ID W0T6D1_KLUMD Unreviewed; 227 AA.
AC W0T6D1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_03168};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate kinase cytosolic and mitochondrial {ECO:0000256|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03168};
GN Name=ADK1 {ECO:0000256|HAMAP-Rule:MF_03168,
GN ECO:0000313|EMBL:BAO38623.1};
GN ORFNames=KLMA_20165 {ECO:0000313|EMBL:BAO38623.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO38623.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO38623.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_03168};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|HAMAP-
CC Rule:MF_03168}. Mitochondrion intermembrane space {ECO:0000256|HAMAP-
CC Rule:MF_03168}. Note=Predominantly mitochondrial. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03168}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03168}.
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DR EMBL; AP012214; BAO38623.1; -; Genomic_DNA.
DR AlphaFoldDB; W0T6D1; -.
DR VEuPathDB; FungiDB:KLMA_20165; -.
DR OrthoDB; 167111at2759; -.
DR Proteomes; UP000065495; Chromosome 2.
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: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 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 PANTHER; PTHR23359:SF234; ADENYLATE KINASE 2, MITOCHONDRIAL; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03168};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03168};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03168};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03168};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03168}.
FT DOMAIN 139..174
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT REGION 41..70
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT REGION 138..175
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 21..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 47
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 68..70
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 97..100
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 104
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 148..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 183
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
SQ SEQUENCE 227 AA; 25199 MW; 0D29964E288288DB CRC64;
MTQDLSHVPE SIRMVLIGPP GAGKGTQAPN LKEKFCACHL ATGDMLRSQV AKQTPLGIEA
KKIMDDGKLV SDEIMINMIK DELSNNPECK KGFILDGFPR TIPQAEKLDE MLADQGRPLE
KAVELKIDDE LLVARITGRL VHPASGRSYH KLFNPPKVEM KDDLTGEPLV QRSDDNVEAL
KKRLSSYHKQ TEPIVDFYKK TGIWAGVDAS QPPKTVWSDI LKCLGKN
//
