ID A0A226NGL3_CALSU Unreviewed; 223 AA.
AC A0A226NGL3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
GN ORFNames=ASZ78_013891 {ECO:0000313|EMBL:OXB66632.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB66632.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB66632.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB66632.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB66632.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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 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 -!- 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:OXB66632.1}.
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DR EMBL; MCFN01000058; OXB66632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226NGL3; -.
DR STRING; 9009.A0A226NGL3; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
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:UP000198323};
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; 25125 MW; BCF5F33114E17FC5 CRC64;
MASKALRAVV LGPPGSGKGT VCERIARSFG LQHLSSGQFL RESLRGGGEV GTLAKQYLER
GLLVPDHVIT RVMMMELEKR RAEHWLLDGF PRTLGQAEAL DRICELDVVI SLHIPFETLK
DRLSARWIHP ASGRVYNMEF NPPHVHGIDD VTGEPLVQRE DDRPEAVTAR LRKYKDAAKP
VIELYKSRGI LHSFSGTETN KIWPYVYALL SNKIPPLRSE EEH
//
