ID Q8I5J0_PLAF7 Unreviewed; 247 AA.
AC Q8I5J0;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=Diphthine--ammonia ligase {ECO:0000256|ARBA:ARBA00018426};
DE EC=6.3.1.14 {ECO:0000256|ARBA:ARBA00012089};
DE AltName: Full=Diphthamide synthase {ECO:0000256|ARBA:ARBA00029814};
DE AltName: Full=Diphthamide synthetase {ECO:0000256|ARBA:ARBA00031552};
GN ORFNames=PF3D7_1222500 {ECO:0000313|EMBL:CZT99384.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT99384.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZT99384.1, ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|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.,
RA Eisen J.A., Rutherford K., 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.,
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.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC ChEBI:CHEBI:456215; EC=6.3.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001559};
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DR EMBL; LN999947; CZT99384.1; -; Genomic_DNA.
DR RefSeq; XP_001350622.1; XM_001350586.1.
DR AlphaFoldDB; Q8I5J0; -.
DR SMR; Q8I5J0; -.
DR STRING; 36329.Q8I5J0; -.
DR PaxDb; 5833-PFL1080c; -.
DR EnsemblProtists; CZT99384; CZT99384; PF3D7_1222500.
DR GeneID; 811268; -.
DR KEGG; pfa:PF3D7_1222500; -.
DR VEuPathDB; PlasmoDB:PF3D7_1222500; -.
DR HOGENOM; CLU_010289_0_0_1; -.
DR InParanoid; Q8I5J0; -.
DR OMA; NYALYWA; -.
DR OrthoDB; 103959at2759; -.
DR PhylomeDB; Q8I5J0; -.
DR Proteomes; UP000001450; Chromosome 12.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.1490.10; putative n-type atp pyrophosphatase, domain 2; 1.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00290; MJ0570_dom; 1.
DR PANTHER; PTHR12196:SF2; DIPHTHINE--AMMONIA LIGASE; 1.
DR PANTHER; PTHR12196; DOMAIN OF UNKNOWN FUNCTION 71 DUF71 -CONTAINING PROTEIN; 1.
DR Pfam; PF01902; Diphthami_syn_2; 1.
DR PIRSF; PIRSF039123; Diphthamide_synthase; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CZT99384.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450}.
FT DOMAIN 1..228
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 247 AA; 28481 MW; 6E3EF4FAB97F7BED CRC64;
MNVLGLISGG KDSIQNLCYC HKNGHTIIAL AHLIPYEYQN ETDSFMYQSA GFELVPSIAR
CMEKPLIQHE IKRKAIKLDL AYTYDPNDEV EDLFELIHKA KTQFPSINAV SCGAIKSTYQ
KKRLEHVCER LNLDILTYLW DRDEKEILQG MINDGVEAIL VKIASYGLKK EHVGKSIKEM
YEYLKMINEK YGLNICGEGG EYETATLDCP LFKHKIIIED YEIIQHTDDL VSPVFLFKPL
KWKLEKK
//
