ID A0A099P2T0_PICKU Unreviewed; 624 AA.
AC A0A099P2T0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=JL09_g2253 {ECO:0000313|EMBL:KGK38589.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK38589.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGK38589.1}.
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DR EMBL; JQFK01000018; KGK38589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099P2T0; -.
DR VEuPathDB; FungiDB:C5L36_0B07880; -.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_010289_2_1_1; -.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR CDD; cd06155; eu_AANH_C_1; 1.
DR CDD; cd06156; eu_AANH_C_2; 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 InterPro; IPR006175; YjgF/YER057c/UK114.
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 Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
PE 4: Predicted;
FT DOMAIN 1..239
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 624 AA; 70665 MW; 7EDA924F5277516D CRC64;
MKFVALVSGG KDSCFNILHC LAQGHELVCL ANLYPAEPDN DEIDSYMYQT VGHDVLTLYE
KCTGKPMYRE PILGNASNQK LEYKKTENDE TEDLYRLLDK VVKKHPDVEG VSVGAILSSY
QRTRVEDVCS RLGLTSLAYL WQRDQGELMN EMCSSGMDAR IIKVAAIGLN DSNLGMSLQE
IHPTLLQLNK MFGVHICGEG GEFETSVLDA PFFKYGRIVI TEKSIVKHTN DEVWYLKMKV
GFEPKDVSDD PIDWKKHVVV PPLLNETFHE IYESGKIRDE YSVAKVNINE KYWKFNVYET
DDKLYISNIT SVEESIEGQV ADIFKQLSGT LNQFELDFEN IQSAKLLLQD MSNFVTINSI
YVKYFTKPLP PARICVETML PNNTHAQLSV VVLKELDAKV GLHVQGISYW APCNIGPYSQ
AISSRNDQIV RISGQIPLIP MNMTLPTPKD DRLSSTLSLK HYHSIKEVTN YKNNLLTICF
IKDCNLVSMV QEQFREYISL CEDEGYTGTE NLVVVQVTEL PKGSDVEWGG LSYREECESL
NYDSDSLSED ENENESKDAK DKVKVSYVDK LSEYSTFKDN RFYEIYGDVL QIDAEMPQHC
EVFPAVAVYG SSGHKSLAIV ESTV
//
