ID   KAD_GIAIN               Reviewed;         248 AA.
AC   P49982;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30957 / WB;
RX   PubMed=7477113; DOI=10.1016/0166-6851(95)00067-b;
RA   Rozario C., Mueller M.;
RT   "Primary structure of a putative adenylate kinase gene of Giardia
RT   lamblia.";
RL   Mol. Biochem. Parasitol. 71:279-283(1995).
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; U19901; AAC46846.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49982; -.
DR   SMR; P49982; -.
DR   PRIDE; P49982; -.
DR   VEuPathDB; GiardiaDB:DHA2_28234; -.
DR   VEuPathDB; GiardiaDB:GL50581_2190; -.
DR   VEuPathDB; GiardiaDB:GL50803_0028234; -.
DR   eggNOG; KOG3078; Eukaryota.
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; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..248
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158936"
FT   REGION          57..86
FT                   /note="NMP"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   REGION          149..181
FT                   /note="LID"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         37..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         63
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         84..86
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         111..114
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         118
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         178
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         189
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
SQ   SEQUENCE   248 AA;  27965 MW;  2DE5DD697CE1DC0F CRC64;
     MQSLIKYQPK SPLKYLSSYF GDRKKNLFKL VLLGAPGAGK GTQAKHLVSK YSLKHISPGN
     LLREEMNRNS PITAQIKDYV SKGQLVPDSI VIKLIENHIA TIGDSNWLLD GFPRSESQAA
     ALRASPDLFP THIVELKVDQ EAVVQRLGGR RFDPITGNTY HIIYDPPPPD IADRVVVRTD
     DREDVIRERF RVYAENKDLV DKVFNHSVVS INCEGQTIDE VSLQLDRVLS MPSTIHPSII
     MPERNKKQ