ID KAD_MYCPN Reviewed; 215 AA. AC Q50299; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=MPN_185; GN ORFNames=MP646; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma RT pneumoniae comprising the dnaA region, the atp operon and a cluster of RT ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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. {ECO:0000255|HAMAP- CC Rule:MF_00235}. 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_00235}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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 dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. Some bacteria have evolved a zinc-coordinating structure CC that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00235}. 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; U34795; AAC43696.1; -; Genomic_DNA. DR EMBL; U00089; AAB96294.1; -; Genomic_DNA. DR PIR; S62823; S62823. DR RefSeq; NP_109873.1; NC_000912.1. DR RefSeq; WP_010874542.1; NZ_OU342337.1. DR AlphaFoldDB; Q50299; -. DR SMR; Q50299; -. DR IntAct; Q50299; 1. DR STRING; 272634.MPN_185; -. DR EnsemblBacteria; AAB96294; AAB96294; MPN_185. DR GeneID; 66609167; -. DR KEGG; mpn:MPN_185; -. DR PATRIC; fig|272634.6.peg.203; -. DR HOGENOM; CLU_032354_1_2_14; -. DR OrthoDB; 9805030at2; -. DR BioCyc; MPNE272634:G1GJ3-298-MONOMER; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 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; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01351; adk; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP 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; Metal-binding; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..215 FT /note="Adenylate kinase" FT /id="PRO_0000158804" FT REGION 34..63 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT REGION 128..165 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 14..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 35 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 40 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 61..63 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 91..94 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 98 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 138..139 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 162 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 173 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 211 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" SQ SEQUENCE 215 AA; 24255 MW; 3F4258BEFA24E8E8 CRC64; MVMENKFLFL GAPGVGKGTL AKQVANTTGL FHLSTGDIFR SVMQEQGALS QTLAHYMNQG LYVPDELTNQ TFWHFVTTHQ NELHKGFILD GYPRTLNQLE FLQSKLQLDQ VFHLKLSDPQ VLVARILNRL VCPSCGSVYN KQSKPPLKAN QCDRCHATLQ ARNDDTEAVI LKRLTLYEDT VKPLIEAFTK QGILTVIEAQ LPLEQQVNLV QQLVH //