ID Q8SUJ3_ENCCU Unreviewed; 247 AA.
AC Q8SUJ3;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 13-SEP-2023, entry version 85.
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 OrderedLocusNames=ECU08_1840 {ECO:0000313|EMBL:CAD26487.1};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD26487.1, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD26487.1, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD26487.1,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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; AL590448; CAD26487.1; -; Genomic_DNA.
DR RefSeq; NP_597311.1; NM_001041920.1.
DR AlphaFoldDB; Q8SUJ3; -.
DR STRING; 284813.Q8SUJ3; -.
DR GeneID; 859733; -.
DR KEGG; ecu:ECU08_1840; -.
DR VEuPathDB; MicrosporidiaDB:ECU08_1840; -.
DR HOGENOM; CLU_010289_0_0_1; -.
DR InParanoid; Q8SUJ3; -.
DR OMA; NYALYWA; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000000819; Chromosome VIII.
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 Reference proteome {ECO:0000313|Proteomes:UP000000819}.
FT DOMAIN 1..221
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 247 AA; 27957 MW; 65C9F5C763462349 CRC64;
MRYLALVSGG KDSVHAMHCL QRLGHHVVGL LHMRCENGYQ DSYMYQTVGS EVANLLGECL
RVPVFICRTR CRSINQSLQY DREEGDEVED LYAAIAHVKE KICFEGVSSG AILSRYQKNR
VENVCNRLSL ECLSPLWGMD QESLLTEMIL SGMDARIVKV ASPLLGRECI NMSLDEVYER
LKTSPSSEIN FCGEGGEYET VVLDCPMFEK RISIDEYEAS PHPEEVGREG CVFHMRILKL
SLVEKHV
//
