KAD1_PLAF7
ID KAD1_PLAF7 Reviewed; 242 AA.
AC Q8IJV6; Q7Z0H0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Adenylate kinase 1 {ECO:0000303|PubMed:22819813};
DE Short=PfAK1 {ECO:0000303|PubMed:22819813};
DE EC=2.7.4.3 {ECO:0000269|PubMed:15478799};
GN Name=AK1 {ECO:0000303|PubMed:22819813};
GN Synonyms=AK {ECO:0000303|PubMed:15478799};
GN ORFNames=PF3D7_1008900 {ECO:0000312|EMBL:CZT98338.1};
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:AAM95703.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=3D7 {ECO:0000312|EMBL:AAM95703.1};
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: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).
RN [4] {ECO:0007744|PDB:3TLX}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH ADP; AMP AND ATP.
RA Wernimont A.K., Loppnau P., Crombet L., Weadge J., Perieteanu A.,
RA Edwards A.M., Arrowsmith C.H., Park H., Bountra C., Hui R., Amani M.;
RT "Crystal Structure of PF10_0086, adenylate kinase from plasmodium
RT falciparum.";
RL Submitted (AUG-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP (PubMed:15478799). Has very low activity with
CC CTP, GTP, ITP and UTP and no activity with GMP, CMP, UMP or IMP in
CC vitro (PubMed:15478799). {ECO:0000269|PubMed:15478799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000269|PubMed:15478799};
CC -!- ACTIVITY REGULATION: Inhibited by the dinucleoside pentaphosphate
CC compound P1,P5-di(adenosine-5') pentaphosphate (AP5A).
CC {ECO:0000269|PubMed:15478799}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for AMP (at 25 degrees Celsius and pH 6 or pH 7.4)
CC {ECO:0000269|PubMed:15478799};
CC KM=130 uM for ATP (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC KM=120 uM for ATP (at 25 degrees Celsius and pH 7.4)
CC {ECO:0000269|PubMed:15478799};
CC KM=240 uM for GTP (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC Vmax=75 umol/min/mg enzyme (at 25 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:15478799};
CC Note=kcat is 35 sec(-1) (at 25 degrees Celsius and pH 6).
CC {ECO:0000269|PubMed:15478799};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:15478799};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22819813}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000255|RuleBase:RU003330}.
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DR EMBL; AY118172; AAM95703.1; -; mRNA.
DR EMBL; LN999944; CZT98338.1; -; Genomic_DNA.
DR RefSeq; XP_001347371.1; XM_001347335.1.
DR PDB; 3TLX; X-ray; 2.75 A; A/B/C/D=1-242.
DR PDBsum; 3TLX; -.
DR AlphaFoldDB; Q8IJV6; -.
DR SMR; Q8IJV6; -.
DR STRING; 5833.PF10_0086; -.
DR SwissPalm; Q8IJV6; -.
DR PRIDE; Q8IJV6; -.
DR EnsemblProtists; CZT98338; CZT98338; PF3D7_1008900.
DR GeneID; 810244; -.
DR KEGG; pfa:PF3D7_1008900; -.
DR VEuPathDB; PlasmoDB:PF3D7_1008900; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000294600; -.
DR VEuPathDB; PlasmoDB:Pf7G8_100013300; -.
DR VEuPathDB; PlasmoDB:PfCD01_100014100; -.
DR VEuPathDB; PlasmoDB:PfDd2_100014200; -.
DR VEuPathDB; PlasmoDB:PfGA01_100014200; -.
DR VEuPathDB; PlasmoDB:PfGB4_100013900; -.
DR VEuPathDB; PlasmoDB:PfGN01_100014500; -.
DR VEuPathDB; PlasmoDB:PfHB3_100013300; -.
DR VEuPathDB; PlasmoDB:PfIT_100012900; -.
DR VEuPathDB; PlasmoDB:PfKE01_100014200; -.
DR VEuPathDB; PlasmoDB:PfKH01_100013500; -.
DR VEuPathDB; PlasmoDB:PfKH02_100014300; -.
DR VEuPathDB; PlasmoDB:PfML01_100013200; -.
DR VEuPathDB; PlasmoDB:PfNF135_100014400; -.
DR VEuPathDB; PlasmoDB:PfNF166_100013900; -.
DR VEuPathDB; PlasmoDB:PfNF54_100014100; -.
DR VEuPathDB; PlasmoDB:PfSD01_100013600; -.
DR VEuPathDB; PlasmoDB:PfSN01_100014300; -.
DR VEuPathDB; PlasmoDB:PfTG01_100014100; -.
DR HOGENOM; CLU_032354_1_2_1; -.
DR InParanoid; Q8IJV6; -.
DR OMA; FHNRMRV; -.
DR PhylomeDB; Q8IJV6; -.
DR BRENDA; 2.7.4.3; 4889.
DR Reactome; R-PFA-499943; Interconversion of nucleotide di- and triphosphates.
DR EvolutionaryTrace; Q8IJV6; -.
DR Proteomes; UP000001450; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:CACAO.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS: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; IPR007862; Adenylate_kinase_lid-dom.
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 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..242
FT /note="Adenylate kinase 1"
FT /id="PRO_0000455418"
FT REGION 58..87
FT /note="NMP"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT REGION 154..191
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 38..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 85..87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 113..116
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 113
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 120
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 199
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3TLX"
SQ SEQUENCE 242 AA; 27611 MW; 08A8F01A74E721DD CRC64;
MNENLENFST IDLLNELKRR YACLSKPDGR YIFLGAPGSG KGTQSLNLKK SHCYCHLSTG
DLLREAAEKK TELGLKIKNI INEGKLVDDQ MVLSLVDEKL KTPQCKKGFI LDGYPRNVKQ
AEDLNKLLQK NQTKLDGVFY FNVPDEVLVN RISGRLIHKP SGRIYHKIFN PPKVPFRDDV
TNEPLIQRED DNEDVLKKRL TVFKSETSPL ISYYKNKNLL INLDATQPAN DLEKKISQHI
DG
