ID   DPHB_METTP              Reviewed;         265 AA.
AC   A0B879;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Mthe_1120;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) 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; CP000477; ABK14903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B879; -.
DR   SMR; A0B879; -.
DR   STRING; 349307.Mthe_1120; -.
DR   EnsemblBacteria; ABK14903; ABK14903; Mthe_1120.
DR   KEGG; mtp:Mthe_1120; -.
DR   HOGENOM; CLU_066040_0_0_2; -.
DR   OMA; TAGDPMV; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000674; 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..265
FT                   /note="Diphthine synthase"
FT                   /id="PRO_1000064825"
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         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         112..113
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         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
SQ   SEQUENCE   265 AA;  29441 MW;  CE333A77AAAB29B2 CRC64;
     MLFFVGLGLY DERDISVKGL EIVRCADAVY AEFYTSRLMG TSIERLEQLY GREIRMLSRS
     EIEGEPEWLE HARDRNVALL VGGDPMISTT HLDLRLRAIE MGIDTRVIHG SNIASAVPGI
     TGLQNYRFGR SATVPFPHIV RGKRIVSSTP YNAVKDNLRR DLHTLLYLDI QDERFMCINE
     AAALLIEVAN GSGDEDFASN LAVGIARAGS EDMCVRAGTL LELKTYSFGP PLHVMVIPGR
     LHFMEAKALR MLAGAPEELL SGYEL