ID KAD2_MALGO Reviewed; 256 AA. AC A8PR17; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 02-SEP-2026, entry version 87. DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_03168}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03168}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_03168}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03168}; DE AltName: Full=Adenylate kinase cytosolic and mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03168}; GN Name=ADK1 {ECO:0000255|HAMAP-Rule:MF_03168}; ORFNames=MGL_0573; OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated OS fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia. OX NCBI_TaxID=425265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4612 / CBS 7966; RX PubMed=18000048; DOI=10.1073/pnas.0706756104; RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E., RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M., RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T., RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.; RT "Dandruff-associated Malassezia genomes reveal convergent and divergent RT virulence traits shared with plant and human fungal pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate CC group between ATP and AMP. Plays an important role in cellular energy CC homeostasis and in adenine nucleotide metabolism. Adenylate kinase CC activity is critical for regulation of the phosphate utilization and CC the AMP de novo biosynthesis pathways. {ECO:0000255|HAMAP- CC Rule:MF_03168}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03168}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03168}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP- CC Rule:MF_03168}. Mitochondrion intermembrane space {ECO:0000255|HAMAP- CC Rule:MF_03168}. Note=Predominantly mitochondrial. {ECO:0000255|HAMAP- CC Rule:MF_03168}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and disassembling the active CC center during each catalytic cycle provides an effective means to CC prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03168}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03168}. 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; AAYY01000001; EDP45584.1; -; Genomic_DNA. DR RefSeq; XP_001732798.1; XM_001732746.1. DR AlphaFoldDB; A8PR17; -. DR SMR; A8PR17; -. DR FunCoup; A8PR17; 459. DR STRING; 425265.A8PR17; -. DR GeneID; 5857104; -. DR KEGG; mgl:MGL_0573; -. DR VEuPathDB; FungiDB:MGL_0573; -. DR InParanoid; A8PR17; -. DR OMA; VYHEQTA; -. DR OrthoDB; 439792at2759; -. DR Proteomes; UP000008837; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:AMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01428; ADK; 1. DR FunFam; 3.40.50.300:FF:000106; Adenylate kinase mitochondrial; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03168; Adenylate_kinase_AK2; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR036193; ADK_active_lid_dom_sf. DR InterPro; IPR028587; AK2. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01351; adk; 1. DR NCBIfam; NF001380; PRK00279.1-2; 1. DR NCBIfam; NF001381; PRK00279.1-3; 1. DR NCBIfam; NF011100; PRK14527.1; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Mitochondrion; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..256 FT /note="Adenylate kinase" FT /id="PRO_0000365679" FT REGION 67..96 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT REGION 164..201 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 45..50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 68 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 73 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 94..96 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 123..126 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 130 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 165 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 174..175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 198 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 209 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" FT BINDING 237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168" SQ SEQUENCE 256 AA; 28329 MW; 5BE65EDBBCDAC511 CRC64; MSNPANTELS YLKSLVNELN EKIAVLEGKA PANQGVRMVL VGPPGAGKGT QAPKILERFQ NMVCHLATGD LLRQQVAMGT DLGKQAKKIM DQGALVSDEI MVGMIKDQLE TNRSCKKGFI LDGFPRTTPQ AEKLDQMLSD RKQKLDHVIE LQIPDELLIS RITGRLIHPG SGRSYHKIFS PPKQPMKDDI TGEPLVQRSD DNEEALRKRL ATYHKQTTAV TDYYKKHGIW SPIDATQSPN TVWQSISAIF NNGASA //