ADK_DICDI
ID ADK_DICDI Reviewed; 340 AA.
AC Q54MB5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenosine kinase;
DE Short=AK;
DE EC=2.7.1.20;
DE AltName: Full=Adenosine 5'-phosphotransferase;
GN Name=adk; ORFNames=DDB_G0286057;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC nucleoside analogs to monophosphate derivatives. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenosine: step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64407.2; -; Genomic_DNA.
DR RefSeq; XP_637919.2; XM_632827.2.
DR AlphaFoldDB; Q54MB5; -.
DR SMR; Q54MB5; -.
DR STRING; 44689.DDB0230174; -.
DR PaxDb; Q54MB5; -.
DR EnsemblProtists; EAL64407; EAL64407; DDB_G0286057.
DR GeneID; 8625430; -.
DR KEGG; ddi:DDB_G0286057; -.
DR dictyBase; DDB_G0286057; adk.
DR eggNOG; KOG2854; Eukaryota.
DR HOGENOM; CLU_045832_0_0_1; -.
DR InParanoid; Q54MB5; -.
DR OMA; APFIAQF; -.
DR PhylomeDB; Q54MB5; -.
DR Reactome; R-DDI-74217; Purine salvage.
DR UniPathway; UPA00588; UER00659.
DR PRO; PR:Q54MB5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004001; F:adenosine kinase activity; ISS:dictyBase.
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:0006144; P:purine nucleobase metabolic process; ISS:dictyBase.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR001805; Adenokinase.
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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..340
FT /note="Adenosine kinase"
FT /id="PRO_0000330873"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37095 MW; DBD310470ABE8450 CRC64;
MSNIKILCAG NPLLDLSTHV EMAILDKYEL KLGNAILAED KHLPLYGEIK SGKVEYIPGG
AAQNTSRVCQ WMLKDKQTVC YTGCVGTDEN ATILKTATES NGVVTKYQVD SSAPTGACAV
LINHKERSMV TNLGAANNFK IAHFQTEEMK AIVNSAQFFY LVGYFLTVSP DSAVHLGKHA
AENDKPFLYG LAAPFLIDFF FDKVSELLPY VDIVFANESE AATLGRKMNW GEDLTVIAEK
LAAWEKVNTK RTRTVVFTQG PDATLVFQNG VLTKYNPIKV ATEDILDLNA AGDSFCGGFL
AAYSNGQEIA KCVEAGHYAS WEIIRQNGAT VPASEPKIQF