ID   DPHB_HALMA              Reviewed;         259 AA.
AC   Q5V2B7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=rrnAC1406;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46335.1; -; Genomic_DNA.
DR   RefSeq; WP_011223602.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V2B7; -.
DR   SMR; Q5V2B7; -.
DR   STRING; 272569.rrnAC1406; -.
DR   EnsemblBacteria; AAV46335; AAV46335; rrnAC1406.
DR   GeneID; 40152375; -.
DR   KEGG; hma:rrnAC1406; -.
DR   PATRIC; fig|272569.17.peg.2102; -.
DR   eggNOG; arCOG04161; Archaea.
DR   HOGENOM; CLU_066040_0_0_2; -.
DR   OMA; TAGDPMV; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001169; Chromosome I.
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..259
FT                   /note="Diphthine synthase"
FT                   /id="PRO_1000064813"
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         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         234
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
SQ   SEQUENCE   259 AA;  27938 MW;  ED67DFB212DB0379 CRC64;
     MLTFVGLGLY DERSVTVAGR DAIRDADRVF AEFYTSRLIG TDIETLEDTL ETSIERRDRA
     GIEQDPEPIL EAAESEHVVF CTAGDTMVST THADLRLRAA DRGIETRIVH GTTAQTAAGS
     LTGLQNYRFG KATTLPFEDA HGGDGVPDSV VATIEDNRDR DLHTLVYLDI KVDDPHWEES
     DDTYMTASQA ATMLSEPFPD TLGVVVARAG SPDPLVAADT LDELATQTFG DPLHLLVIPG
     SLHPLEADTL ESVAGAALE