ID A0A1E3Q5R5_LIPST Unreviewed; 663 AA.
AC A0A1E3Q5R5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=LIPSTDRAFT_281312 {ECO:0000313|EMBL:ODQ72991.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ72991.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ72991.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ72991.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454294; ODQ72991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3Q5R5; -.
DR STRING; 675824.A0A1E3Q5R5; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
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 Gene3D; 3.30.1330.40; RutC-like; 2.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
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 SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT DOMAIN 1..237
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 663 AA; 72460 MW; AF90A09FDC553BF1 CRC64;
MKTVALVSGG KDSCYNILHC IKNGHEVIAL ANLHPPPQSI FNDEDELIHE MDSFMYQTVG
HSVLNLYSDC FEIPMYRAPI TGSSVTTELD YATTATDETE DLYTLLQTVK AMHPDIEAVS
VGAILSTYQR SRVENVCSRL GLTVLAYLWR RDQAALFDEM IQGGVHAIII KVAGAGLTAE
KHLGKSLQQV RHQLFKLNQI YGSHICGEGG EYETLVLDCP VFVKKLVVDE TQVVNDDNGD
VAYLKLRAHA EDKDAVAEEW IDNIAVPPLL SEPFQGIFED LKGTDFGANE PEMAVSPATV
PELSIGISPT TISVANITAP NSSFISDEIP SIFEQLSNIM ATFKITDPYS ITSVTFQLAD
MQTFPAANES YKKFFSHPIT KPNPPARACI STLLPSSCRA SLSATITRVP DARSGLHVQG
RSYWAPANIG PYAQACTVQE GIYLAGQIPL IPARMVLYKD EGVLGQAALA MQNLARVMDA
VVVRLSEDDC GQFYYLIAYT SSLAAAKAAI RVASQTGVEC GIFAVVLVGL PVGAWVEYGG
VGINTRYVRS CTAGDVDEED EFTVKYSKHD RIDRVEYGTV IFGSWCCDDI ISEIANYVEK
KTEALLSVSV YISSSVSDAQ EVLMKLKEIV GINVCVEIVH VIHVVDKDCI IRNYGVLVRG
YLD
//
