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Database: UniProt
Entry: A0A075A1K6_9TREM
LinkDB: A0A075A1K6_9TREM
Original site: A0A075A1K6_9TREM 
ID   A0A075A1K6_9TREM        Unreviewed;       347 AA.
AC   A0A075A1K6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Adenosine kinase {ECO:0000256|ARBA:ARBA00012119, ECO:0000256|RuleBase:RU368116};
DE            Short=AK {ECO:0000256|RuleBase:RU368116};
DE            EC=2.7.1.20 {ECO:0000256|ARBA:ARBA00012119, ECO:0000256|RuleBase:RU368116};
DE   AltName: Full=Adenosine 5'-phosphotransferase {ECO:0000256|RuleBase:RU368116};
GN   ORFNames=T265_10359 {ECO:0000313|EMBL:KER21274.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER21274.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER21274.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP dependent phosphorylation of adenosine and other related
CC       nucleoside analogs to monophosphate derivatives.
CC       {ECO:0000256|RuleBase:RU368116}.
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         Evidence={ECO:0000256|RuleBase:RU368116};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU368116};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|RuleBase:RU368116};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenosine: step 1/1. {ECO:0000256|ARBA:ARBA00004801,
CC       ECO:0000256|RuleBase:RU368116}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU368116}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368116}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|RuleBase:RU368116}.
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DR   EMBL; KL596979; KER21274.1; -; Genomic_DNA.
DR   RefSeq; XP_009174970.1; XM_009176706.1.
DR   AlphaFoldDB; A0A075A1K6; -.
DR   STRING; 6198.A0A075A1K6; -.
DR   GeneID; 20324527; -.
DR   KEGG; ovi:T265_10359; -.
DR   CTD; 20324527; -.
DR   OrthoDB; 22683at2759; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004001; F:adenosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368116};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU368116};
KW   Magnesium {ECO:0000256|RuleBase:RU368116};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU368116}; Nucleus {ECO:0000256|RuleBase:RU368116};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU368116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT   DOMAIN          43..338
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   347 AA;  37958 MW;  BE4CBF2C54EC84DC CRC64;
     MKAGEVRILG LGNPLLDLMV KAEGDIYDRY KLKKDDALLA AEHHLPLFDE VAQNPTTRYA
     AGGATLNTMR MIKWILQEPH KCTFIGCIAA DEAGERLRNE CEKLQLMTHF EVTQGEAATG
     KCAVLLHGKC RSMVTHVGAA ANLTMDHILK PDTWHSIESA SAYYVAGFAT GTCFEGVLEV
     AKHARSRGKL FAFNLSSPAI LQHFKDQMDA IFPYVDILFG NSSEAQAYAE LHELSGQALE
     NIVLKLASIT SAKSENPRKR IVLITQGQDP VLLGESGGKE VMHFPVYPVS DEDIVDTNGA
     GDAFVAGFLA EYLRGSSIEK AVEEAINAAR YIIQRNGFTL GPRDQYA
//
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