KAD2_CRYNJ
ID KAD2_CRYNJ Reviewed; 269 AA.
AC P0CO42; Q55KH8; Q5K931;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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}; OrderedLocusNames=CNK03420;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017351; AAW46409.1; -; Genomic_DNA.
DR RefSeq; XP_567926.1; XM_567926.1.
DR AlphaFoldDB; P0CO42; -.
DR SMR; P0CO42; -.
DR STRING; 5207.AAW46409; -.
DR PaxDb; P0CO42; -.
DR PRIDE; P0CO42; -.
DR EnsemblFungi; AAW46409; AAW46409; CNK03420.
DR GeneID; 3254609; -.
DR KEGG; cne:CNK03420; -.
DR VEuPathDB; FungiDB:CNK03420; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_1_0_1; -.
DR InParanoid; P0CO42; -.
DR OMA; FHNRMRV; -.
DR OrthoDB; 1004067at2759; -.
DR Proteomes; UP000002149; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
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..269
FT /note="Adenylate kinase"
FT /id="PRO_0000365672"
FT REGION 81..110
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT REGION 178..215
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 61..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 82
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 108..110
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 137..140
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 144
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 188..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 212
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 223
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
SQ SEQUENCE 269 AA; 29289 MW; AFF61FED70AE3F8D CRC64;
MSGNSEVEYL KSLVSQLQDK IHHLEKSTST SVSNTISSVT SALSPSSSIK PPRMVLIGPP
GAGKGTQAPN ISSKYCICHL ATGDMLREQV ARQTELGKAA KQIMDQGGLV SDEIMVGMIK
QELEKNAECK NGFILDGFPR TVPQASKLDA MLAERKQAID HAIELKIPDV LLISRITGRL
VHPASGRSYH KEFNPPKKPM TDDITGEPLI QRSDDNVGTL RKRLDTYHAQ TGPVVDYYKG
TGVWTPVDAA QSPKLVWASI SSILESKKN
