KAD2_PONAB
ID KAD2_PONAB Reviewed; 239 AA.
AC Q5REI7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Adenylate kinase 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168};
DE Short=AK 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP-AMP transphosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03168};
GN Name=AK2 {ECO:0000255|HAMAP-Rule:MF_03168};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. Plays a key role in
CC hematopoiesis. {ECO:0000255|HAMAP-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: Mitochondrion intermembrane space
CC {ECO:0000255|HAMAP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857541; CAH89820.1; -; mRNA.
DR RefSeq; NP_001124843.1; NM_001131371.1.
DR AlphaFoldDB; Q5REI7; -.
DR SMR; Q5REI7; -.
DR STRING; 9601.ENSPPYP00000001820; -.
DR Ensembl; ENSPPYT00000051061; ENSPPYP00000034629; ENSPPYG00000037048.
DR GeneID; 100171703; -.
DR KEGG; pon:100171703; -.
DR CTD; 204; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000154576; -.
DR HOGENOM; CLU_032354_1_0_1; -.
DR InParanoid; Q5REI7; -.
DR OrthoDB; 1004067at2759; -.
DR TreeFam; TF300896; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0097226; C:sperm mitochondrial sheath; IEA:Ensembl.
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; -; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Disulfide bond; Kinase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..239
FT /note="Adenylate kinase 2, mitochondrial"
FT /id="PRO_0000158919"
FT REGION 45..74
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT REGION 141..178
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT REGION 150..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 46
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 72..74
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 100..103
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 151..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 186
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 62
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT DISULFID 42..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
SQ SEQUENCE 239 AA; 26478 MW; 86FA94F9EE33629F CRC64;
MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML RAMVASGSEL
GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE
KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE
KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI
