ID E2LY62_MONPE Unreviewed; 325 AA. AC E2LY62; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 24-JUL-2024, entry version 54. 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}; DE Flags: Fragment; GN ORFNames=MPER_12242 {ECO:0000313|EMBL:EEB89639.1}; OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom OS disease fungus) (Marasmius perniciosus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora. OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB89639.1, ECO:0000313|Proteomes:UP000000741}; RN [1] {ECO:0000313|EMBL:EEB89639.1, ECO:0000313|Proteomes:UP000000741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741}; RX PubMed=19019209; DOI=10.1186/1471-2164-9-548; RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P., RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O., RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B., RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P., RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J., RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.; RT "A genome survey of Moniliophthora perniciosa gives new insights into RT Witches' broom disease of cacao."; RL BMC Genomics 9:548-548(2008). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EEB89639.1}. 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; ABRE01017251; EEB89639.1; -; Genomic_DNA. DR AlphaFoldDB; E2LY62; -. DR STRING; 554373.E2LY62; -. DR KEGG; mpr:MPER_12242; -. DR HOGENOM; CLU_045832_1_0_1; -. DR InParanoid; E2LY62; -. DR OMA; APFIAQF; -. DR OrthoDB; 22683at2759; -. DR UniPathway; UPA00588; UER00659. DR Proteomes; UP000000741; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. 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:0006144; P:purine nucleobase metabolic process; IEA:TreeGrafter. 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|RuleBase:RU368116}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU368116}; KW Magnesium {ECO:0000256|RuleBase:RU368116}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU368116}; KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, KW ECO:0000256|RuleBase:RU368116}; KW Reference proteome {ECO:0000313|Proteomes:UP000000741}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368116}. FT DOMAIN 23..325 FT /note="Carbohydrate kinase PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT ACT_SITE 297 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR601805-1" FT NON_TER 325 FT /evidence="ECO:0000313|EMBL:EEB89639.1" SQ SEQUENCE 325 AA; 34215 MW; 55A6CCFF90A3DB20 CRC64; MSYSLFCIGN PLLDIQVTNG EKLLEKYGLK ANDAILAEEK HTPIYDEIVR EHKVTYVAGG AAQNAARGAA YILPPDSVVY TGCVGDDDLA EQLKAANKRE GLHQVYQVKK GEKTGACAVV ITGHNRSLVT TLRAAEKFEK SHLSSPEVAP LIDGAKAFYV EGYFLTHGTE AIVEVGQKAS AAGKVFALNF SAPFIPPLFG AQLQQVLPYT DIAICNESEA EAWASATGHA DPKDLAAVAK SIALLPKSNP SRPRIAVITH GAESTILVSS AEPDAPKVIP VHALKDSEIV DTNGAGDAFA GGFMGAFVAG KSLDECVEGG HKMGS //