DPHB_METLZ
ID DPHB_METLZ Reviewed; 252 AA.
AC A2SQF6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Mlab_0386;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06562.1; -; Genomic_DNA.
DR RefSeq; WP_011832763.1; NC_008942.1.
DR AlphaFoldDB; A2SQF6; -.
DR SMR; A2SQF6; -.
DR STRING; 410358.Mlab_0386; -.
DR EnsemblBacteria; ABN06562; ABN06562; Mlab_0386.
DR GeneID; 4794720; -.
DR KEGG; mla:Mlab_0386; -.
DR eggNOG; arCOG04161; Archaea.
DR HOGENOM; CLU_066040_0_0_2; -.
DR OMA; TAGDPMV; -.
DR OrthoDB; 102360at2157; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000000365; 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..252
FT /note="Diphthine synthase"
FT /id="PRO_1000064820"
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 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01084"
SQ SEQUENCE 252 AA; 27852 MW; 4BD7E5DB16CAF8E1 CRC64;
MLTFIGLGLF DEYDVSVRGL DAIKSADTVF LEVYTSVLMG APIERLEAFY GKKITPLYRE
DVEIHADKIL DAAEFGNAVF LTAGDSMVAT THSDLRIRAA DRNIPTTIIH GASITTAVCG
LSGLQNYRFG KSVSVPFPYG KWFPMTPIEV ISANLKENLH TLVFLDIQKD KERYMKISEA
VDLLEEQARR VDAGIPLYVG IARAGSPEPT VHAGNAEEMK AFDFGSPLHI LIVPATLHEI
EREYLERFAG LC