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Database: UniProt
Entry: A0A0P1BR26_9BASI
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ID   A0A0P1BR26_9BASI        Unreviewed;       291 AA.
AC   A0A0P1BR26;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
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};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH19364.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH19364.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000389; CEH19364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BR26; -.
DR   STRING; 401625.A0A0P1BR26; -.
DR   OrthoDB; 167111at2759; -.
DR   Proteomes; UP000054845; 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; IPR036193; ADK_active_lid_dom_sf.
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; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
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:UP000054845};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03168}.
FT   DOMAIN          197..232
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..128
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   REGION          196..233
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   REGION          202..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         77..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         100
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         105
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         126..128
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         155..158
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         162
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         206..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         230
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         241
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03168"
SQ   SEQUENCE   291 AA;  31430 MW;  7509C9333AF7C377 CRC64;
     MATSTTANTP AAPDPAVFGG KKSDQSGNSS AELAYLKSLV SQLNDKIKSI ESTAGSVLGS
     LTSSNEGVRM ILIGPPGAGK GTQAPKILQR FSGSICHLAT GDMLREQVAQ GTDLGKKAKE
     IMNQGGLVPD EIMVGMIENQ LEQNQQCANG FILDGFPRTT PQAEKLDDML KSKQQKLDHA
     VELKINDQLL ISRITGRLVH PPSGRSYHKE FHPPKKPMTD DVTGEPLIQR SDDNAETLKK
     RLGTYHAQTA AVTDYYRKQG IWSAVDAAQS QQVVWSSISA IFDQKAKSAQ K
//
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