ID Q8IJV5_PLAF7 Unreviewed; 274 AA.
AC Q8IJV5;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
GN ORFNames=PF3D7_1009000 {ECO:0000313|EMBL:CZT98339.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT98339.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZT98339.1, 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 -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes four methylations of the modified target histidine residue in
CC translation elongation factor 2 (EF-2), to form an intermediate called
CC diphthine methyl ester. The four successive methylation reactions
CC represent the second step of diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl
CC ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA-
CC COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314;
CC Evidence={ECO:0000256|ARBA:ARBA00000054};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the diphthine synthase family.
CC {ECO:0000256|ARBA:ARBA00006729}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN999944; CZT98339.1; -; Genomic_DNA.
DR RefSeq; XP_001347372.1; XM_001347336.1.
DR AlphaFoldDB; Q8IJV5; -.
DR SMR; Q8IJV5; -.
DR STRING; 36329.Q8IJV5; -.
DR PaxDb; 5833-PF10_0087; -.
DR EnsemblProtists; CZT98339; CZT98339; PF3D7_1009000.
DR GeneID; 810245; -.
DR KEGG; pfa:PF3D7_1009000; -.
DR VEuPathDB; PlasmoDB:PF3D7_1009000; -.
DR HOGENOM; CLU_066040_1_0_1; -.
DR InParanoid; Q8IJV5; -.
DR OMA; TAGDPMV; -.
DR OrthoDB; 1093496at2759; -.
DR PhylomeDB; Q8IJV5; -.
DR Reactome; R-PFA-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001450; Chromosome 10.
DR GO; GO:0004164; F:diphthine synthase activity; ISS:GeneDB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd11647; DHP5_DphB; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR004551; Dphthn_synthase.
DR NCBIfam; TIGR00522; dph5; 1.
DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036432; Diphthine_synth; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CZT98339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR036432-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CZT98339.1}.
FT DOMAIN 3..178
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
SQ SEQUENCE 274 AA; 31735 MW; EE07DDE120801250 CRC64;
MVLYIIGLGL GDEKDITIKG KELIEKSDVV YLETYTSILF VSKDVLEETY KKSIEEVDRD
FAEENCDKIL DEAKNKKVSF LVVGDPLCAT THHDIILRAK KKNIDVEIIH NTSIISAIGE
CGMQLYNFGQ IVSIPYFEDN YKPTSYYDKI YINLKNNFHT LCLLDIKVKE RTVENIMRNK
KIYEPPRFMT INDSIEQLLY CEHIHKKNII TKNTLGIAII QIGTDNQQII SGDLLTLKDI
SYNKPLHSLI ICAPTLHDIE KEYFDLYHYN NMKK
//
