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Database: UniProt
Entry: A0A1V6PUC0_9EURO
LinkDB: A0A1V6PUC0_9EURO
Original site: A0A1V6PUC0_9EURO 
ID   A0A1V6PUC0_9EURO        Unreviewed;       257 AA.
AC   A0A1V6PUC0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=PENANT_c034G06702 {ECO:0000313|EMBL:OQD80570.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD80570.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD80570.1}.
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DR   EMBL; MDYN01000034; OQD80570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PUC0; -.
DR   STRING; 416450.A0A1V6PUC0; -.
DR   OrthoDB; 167111at2759; -.
DR   Proteomes; UP000191672; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03168}.
FT   DOMAIN          170..205
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   REGION          72..101
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   REGION          169..206
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         52..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         73
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         78
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         99..101
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         128..131
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         135
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         179..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         203
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         214
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
SQ   SEQUENCE   257 AA;  28386 MW;  712A89F3E8CADF99 CRC64;
     MAPITDEVVS GLKDTINKLE AKVSELEGRL SNGGQPKSVA EQMRIILMGP PGAGKGTQAP
     NLKEKYCACH LATGDMLRSQ VAKKTDLGKE AKKIMDQGGL VSDEIMVNMI KSELDNNIEC
     KNGFILDGFP RTVAQAERLD DMLSDRKQKL QHAVELQIDD SLLVARITGR LVHPASGRSY
     HKIFNPPKDD MKDDISGEPL IQRSDDNADT LTKRLATYHA QTTPVVDYYK KTGIWRGIDA
     SQEPGQVWKS ILGVFRQ
//
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