KAD4_BOVIN
ID KAD4_BOVIN Reviewed; 223 AA.
AC Q0VCP1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Adenylate kinase 4, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03170};
DE Short=AK 4 {ECO:0000255|HAMAP-Rule:MF_03170};
DE EC=2.7.4.10 {ECO:0000255|HAMAP-Rule:MF_03170};
DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03170};
DE AltName: Full=Adenylate kinase 3-like {ECO:0000255|HAMAP-Rule:MF_03170};
DE AltName: Full=Adenylate kinase isoenzyme 4;
DE AltName: Full=GTP:AMP phosphotransferase AK4 {ECO:0000255|HAMAP-Rule:MF_03170};
GN Name=AK4 {ECO:0000255|HAMAP-Rule:MF_03170};
GN Synonyms=AK3L1 {ECO:0000255|HAMAP-Rule:MF_03170};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates
CC (By similarity). Efficiently phosphorylates AMP and dAMP using ATP as
CC phosphate donor, but phosphorylates only AMP when using GTP as
CC phosphate donor (By similarity). Also displays broad nucleoside
CC diphosphate kinase activity (By similarity). Plays a role in
CC controlling cellular ATP levels by regulating phosphorylation and
CC activation of the energy sensor protein kinase AMPK (By similarity).
CC Plays a protective role in the cellular response to oxidative stress
CC (By similarity). {ECO:0000250|UniProtKB:P27144, ECO:0000255|HAMAP-
CC Rule:MF_03170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-
CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03170};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with SLC25A5/ANT2 (By
CC similarity). {ECO:0000250|UniProtKB:P27144, ECO:0000255|HAMAP-
CC Rule:MF_03170}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03170}.
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 GTP/ATP binding. Assembling and dissambling the active
CC center during each catalytic cycle provides an effective means to
CC prevent GTP/ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03170}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03170}.
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DR EMBL; BC120077; AAI20078.1; -; mRNA.
DR RefSeq; NP_001071401.1; NM_001077933.2.
DR RefSeq; XP_005204514.1; XM_005204457.3.
DR RefSeq; XP_010801745.1; XM_010803443.2.
DR AlphaFoldDB; Q0VCP1; -.
DR SMR; Q0VCP1; -.
DR STRING; 9913.ENSBTAP00000040941; -.
DR PaxDb; Q0VCP1; -.
DR PRIDE; Q0VCP1; -.
DR Ensembl; ENSBTAT00000043366; ENSBTAP00000040941; ENSBTAG00000030674.
DR GeneID; 517063; -.
DR KEGG; bta:517063; -.
DR CTD; 205; -.
DR VEuPathDB; HostDB:ENSBTAG00000030674; -.
DR VGNC; VGNC:25773; AK4.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000154568; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR InParanoid; Q0VCP1; -.
DR OMA; IKVENTM; -.
DR OrthoDB; 1004067at2759; -.
DR TreeFam; TF312916; -.
DR Reactome; R-BTA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; Q0VCP1; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000030674; Expressed in metanephros cortex and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:2001169; P:regulation of ATP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03169; Adenylate_kinase_AK3; 1.
DR HAMAP; MF_03170; Adenylate_kinase_AK4; 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; IPR028586; AK3/Ak4_mitochondrial.
DR InterPro; IPR028585; AK4_mitochondrial.
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 SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; GTP-binding; Kinase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..223
FT /note="Adenylate kinase 4, mitochondrial"
FT /id="PRO_0000262883"
FT REGION 35..64
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT REGION 125..162
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 15..20
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 41
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 62..64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 89..92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 96
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 126
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 135..136
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 170
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT BINDING 199
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03170"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
FT MOD_RES 179
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
FT MOD_RES 179
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
FT MOD_RES 186
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
FT MOD_RES 186
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR9"
SQ SEQUENCE 223 AA; 25348 MW; 4CCA67455279F3AF CRC64;
MASKLLRAVI LGPPGSGKGT VCQRIAQNFG LQHLSSGHFL RENIKANTEV GDMAKQYIEK
GLLVPDHVIT RLMLLELENR RGEHWLLDGF PRTLVQAEAL DRLCDLDLVI TLNIPFETLK
DRLSRRWIHP PSGRVYNLDF NPPHVHGMDD VTGEPLVQQE DDKPEAVAAR LRQYKDVAKP
VIELYKSRGV LHQFSGTETN KIWPYVYTLF SNKITPVQSK EAY
