KAD3_YEASX
ID KAD3_YEASX Reviewed; 234 AA.
AC E9P974;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
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;
GN OrderedLocusNames=YER170W;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 24657 / D273-10B;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 24657 / D273-10B;
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).
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:8537371};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=100 umol/min/mg enzyme for GTP {ECO:0000269|PubMed:15753074,
CC ECO:0000269|PubMed:8537371};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:15753074,
CC ECO:0000269|PubMed:8537371};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Active from 30 to 55
CC degrees Celsius. {ECO:0000269|PubMed:15753074,
CC ECO:0000269|PubMed:8537371};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03169, ECO:0000269|PubMed:8537371}.
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 disassembling the active
CC center during each catalytic cycle provides an effective means to
CC prevent GTP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03169}.
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 long form (this entry) is
CC also referred to as AKY3, while the short form has been named PAK3. A
CC sequence of the short form can be found in strain S288c (AC P26364).
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; AY949617; AAX51239.1; -; Genomic_DNA.
DR AlphaFoldDB; E9P974; -.
DR SMR; E9P974; -.
DR VEuPathDB; FungiDB:YER170W; -.
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:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0046039; P:GTP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046041; P:ITP 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; -; 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 GTP-binding; Kinase; Mitochondrion; Nucleotide-binding; Transferase.
FT CHAIN 1..234
FT /note="GTP:AMP phosphotransferase, mitochondrial"
FT /id="PRO_0000422161"
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 234 AA; 26073 MW; 3594817FFAB5FFE1 CRC64;
MKADAKQITH LLKPLRLLLL GAPGSGKGTQ TSRLLKQIPQ LSSISSGDIL RQEIKSESTL
GREATTYIAQ GKLLPDDLIT RLITFRLSAL GWLKPSAMWL LDGFPRTTAQ ASALDELLKQ
HDASLNLVVE LDVPESTILE RIENRYVHVP SGRVYNLQYN PPKVPGLDDI TGEPLTKRLD
DTAEVFKKRL EEYKKTNEPL KDYYKKSGIF GTVSGETSDI IFPKLLNLIT SKFG
