ID A0A286XMG8_CAVPO Unreviewed; 223 AA.
AC A0A286XMG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Adenylate kinase 4, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03170};
DE Short=AK 4 {ECO:0000256|HAMAP-Rule:MF_03170};
DE EC=2.7.4.10 {ECO:0000256|HAMAP-Rule:MF_03170};
DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03170};
DE AltName: Full=Adenylate kinase 3-like {ECO:0000256|HAMAP-Rule:MF_03170};
DE AltName: Full=GTP:AMP phosphotransferase AK4 {ECO:0000256|HAMAP-Rule:MF_03170};
GN Name=AK4 {ECO:0000256|HAMAP-Rule:MF_03170};
GN Synonyms=AK3L1 {ECO:0000256|HAMAP-Rule:MF_03170}, Ak4
GN {ECO:0000313|Ensembl:ENSCPOP00000026612.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000026612.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000026612.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000026612.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor,
CC but phosphorylates only AMP when using GTP as phosphate donor. Also
CC displays broad nucleoside diphosphate kinase activity.
CC {ECO:0000256|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:0000256|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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_03170};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03170}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_03170}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03170}.
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; AAKN02005146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003479162.1; XM_003479114.3.
DR AlphaFoldDB; A0A286XMG8; -.
DR STRING; 10141.ENSCPOP00000026612; -.
DR Ensembl; ENSCPOT00000032487.1; ENSCPOP00000026612.1; ENSCPOG00000037978.1.
DR GeneID; 100725972; -.
DR KEGG; cpoc:100725972; -.
DR CTD; 205; -.
DR VEuPathDB; HostDB:ENSCPOG00000037978; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000154568; -.
DR InParanoid; A0A286XMG8; -.
DR OMA; IKVENTM; -.
DR OrthoDB; 167111at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000037978; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046039; P:GTP 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_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 NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359:SF58; ADENYLATE KINASE 4 PSEUDOGENE 3-RELATED; 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_03170};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03170};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03170};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03170};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03170}; Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03170}.
FT DOMAIN 126..161
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT REGION 35..64
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT REGION 125..162
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 15..20
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 41
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 62..64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 89..92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 96
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 126
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 135..136
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 170
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
FT BINDING 199
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03170"
SQ SEQUENCE 223 AA; 25092 MW; B62006295D897BE2 CRC64;
MAARLLRAAV LGPPGSGKGT VSQRVAHSFG LQHLSSGRFL RDSLRAGSEV GHMARQYLEK
GLLVPDHVIT RLMMSELELR SDQHWLLDGF PRTIGQAEAL DRVCDLDLVI SLNIPFETLK
DRLSRRWVHL PSGRVYNLDF NPPLVPGVDD VTGEPLVQQE DDRPDAVAAR LRRYKDAAKP
VIELYRRRGV LHQFSGTETN KIWPYVHNLF SSKLAPLQSK DTN
//
