ID ADK_TOXGO Reviewed; 363 AA. AC Q9TVW2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 22-FEB-2023, entry version 107. DE RecName: Full=Adenosine kinase; DE Short=AK; DE EC=2.7.1.20; DE AltName: Full=Adenosine 5'-phosphotransferase; GN Name=AK; OS Toxoplasma gondii. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma. OX NCBI_TaxID=5811; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=RH; RX PubMed=10514076; DOI=10.1016/s0166-6851(99)00114-0; RA Sullivan W.J. Jr., Chiang C.-W., Wilson C.M., Naguib F.N.M., el Kouni M.H., RA Donald R.G.K., Roos D.S.; RT "Insertional tagging of at least two loci associated with resistance to RT adenine arabinoside in Toxoplasma gondii, and cloning of the adenosine RT kinase locus."; RL Mol. Biochem. Parasitol. 103:1-14(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS). RX PubMed=10669608; DOI=10.1006/jmbi.1999.3474; RA Schumacher M.A., Scott D.M., Mathews I.I., Ealick S.E., Roos D.S., RA Ullman B., Brennan R.G.; RT "Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel RT catalytic mechanism and prodrug binding."; RL J. Mol. Biol. 296:549-567(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=10794412; DOI=10.1110/ps.9.4.704; RA Cook W.J., DeLucas L.J., Chattopadhyay D.; RT "Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A RT resolution."; RL Protein Sci. 9:704-712(2000). CC -!- FUNCTION: ATP-dependent phosphorylation of adenosine and other related CC nucleoside analogs to monophosphate derivatives. It is a key purine CC metabolic enzyme in the opportunistic parasitic protozoan toxoplasma CC gondii as it cannot synthesize purines de novo. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from adenosine: step 1/1. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF128274; AAF01261.1; -; Genomic_DNA. DR EMBL; AF128275; AAF01262.1; -; mRNA. DR PDB; 1DGM; X-ray; 1.80 A; A=1-363. DR PDB; 1LII; X-ray; 1.73 A; A=1-363. DR PDB; 1LIJ; X-ray; 1.86 A; A=1-363. DR PDB; 1LIK; X-ray; 2.55 A; A=1-363. DR PDB; 1LIO; X-ray; 2.50 A; A=1-363. DR PDB; 2A9Y; X-ray; 1.35 A; A=1-363. DR PDB; 2A9Z; X-ray; 1.35 A; A=1-363. DR PDB; 2AA0; X-ray; 1.75 A; A=1-363. DR PDB; 2AB8; X-ray; 1.75 A; A=1-363. DR PDB; 2ABS; X-ray; 1.10 A; A=1-363. DR PDBsum; 1DGM; -. DR PDBsum; 1LII; -. DR PDBsum; 1LIJ; -. DR PDBsum; 1LIK; -. DR PDBsum; 1LIO; -. DR PDBsum; 2A9Y; -. DR PDBsum; 2A9Z; -. DR PDBsum; 2AA0; -. DR PDBsum; 2AB8; -. DR PDBsum; 2ABS; -. DR AlphaFoldDB; Q9TVW2; -. DR SMR; Q9TVW2; -. DR BindingDB; Q9TVW2; -. DR ChEMBL; CHEMBL2982; -. DR DrugCentral; Q9TVW2; -. DR EnsemblProtists; TGME49_250880-t26_1; TGME49_250880-t26_1; TGME49_250880. DR VEuPathDB; ToxoDB:TGARI_250880; -. DR VEuPathDB; ToxoDB:TGCAST_250880; -. DR VEuPathDB; ToxoDB:TGCOUG_250880; -. DR VEuPathDB; ToxoDB:TGDOM2_250880; -. DR VEuPathDB; ToxoDB:TGFOU_250880; -. DR VEuPathDB; ToxoDB:TGGT1_250880; -. DR VEuPathDB; ToxoDB:TGMAS_250880; -. DR VEuPathDB; ToxoDB:TGME49_250880; -. DR VEuPathDB; ToxoDB:TGP89_250880; -. DR VEuPathDB; ToxoDB:TGPRC2_250880; -. DR VEuPathDB; ToxoDB:TGRH88_064140; -. DR VEuPathDB; ToxoDB:TGRUB_250880; -. DR VEuPathDB; ToxoDB:TGVAND_250880; -. DR VEuPathDB; ToxoDB:TGVEG_250880; -. DR BRENDA; 2.7.1.20; 6411. DR UniPathway; UPA00588; UER00659. DR EvolutionaryTrace; Q9TVW2; -. DR GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR CDD; cd01168; adenosine_kinase; 1. DR Gene3D; 3.30.1110.10; -; 1. 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; ADENOSINE KINASE; 1. DR PANTHER; PTHR45769:SF3; ADENOSINE KINASE; 1. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00989; ADENOKINASE. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine salvage; Transferase. FT CHAIN 1..363 FT /note="Adenosine kinase" FT /id="PRO_0000080056" FT ACT_SITE 318 FT BINDING 185 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 188 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 22..28 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 31..36 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 49..56 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 87..94 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 98..110 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 125..132 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 143..147 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 154..157 FT /evidence="ECO:0007829|PDB:2ABS" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 168..171 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 176..186 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1LIO" FT STRAND 192..196 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 200..205 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 224..234 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:2A9Y" FT HELIX 249..264 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:2ABS" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:1LIO" FT STRAND 295..300 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 316..329 FT /evidence="ECO:0007829|PDB:2ABS" FT HELIX 334..349 FT /evidence="ECO:0007829|PDB:2ABS" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:2ABS" SQ SEQUENCE 363 AA; 38356 MW; 6C621C7D5A56739C CRC64; MAVDSSNSAT GPMRVFAIGN PILDLVAEVP SSFLDEFFLK RGDATLATPE QMRIYSTLDQ FNPTSLPGGS ALNSVRVVQK LLRKPGSAGY MGAIGDDPRG QVLKELCDKE GLATRFMVAP GQSTGVCAVL INEKERTLCT HLGACGSFRL PEDWTTFASG ALIFYATAYT LTATPKNALE VAGYAHGIPN AIFTLNLSAP FCVELYKDAM QSLLLHTNIL FGNEEEFAHL AKVHNLVAAE KTALSTANKE HAVEVCTGAL RLLTAGQNTG ATKLVVMTRG HNPVIAAEQT ADGTVVVHEV GVPVVAAEKI VDTNGAGDAF VGGFLYALSQ GKTVKQCIMC GNACAQDVIQ HVGFSLSFTS LPC //