ID   DPHB_METM5              Reviewed;         255 AA.
AC   A4FYP1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=MmarC5_1019;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO35325.1; -; Genomic_DNA.
DR   RefSeq; WP_011868778.1; NC_009135.1.
DR   AlphaFoldDB; A4FYP1; -.
DR   SMR; A4FYP1; -.
DR   STRING; 402880.MmarC5_1019; -.
DR   EnsemblBacteria; ABO35325; ABO35325; MmarC5_1019.
DR   GeneID; 4928434; -.
DR   KEGG; mmq:MmarC5_1019; -.
DR   eggNOG; arCOG04161; Archaea.
DR   HOGENOM; CLU_066040_1_0_2; -.
DR   OMA; TAGDPMV; -.
DR   OrthoDB; 102360at2157; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000253; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..255
FT                   /note="Diphthine synthase"
FT                   /id="PRO_1000064821"
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         164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
SQ   SEQUENCE   255 AA;  28655 MW;  2BCA4A3E0506A42E CRC64;
     MLVMAGLGLY DERDVTLKTL DFAKKVDKIY AEFYTAILTG TTMEKVEETL QKPITVLDRE
     KVEYETNKLI EEAKDKDIMF LTAGDPMVAT THVDIAVEAR KKGIEVVIIN APSIYSAIGI
     TGLQLYKFGK TTSIVFPEPN YFPETPYDVI KDNLKLGYHT LCLLDIQADK ERFMTANEGL
     SALLEIEEKR NENVISGETH AAVVARAGST KPGLYYGKIK DLINYDFGTP LHCVIIPGKL
     HFMEEDALKY LFENI