KAD3_YEAST
ID KAD3_YEAST Reviewed; 225 AA.
AC P26364; D3DM78;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GTP:AMP phosphotransferase, 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};
GN Name=ADK2 {ECO:0000255|HAMAP-Rule:MF_03169}; Synonyms=AKY3, PAK3;
GN OrderedLocusNames=YER170W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1587477; DOI=10.1016/0378-1119(92)90721-z;
RA Cooper A.J., Friedberg E.C.;
RT "A putative second adenylate kinase-encoding gene from the yeast
RT Saccharomyces cerevisiae.";
RL Gene 114:145-148(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=DL-1;
RX PubMed=1620094; DOI=10.1007/bf00265432;
RA Schricker R., Magdolen V., Bandlow W.;
RT "A new member of the adenylate kinase family in yeast: PAK3 is highly
RT homologous to mammalian AK3 and is targeted to mitochondria.";
RL Mol. Gen. Genet. 233:363-371(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION.
RC STRAIN=DL-1;
RX PubMed=8537371; DOI=10.1074/jbc.270.52.31103;
RA Schricker R., Magdolen V., Strobel G., Bogengruber E., Breitenbach M.,
RA Bandlow W.;
RT "Strain-dependent occurrence of functional GTP:AMP phosphotransferase (AK3)
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:31103-31110(1995).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15753074; DOI=10.1074/jbc.m500847200;
RA Gu Y., Gordon D.M., Amutha B., Pain D.;
RT "A GTP:AMP phosphotransferase, Adk2p, in Saccharomyces cerevisiae. Role of
RT the C terminus in protein folding/stabilization, thermal tolerance, and
RT enzymatic activity.";
RL J. Biol. Chem. 280:18604-18609(2005).
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. Does not accept ATP as phosphate donor. {ECO:0000255|HAMAP-
CC Rule:MF_03169, ECO:0000269|PubMed:15753074,
CC ECO:0000269|PubMed:8537371}.
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 ECO:0000269|PubMed:15753074};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Active at 30 degrees
CC Celsius, and rapidly inactivated with an increase of 5 degrees
CC Celsius. {ECO:0000269|PubMed:15753074};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03169, ECO:0000269|PubMed:1620094}.
CC -!- INDUCTION: Expression level is low on glucose or other fermentable
CC carbon sources. Induced about 3-fold on glycerol, and significantly
CC induced by ethanol. {ECO:0000269|PubMed:1620094}.
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 -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Depending on the yeast strain, the GTP:AMP
CC phosphotransferase is encoded by ADK2 with or without a single base
CC pair deletion/insertion near the 3' end of the open reading frame,
CC resulting in a long or a short form. The ADK2 short form (this entry)
CC is also referred to as PAK3, while the long form has been named AKY3. A
CC sequence of the long form can be found in strain D273-10B (AC E9P974).
CC The modified C-terminus in the long form contributes to protein folding
CC and is critical for protein stability. {ECO:0000305|PubMed:8537371}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03169}.
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DR EMBL; M77757; AAA34418.1; -; Genomic_DNA.
DR EMBL; X65126; CAA46254.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64697.1; -; Genomic_DNA.
DR EMBL; AY558457; AAS56783.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07832.1; -; Genomic_DNA.
DR PIR; S23568; S23568.
DR RefSeq; NP_011097.3; NM_001179060.3.
DR AlphaFoldDB; P26364; -.
DR SMR; P26364; -.
DR BioGRID; 36923; 33.
DR DIP; DIP-4877N; -.
DR IntAct; P26364; 1.
DR MINT; P26364; -.
DR STRING; 4932.YER170W; -.
DR PaxDb; P26364; -.
DR PRIDE; P26364; -.
DR EnsemblFungi; YER170W_mRNA; YER170W; YER170W.
DR GeneID; 856917; -.
DR KEGG; sce:YER170W; -.
DR SGD; S000000972; ADK2.
DR VEuPathDB; FungiDB:YER170W; -.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00940000175921; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR InParanoid; P26364; -.
DR OMA; IKVENTM; -.
DR BioCyc; YEAST:YER170W-MON; -.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P26364; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P26364; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IDA:SGD.
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:0009117; P:nucleotide metabolic process; IDA:SGD.
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; 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 TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..225
FT /note="GTP:AMP phosphotransferase, mitochondrial"
FT /id="PRO_0000158907"
FT REGION 45..74
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT REGION 144..181
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 24..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 46
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 72..74
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 103..106
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 110
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 154..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 178
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 189
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
SQ SEQUENCE 225 AA; 25194 MW; 3B192BE2535BF91F CRC64;
MKADAKQITH LLKPLRLLLL GAPGSGKGTQ TSRLLKQIPQ LSSISSGDIL RQEIKSESTL
GREATTYIAQ GKLLPDDLIT RLITFRLSAL GWLKPSAMWL LDGFPRTTAQ ASALDELLKQ
HDASLNLVVE LDVPESTILE RIENRYVHVP SGRVYNLQYN PPKVPGLDDI TGEPLTKRLD
DTAEVFKKRL EEYKKTNEPL KDYYKKSGIF GTVSGETSDI IFRNY
