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Q9TVW2 (ADK_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine kinase

Short name=AK
EC=2.7.1.20
Alternative name(s):
Adenosine 5'-phosphotransferase
Gene names
Name:AK
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. It is a key purine metabolic enzyme in the opportunistic parasitic protozoan toxoplasma gondii as it cannot synthesize purines de novo.

Catalytic activity

ATP + adenosine = ADP + AMP.

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.

Sequence similarities

Belongs to the carbohydrate kinase PfkB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Adenosine kinase
PRO_0000080056

Sites

Active site3181
Metal binding1851Magnesium; via carbonyl oxygen
Metal binding1881Magnesium; via carbonyl oxygen
Metal binding1911Magnesium; via carbonyl oxygen

Secondary structure

................................................................... 363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9TVW2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6C621C7D5A56739C

FASTA36338,356
        10         20         30         40         50         60 
MAVDSSNSAT GPMRVFAIGN PILDLVAEVP SSFLDEFFLK RGDATLATPE QMRIYSTLDQ 

        70         80         90        100        110        120 
FNPTSLPGGS ALNSVRVVQK LLRKPGSAGY MGAIGDDPRG QVLKELCDKE GLATRFMVAP 

       130        140        150        160        170        180 
GQSTGVCAVL INEKERTLCT HLGACGSFRL PEDWTTFASG ALIFYATAYT LTATPKNALE 

       190        200        210        220        230        240 
VAGYAHGIPN AIFTLNLSAP FCVELYKDAM QSLLLHTNIL FGNEEEFAHL AKVHNLVAAE 

       250        260        270        280        290        300 
KTALSTANKE HAVEVCTGAL RLLTAGQNTG ATKLVVMTRG HNPVIAAEQT ADGTVVVHEV 

       310        320        330        340        350        360 
GVPVVAAEKI VDTNGAGDAF VGGFLYALSQ GKTVKQCIMC GNACAQDVIQ HVGFSLSFTS 


LPC 

« Hide

References

[1]"Insertional tagging of at least two loci associated with resistance to adenine arabinoside in Toxoplasma gondii, and cloning of the adenosine kinase locus."
Sullivan W.J. Jr., Chiang C.-W., Wilson C.M., Naguib F.N.M., el Kouni M.H., Donald R.G.K., Roos D.S.
Mol. Biochem. Parasitol. 103:1-14(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: RH.
[2]"Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding."
Schumacher M.A., Scott D.M., Mathews I.I., Ealick S.E., Roos D.S., Ullman B., Brennan R.G.
J. Mol. Biol. 296:549-567(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
[3]"Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution."
Cook W.J., DeLucas L.J., Chattopadhyay D.
Protein Sci. 9:704-712(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF128274 Genomic DNA. Translation: AAF01261.1.
AF128275 mRNA. Translation: AAF01262.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DGMX-ray1.80A1-363[»]
1LIIX-ray1.73A1-363[»]
1LIJX-ray1.86A1-363[»]
1LIKX-ray2.55A1-363[»]
1LIOX-ray2.50A1-363[»]
2A9YX-ray1.35A1-363[»]
2A9ZX-ray1.35A1-363[»]
2AA0X-ray1.75A1-363[»]
2AB8X-ray1.75A1-363[»]
2ABSX-ray1.10A1-363[»]
ProteinModelPortalQ9TVW2.
SMRQ9TVW2. Positions 10-359.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9TVW2.
ChEMBLCHEMBL2982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00588; UER00659.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
InterProIPR001805. Adenokinase.
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERPTHR10584:SF24. PTHR10584:SF24. 1 hit.
PfamPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSPR00989. ADENOKINASE.
SUPFAMSSF53613. SSF53613. 1 hit.
PROSITEPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9TVW2.

Entry information

Entry nameADK_TOXGO
AccessionPrimary (citable) accession number: Q9TVW2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways