ID A0A3P8Y3J5_ESOLU Unreviewed; 361 AA.
AC A0A3P8Y3J5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=ADK {ECO:0000313|Ensembl:ENSELUP00000011226.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000011226.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000011226.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000011226.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_019903083.1; XM_020047524.1.
DR AlphaFoldDB; A0A3P8Y3J5; -.
DR STRING; 8010.ENSELUP00000011226; -.
DR Ensembl; ENSELUT00000000824.2; ENSELUP00000011226.1; ENSELUG00000011679.2.
DR GeneID; 105029558; -.
DR KEGG; els:105029558; -.
DR GeneTree; ENSGT00390000014320; -.
DR OrthoDB; 22683at2759; -.
DR UniPathway; UPA00588; UER00659.
DR Proteomes; UP000265140; LG06.
DR Bgee; ENSELUG00000011679; Expressed in embryo and 14 other cell types or tissues.
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:SF6; 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:UP000265140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT DOMAIN 42..355
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 361 AA; 40003 MW; 9F5EC79F6602AC2B CRC64;
MSAVDETNVE KGRVADKALG ENALFGMGNP LLDISAVVDK DFLDKYGLKP NDQILAEDKH
KAMFDEIAKK SKVEYHAGGS TQNSVKIAQW MIQKPHKVAT FFGCIGSDRF GEILKQKAEE
AHVDAHYYQQ TDEPTGTCAA CITGDNRSLV ANLAAANCYD KEKHLDLESN WDLVEKARVY
YIAGFFLTVS PESILKVAKH ASENNKIFGL NLSAPFISQF FKDDMMEVMP YVDILFGNET
EAATFAREQG FEETGDIAAI ARWAQALPKV NQRRPRTVVF TQGRDDTVAT VGEKVTMFPV
LDIDQNDIVD TNGAGDAFVG GFLSELVQER PLEECIRAGH YAANVIIRRA GCTFPEKPNF
R
//
