ID   DPHB_HALWD              Reviewed;         260 AA.
AC   Q18JS3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Diphthine synthase {ECO:0000255|HAMAP-Rule:MF_01084};
DE            EC=2.1.1.98 {ECO:0000255|HAMAP-Rule:MF_01084};
DE   AltName: Full=Diphthamide biosynthesis methyltransferase {ECO:0000255|HAMAP-Rule:MF_01084};
GN   Name=dphB {ECO:0000255|HAMAP-Rule:MF_01084}; OrderedLocusNames=HQ_1603A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       catalyzes the trimethylation of the amino group of the modified target
CC       histidine residue in translation elongation factor 2 (EF-2), to form an
CC       intermediate called diphthine. The three successive methylation
CC       reactions represent the second step of diphthamide biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01084}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC         elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-
CC         [translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:36415, Rhea:RHEA-COMP:9749, Rhea:RHEA-
CC         COMP:10172, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73995, ChEBI:CHEBI:82696; EC=2.1.1.98;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01084};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01084}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01084}.
CC   -!- SIMILARITY: Belongs to the diphthine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01084}.
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DR   EMBL; AM180088; CAJ51731.1; -; Genomic_DNA.
DR   RefSeq; WP_011570883.1; NC_008212.1.
DR   AlphaFoldDB; Q18JS3; -.
DR   SMR; Q18JS3; -.
DR   STRING; 362976.HQ_1603A; -.
DR   PRIDE; Q18JS3; -.
DR   EnsemblBacteria; CAJ51731; CAJ51731; HQ_1603A.
DR   GeneID; 4193927; -.
DR   KEGG; hwa:HQ_1603A; -.
DR   eggNOG; arCOG04161; Archaea.
DR   HOGENOM; CLU_066040_0_0_2; -.
DR   OMA; TAGDPMV; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0004164; F:diphthine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniRule.
DR   CDD; cd11647; DHP5_DphB; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 1.
DR   HAMAP; MF_01084; Diphthine_synth; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR004551; Dphthn_synthase.
DR   PANTHER; PTHR10882; PTHR10882; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036432; Diphthine_synth; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR00522; dph5; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..260
FT                   /note="Diphthine synthase"
FT                   /id="PRO_1000064814"
FT   BINDING         9
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         113..114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
SQ   SEQUENCE   260 AA;  28086 MW;  889994EE70590424 CRC64;
     MLTFIGLGLY DERSISIAGR DALQAADYVA AEFYTSYLVD ATVSDLETAH DIDIDVRDRE
     GVEQHPEDIL RKAQSEDVAF LTAGDTMIST THTDLRLRAI DRGIDTRVIH GVTAQTAASG
     LTGLQNYRFG KSVTLPFPYA HGAEGVPTSV TDSIAANRER GLHTVVYLDI KANRDEYLRA
     SDAAEMLATD LEDMLAIAVA RAGSPDPTVR ADRLSALAEK DFGDPLHLLV LPGELHHLEE
     EALAALADAP ADMLNAVDSQ