     LIQRIVSRGK TSGRADDNTE AAAKRLAVYH AQHDEMIKAI KAKNLPYFVV DHLGGPDEVF
     NEIKGVFANV GLH