KAD3_BOVIN
ID KAD3_BOVIN Reviewed; 227 AA.
AC P08760; Q29RI4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03169};
DE EC=2.7.4.10 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE Short=AK 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 alpha-like 1 {ECO:0000255|HAMAP-Rule:MF_03169};
GN Name=AK3 {ECO:0000255|HAMAP-Rule:MF_03169}; Synonyms=AK3L1;
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 [MRNA].
RX PubMed=2478555; DOI=10.1016/s0021-9258(19)47286-4;
RA Yamada M., Shahjahan M., Tanabe T., Kishi F., Nakazawa A.;
RT "Cloning and characterization of cDNA for mitochondrial GTP:AMP
RT phosphotransferase of bovine liver.";
RL J. Biol. Chem. 264:19192-19199(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-227, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=6088234; DOI=10.1111/j.1432-1033.1984.tb08376.x;
RA Wieland B., Tomasselli A.G., Noda L.H., Frank R., Schulz G.E.;
RT "The amino acid sequence of GTP:AMP phosphotransferase from beef-heart
RT mitochondria. Extensive homology with cytosolic adenylate kinase.";
RL Eur. J. Biochem. 143:331-339(1984).
RN [4]
RP PROTEIN SEQUENCE OF 2-227.
RC TISSUE=Heart;
RX PubMed=3013690; DOI=10.1016/0014-5793(86)80706-2;
RA Tomasselli A.G., Frank R., Schiltz E.;
RT "The complete primary structure of GTP:AMP phosphotransferase from beef
RT heart mitochondria.";
RL FEBS Lett. 202:303-308(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX PubMed=1748300; DOI=10.1016/0378-1119(91)90332-6;
RA Shahjahan M., Yamada M., Tanaka H., Nakazawa A.;
RT "Cloning and characterization of the gene encoding bovine mitochondrial
RT adenylate kinase isozyme 3.";
RL Gene 107:313-317(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2175649; DOI=10.1021/bi00487a022;
RA Diederichs K., Schulz G.E.;
RT "Three-dimensional structure of the complex between the mitochondrial
RT matrix adenylate kinase and its substrate AMP.";
RL Biochemistry 29:8138-8144(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH AMP.
RX PubMed=1994037; DOI=10.1016/0022-2836(91)90756-v;
RA Diederichs K., Schulz G.E.;
RT "The refined structure of the complex between adenylate kinase from beef
RT heart mitochondrial matrix and its substrate AMP at 1.85-A resolution.";
RL J. Mol. Biol. 217:541-549(1991).
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase
CC activities. {ECO:0000255|HAMAP-Rule:MF_03169}.
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_03169};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169,
CC ECO:0000269|PubMed:1994037}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03169, ECO:0000269|PubMed:6088234}.
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 binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent GTP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03169,
CC ECO:0000305|PubMed:1994037}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03169}.
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DR EMBL; M25757; AAA30705.1; -; mRNA.
DR EMBL; BC114157; AAI14158.1; -; mRNA.
DR EMBL; D10376; BAA01210.1; -; Genomic_DNA.
DR PIR; A34442; A34442.
DR RefSeq; NP_776662.1; NM_174237.2.
DR PDB; 2AK3; X-ray; 1.85 A; A/B=2-227.
DR PDBsum; 2AK3; -.
DR AlphaFoldDB; P08760; -.
DR SMR; P08760; -.
DR IntAct; P08760; 1.
DR STRING; 9913.ENSBTAP00000022789; -.
DR PaxDb; P08760; -.
DR PeptideAtlas; P08760; -.
DR PRIDE; P08760; -.
DR Ensembl; ENSBTAT00000022789; ENSBTAP00000022789; ENSBTAG00000017147.
DR GeneID; 281613; -.
DR KEGG; bta:281613; -.
DR CTD; 50808; -.
DR VEuPathDB; HostDB:ENSBTAG00000017147; -.
DR VGNC; VGNC:25772; AK3.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000156479; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR InParanoid; P08760; -.
DR OMA; MSPVIAW; -.
DR OrthoDB; 1004067at2759; -.
DR TreeFam; TF312916; -.
DR Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
DR SABIO-RK; P08760; -.
DR EvolutionaryTrace; P08760; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000017147; Expressed in neutrophil and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IBA:GO_Central.
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:0046039; P:GTP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046041; P:ITP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
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_03169; Adenylate_kinase_AK3; 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; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; GTP-binding; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:3013690"
FT CHAIN 2..227
FT /note="GTP:AMP phosphotransferase AK3, mitochondrial"
FT /id="PRO_0000158921"
FT REGION 37..66
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:1994037"
FT REGION 127..164
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:1994037"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 38
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:1994037"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 64..66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:1994037"
FT BINDING 91..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169,
FT ECO:0000269|PubMed:1994037"
FT BINDING 128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 137..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 161
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT MOD_RES 20
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 29
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 29
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 64
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 64
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 189
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 189
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP7"
FT CONFLICT 11
FT /note="Missing (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2AK3"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2AK3"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2AK3"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 166..189
FT /evidence="ECO:0007829|PDB:2AK3"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:2AK3"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:2AK3"
SQ SEQUENCE 227 AA; 25671 MW; 2C29AEF195FBFBFA CRC64;
MGASARLLRA AIMGAPGSGK GTVSSRITKH FELKHLSSGD LLRDNMLRGT EIGVLAKTFI
DQGKLIPDDV MTRLVLHELK NLTQYNWLLD GFPRTLPQAE ALDRAYQIDT VINLNVPFEV
IKQRLTARWI HPGSGRVYNI EFNPPKTMGI DDLTGEPLVQ REDDRPETVV KRLKAYEAQT
EPVLEYYRKK GVLETFSGTE TNKIWPHVYA FLQTKLPQRS QETSVTP
