KAD3_PLAF7
ID KAD3_PLAF7 Reviewed; 229 AA.
AC Q8I1T1; Q964H2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GTP:AMP phosphotransferase {ECO:0000303|PubMed:15478799};
DE Short=PfGAK {ECO:0000303|PubMed:15478799};
DE EC=2.7.4.10 {ECO:0000269|PubMed:15478799};
DE Flags: Precursor;
GN Name=GAK {ECO:0000303|PubMed:15478799};
GN ORFNames=PF3D7_0415600 {ECO:0000312|EMBL:CAD49193.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|EMBL:AAK58841.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RC STRAIN=3D7 {ECO:0000312|EMBL:AAK58841.1};
RX PubMed=15478799; DOI=10.1016/j.molbiopara.2004.04.001;
RA Ulschmid J.K., Rahlfs S., Schirmer R.H., Becker K.;
RT "Adenylate kinase and GTP:AMP phosphotransferase of the malarial parasite
RT Plasmodium falciparum. Central players in cellular energy metabolism.";
RL Mol. Biochem. Parasitol. 136:211-220(2004).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=22819813; DOI=10.1016/j.febslet.2012.07.013;
RA Ma J., Rahlfs S., Jortzik E., Schirmer R.H., Przyborski J.M., Becker K.;
RT "Subcellular localization of adenylate kinases in Plasmodium falciparum.";
RL FEBS Lett. 586:3037-3043(2012).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between GTP and AMP (PubMed:15478799). Has very low activity with
CC UTP, ITP, CTP and IMP and no activity with ATP, GMP, CMP and UMP in
CC vitro (PubMed:15478799). {ECO:0000269|PubMed:15478799}.
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:0000269|PubMed:15478799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + GTP = ADP + GDP; Xref=Rhea:RHEA:29863,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15478799};
CC -!- ACTIVITY REGULATION: Inhibited by the dinucleoside pentaphosphate
CC compound P1,P5-di(guanosine-5') pentaphosphate (GP5A).
CC {ECO:0000269|PubMed:15478799}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for AMP (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC KM=130 uM for GTP (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC Vmax=100 umol/min/mg enzyme (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC Note=kcat is 46 sec(-1) (at 25 degrees Celsius and pH 6).
CC {ECO:0000269|PubMed:15478799};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:15478799};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22819813}.
CC -!- DOMAIN: There is a putative zinc finger domain which may bind to iron.
CC {ECO:0000269|PubMed:15478799}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000255|RuleBase:RU003330}.
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DR EMBL; AF308612; AAK58841.1; -; mRNA.
DR EMBL; AL844503; CAD49193.1; -; Genomic_DNA.
DR RefSeq; XP_001351464.1; XM_001351428.1.
DR AlphaFoldDB; Q8I1T1; -.
DR SMR; Q8I1T1; -.
DR STRING; 5833.PFD0755c; -.
DR PRIDE; Q8I1T1; -.
DR EnsemblProtists; CAD49193; CAD49193; PF3D7_0415600.
DR GeneID; 812591; -.
DR KEGG; pfa:PF3D7_0415600; -.
DR VEuPathDB; PlasmoDB:PF3D7_0415600; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000108500; -.
DR VEuPathDB; PlasmoDB:Pf7G8_040020500; -.
DR VEuPathDB; PlasmoDB:PfCD01_040021100; -.
DR VEuPathDB; PlasmoDB:PfDd2_040020800; -.
DR VEuPathDB; PlasmoDB:PfGA01_040020100; -.
DR VEuPathDB; PlasmoDB:PfGB4_040020900; -.
DR VEuPathDB; PlasmoDB:PfGN01_040021000; -.
DR VEuPathDB; PlasmoDB:PfHB3_040019600; -.
DR VEuPathDB; PlasmoDB:PfIT_040020000; -.
DR VEuPathDB; PlasmoDB:PfKE01_040022500; -.
DR VEuPathDB; PlasmoDB:PfKH01_040021000; -.
DR VEuPathDB; PlasmoDB:PfKH02_040020600; -.
DR VEuPathDB; PlasmoDB:PfML01_040021700; -.
DR VEuPathDB; PlasmoDB:PfNF135_040021100; -.
DR VEuPathDB; PlasmoDB:PfNF166_040021600; -.
DR VEuPathDB; PlasmoDB:PfNF54_040021300; -.
DR VEuPathDB; PlasmoDB:PfSD01_070031600; -.
DR VEuPathDB; PlasmoDB:PfSN01_040020400; -.
DR VEuPathDB; PlasmoDB:PfTG01_040021000; -.
DR HOGENOM; CLU_032354_1_2_1; -.
DR InParanoid; Q8I1T1; -.
DR OMA; PPPHCET; -.
DR PhylomeDB; Q8I1T1; -.
DR BRENDA; 2.7.4.10; 4889.
DR Reactome; R-PFA-499943; Interconversion of nucleotide di- and triphosphates.
DR Proteomes; UP000001450; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:GeneDB.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IDA:GeneDB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:GeneDB.
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 InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 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 Iron; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:22819813"
FT CHAIN ?..229
FT /note="GTP:AMP phosphotransferase"
FT /id="PRO_0000455421"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT REGION 123..170
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 10..15
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 87..90
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
FT BINDING 178
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8IJV6"
SQ SEQUENCE 229 AA; 26738 MW; A6AE8D0844C260E4 CRC64;
MRIVLFGAPG VGKGTFAEIL SKKENLKHIN VGNILRNEIK KESNIGKEVQ NVVRSGNLVS
DSLIINIVHD EMKNILNKKY KGFILDGFPR NMYQSKELIK MTNIDLFVNI YLPRNILIKK
LLGRRICNIC DKNFNVSNIQ QDSFDMPPIL PSKDCIQCNG HTNLIKRKDD NEDIINHRLN
SYESDYIPII QFFKNEKYNL IDFPLRRGIR DFDDFYSILV NYRKNEKLK
