UniProt: A0A316W754

Database: UniProt
Entry: A0A316W754_9BASI

LinkDB:  A0A316W754_9BASI 
Original site:  A0A316W754_9BASI

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

Download RDF

ID   A0A316W754_9BASI        Unreviewed;       341 AA.
AC   A0A316W754;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=IE81DRAFT_308826 {ECO:0000313|EMBL:PWN45679.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN45679.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN45679.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN45679.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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|ARBA:ARBA00001946,
CC         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   -!- 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   EMBL; KZ819354; PWN45679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316W754; -.
DR   STRING; 1522189.A0A316W754; -.
DR   InParanoid; A0A316W754; -.
DR   OrthoDB; 22683at2759; -.
DR   UniPathway; UPA00588; UER00659.
DR   Proteomes; UP000245783; Unassembled WGS sequence.
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};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU368116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}.
FT   DOMAIN          32..336
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   341 AA;  36439 MW;  501F47D581E9578B CRC64;
     MPGQYDLVAF GNPLLDMSIR DGEEVLKKYN LKSNDAILVE PQHESIYEYI VQNYKVQYVA
     GGAAQNTARA AQYILPEKST AYLGAVGNDD LAQQLRAAND REGLRSAYQV TPDHPTGSCA
     VVITGHDRSL VTRLGAAEKF DKAHLETPEV KQLTDNAKFF YMGGFFVTHG AEVGLIVAKK
     AKEIGVPFSL NLSAPFIPQF FTQQLDSIIP YASLVIGNES EAVAYAEAHK LGTTDLSAIA
     EAIANSPSEI SKPRTVVITH GSEPTILVEG GNKPRTIPTK QIPASEIVDT NGAGDAFAGG
     VVGALILGKS IDEAVQIGQK LGGMCIGQDG PRLKFPKEQV V
//

DBGET integrated database retrieval system