ID   KAD2_SCHPO              Reviewed;         220 AA.
AC   P33075;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 170.
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; ORFNames=SPAC4G9.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8496185; DOI=10.1016/s0021-9258(18)82128-7;
RA   Konrad M.;
RT   "Molecular analysis of the essential gene for adenylate kinase from the
RT   fission yeast Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 268:11326-11334(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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, ECO:0000269|PubMed:8496185}.
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         ECO:0000269|PubMed:8496185};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03168}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC       Rule:MF_03168, ECO:0000269|PubMed:16823372}. Mitochondrion
CC       intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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}.
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DR   EMBL; X70363; CAA49826.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA93553.1; -; Genomic_DNA.
DR   PIR; A46718; S31338.
DR   RefSeq; NP_593685.1; NM_001019117.3.
DR   AlphaFoldDB; P33075; -.
DR   SMR; P33075; -.
DR   BioGRID; 279157; 1.
DR   FunCoup; P33075; 662.
DR   STRING; 284812.P33075; -.
DR   iPTMnet; P33075; -.
DR   PaxDb; 284812-P33075; -.
DR   GeneID; 2542704; -.
DR   KEGG; spo:2542704; -.
DR   PomBase; SPAC4G9.03; adk1.
DR   VEuPathDB; FungiDB:SPAC4G9.03; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   HOGENOM; CLU_032354_1_0_1; -.
DR   InParanoid; P33075; -.
DR   OMA; HYKVDAA; -.
DR   PhylomeDB; P33075; -.
DR   Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR   PRO; PR:P33075; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004017; F:AMP kinase activity; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006172; P:ADP biosynthetic process; IDA:PomBase.
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; IPR028587; AK2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01351; adk; 1.
DR   NCBIfam; NF001379; PRK00279.1-1; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..220
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158906"
FT   REGION          33..62
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   REGION          130..167
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         34
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         39
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         60..62
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         89..92
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         96
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         140..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         164
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         175
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
SQ   SEQUENCE   220 AA;  24375 MW;  F5335A025C971D78 CRC64;
     MAGMRLILVG PPGAGKGTQA PNIQKKYGIA HLATGDMLRS QVARQTELGK EAKKIMDQGG
     LVSDDIVTGM IKDEILNNPE CKNGFILDGF PRTVVQAEKL TALLDELKLD LNTVLELQVD
     DELLVRRITG RLVHPGSGRS YHLEFNPPKV PMKDDVTGEP LIQRSDDNAD ALRKRLVTYH
     EQTTPVVEFY KKKGKWAAVD AAQKPEQVWE QIVAILEKAE
//