KAD2_LACBS
ID KAD2_LACBS Reviewed; 256 AA.
AC B0D360;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=LACBIDRAFT_290988;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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 dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03168}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03168}.
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DR EMBL; DS547096; EDR11223.1; -; Genomic_DNA.
DR RefSeq; XP_001878524.1; XM_001878489.1.
DR AlphaFoldDB; B0D360; -.
DR SMR; B0D360; -.
DR STRING; 486041.B0D360; -.
DR EnsemblFungi; EDR11223; EDR11223; LACBIDRAFT_290988.
DR GeneID; 6073701; -.
DR KEGG; lbc:LACBIDRAFT_290988; -.
DR HOGENOM; CLU_032354_1_0_1; -.
DR InParanoid; B0D360; -.
DR OrthoDB; 1004067at2759; -.
DR Proteomes; UP000001194; 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:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR028587; AK2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 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_0000365676"
FT REGION 69..98
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT REGION 166..203
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 49..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 70
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 75
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 96..98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 125..128
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 132
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 176..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 211
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
SQ SEQUENCE 256 AA; 28177 MW; E994234C4EA4BCE5 CRC64;
MGASEELEYL KSLVSQLNGK IAAIEAKAKG SPSPTPAQQL RTILIGPPGA GKGTQAPKIR
DEFCVCHLAT GDMLREQVQQ KTPLGIEAKK IMDAGGLVSD DIMVGIIKDQ LENNKSCKNG
FVLDGFPRTI PQAQKLDGML AERKEKIDSV VQLLIDDQLL ISRITGRLVH PASGRSYHKE
FNPPKKRNVD DVTGEPLIQR SDDNVETLTK RLRTFHSQTG PVVDYYKVKG LWHGIDAAQS
PSVVWENLRS IFVSKK
