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DPHB_THEKO
ID   DPHB_THEKO              Reviewed;         264 AA.
AC   Q5JFE7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=TK0106;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD84295.1; -; Genomic_DNA.
DR   RefSeq; WP_011249061.1; NC_006624.1.
DR   AlphaFoldDB; Q5JFE7; -.
DR   SMR; Q5JFE7; -.
DR   STRING; 69014.TK0106; -.
DR   EnsemblBacteria; BAD84295; BAD84295; TK0106.
DR   GeneID; 3235243; -.
DR   KEGG; tko:TK0106; -.
DR   PATRIC; fig|69014.16.peg.106; -.
DR   eggNOG; arCOG04161; Archaea.
DR   HOGENOM; CLU_066040_0_0_2; -.
DR   InParanoid; Q5JFE7; -.
DR   OMA; TAGDPMV; -.
DR   OrthoDB; 102360at2157; -.
DR   PhylomeDB; Q5JFE7; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000536; 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..264
FT                   /note="Diphthine synthase"
FT                   /id="PRO_0000156127"
FT   BINDING         10
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         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         115..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT   BINDING         166
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   264 AA;  29687 MW;  C448E52ECBC7AD86 CRC64;
     MVLYFIGLGL YDEKDITLKG LETARRCDKV FAEFYTSLLA GTTLEKIEEL IGKPIVRLSR
     EDVELNFERI VLPEAKDKDV AFLTAGDPMV ATTHSDLRIR AKKAGVKSYV IHAPSIYSAV
     AITGLQIYKF GKSATVAYPE KNWFPTSHYD VIRDNKERGL HTLLFLDIKA DQNRYMTANE
     AMEILLKVEE MKGEGVFTPE TLVVVLARAG SLEPTLRAGY VRELINEDFG RQPHVLIVPG
     RLHIVEAEYL VEFAGAPEKI LEEV
 
 
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