ADK_TOXGO
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 03-AUG-2022, entry version 105.
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}.
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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 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 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
