ID R0MF74_NOSB1 Unreviewed; 242 AA.
AC R0MF74;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 Name=ATBD4 {ECO:0000313|EMBL:EOB11378.1};
GN ORFNames=NBO_1239g0006 {ECO:0000313|EMBL:EOB11378.1};
OS Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS (Pebrine of silkworm).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB11378.1, ECO:0000313|Proteomes:UP000016927};
RN [1] {ECO:0000313|EMBL:EOB11378.1, ECO:0000313|Proteomes:UP000016927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT "Comparative genomics of parasitic silkworm microsporidia reveal an
RT association between genome expansion and host adaptation.";
RL BMC Genomics 14:186-186(2013).
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; KB910146; EOB11378.1; -; Genomic_DNA.
DR AlphaFoldDB; R0MF74; -.
DR STRING; 578461.R0MF74; -.
DR EnsemblFungi; EOB11378; EOB11378; NBO_1239g0006.
DR VEuPathDB; MicrosporidiaDB:NBO_1239g0006; -.
DR HOGENOM; CLU_010289_0_0_1; -.
DR OMA; EMECNED; -.
DR Proteomes; UP000016927; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000313|EMBL:EOB11378.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EOB11378.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016927}.
FT DOMAIN 2..217
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 242 AA; 27577 MW; AE8EF46469673C0F CRC64;
MDFVALVSGG KDSIYSIKCS IDQGHRLVGL LYMKNTSSYV DSYMYQTVGS EVVEHFGKCL
DVPLFTSVSQ CKAIDTELNY TGDREDEVED LFKALSEIKK KIKFEAISSG AILSRYQKNR
VEHVANRLNL VSLSPLWQRD QKILLKEMLD YEIEAFIVKV ASSSLDKSYL GKHIRSIYES
NALLDDNYCG EGGEYESVVL DCPLFKYKLE YNDFTILNHP EEQDGFGSVF YCVFNGLRLI
KK
//
