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Database: UniProt
Entry: A0A197KAX8_9FUNG
LinkDB: A0A197KAX8_9FUNG
Original site: A0A197KAX8_9FUNG 
ID   A0A197KAX8_9FUNG        Unreviewed;       233 AA.
AC   A0A197KAX8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=K457DRAFT_15045 {ECO:0000313|EMBL:OAQ33841.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ33841.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ33841.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ33841.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV442019; OAQ33841.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197KAX8; -.
DR   STRING; 1314771.A0A197KAX8; -.
DR   OrthoDB; 316736at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01902; Diphthami_syn_2; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OAQ33841.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT   DOMAIN          7..219
FT                   /note="Diphthamide synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01902"
SQ   SEQUENCE   233 AA;  26283 MW;  291A5F315C55B3FB CRC64;
     MTATRKRAAI SFTGGKDCTL AMAMTKKAHD VVLLVTFGPK NFKSFKAHSL EIIRLQAKAM
     GVEHILVEIG EEGKTHLQCY REAIAEIKEK YNLDLLVTGD ILNVCDNFMT RATQDIIELS
     SPIWAIDRHK LLDTLFEHKF ELLITCASIK KLGDDENLAR KFVGSKLTPE FVEETLKPQE
     KTVDLGGELG EFHTMVLTVP ELYNGQRIEY EGLQIVEGEF MFMEFSSVQL VPV
//
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