ID A0A183WAP9_TRIRE Unreviewed; 323 AA.
AC A0A183WAP9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=TRE_LOCUS9203 {ECO:0000313|EMBL:VDQ05083.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000981501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0000981501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ05083.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UZAO01063040; VDQ05083.1; -; Genomic_DNA.
DR STRING; 157069.A0A183WAP9; -.
DR WBParaSite; TRE_0000981501-mRNA-1; TRE_0000981501-mRNA-1; TRE_0000981501.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000280995; 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:UP000280995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT DOMAIN 30..315
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 323 AA; 35984 MW; 7AC53F72EB8EA044 CRC64;
MDEVSEGYLF GMGNPLLDML WKADEDTYKS YGLNVDDAIL AEDKHMSIYT ELMKKPDVKY
VAGGSTLNTV KMIQWILRKP LSCSFVGCIG ADRMGDRIEA ECRELGLETE FQTTKKPLET
GKVAVLINGK NRSIVTYLGA ACDLTVQHVK QPRVWSLVER ARVFYIAVSL TMAKHATTFG
KLFCFNLSAP FISKFYTKEV DEMISHAAHN LPNITVYAVA QHIASRPLAT RMKRNRLVII
TRGKHPVVYV NSLDMKVHEF PVKTVESCQI VDTNGAGDAF AAGFIAEHIL SRPIVSSLES
AVKAATYIIQ RSGFTLDARD SFM
//
