UniProt: H2U9N9

Database: UniProt
Entry: H2U9N9_TAKRU

LinkDB:  H2U9N9_TAKRU 
Original site:  H2U9N9_TAKRU

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   H2U9N9_TAKRU            Unreviewed;       347 AA.
AC   H2U9N9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 58.
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=LOC101066176 {ECO:0000313|Ensembl:ENSTRUP00000033655.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000033655.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000033655.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000033655.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   AlphaFoldDB; H2U9N9; -.
DR   Ensembl; ENSTRUT00000033781.3; ENSTRUP00000033655.3; ENSTRUG00000013223.3.
DR   eggNOG; KOG2854; Eukaryota.
DR   GeneTree; ENSGT00390000014320; -.
DR   TreeFam; TF300745; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000005226; Chromosome 1.
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:UP000005226};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT   DOMAIN          31..341
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   347 AA;  38403 MW;  2210486E68FC5CAE CRC64;
     LKSVITNVEN TLFGMGNPLL DISAVVDKDF LDKFGLKPND QILAEDKHKA LFDEIVKKSN
     VEYHAGGSTQ NSVKIAQWMI QKPHKVATFF GCIGSDHFGE ILKKKAEEAH VDAHYYEQNV
     VPTGTCAACI TGDNRSLVAN LAAANCYKKE KHLDLDSNWE LAKKARVYYI AGFFLTVSPE
     SILKVAKHAS DNNKIFCMNL SAPFISQFFK QPLMEIMPYV DILFGNETEA ATFAKELGFE
     TDDIGEIAKK TQTLPKANTK RQRVVVFTQG KDDTVATVGR ATMFPVLDID QNDIVDTNGA
     GDAFVGGFLS ALVQEQVLEE CIRAGHYAAN IIIRRVGCTF PEKPDFH
//

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