ID A0A2B7GVR6_9EURY Unreviewed; 257 AA.
AC A0A2B7GVR6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Diphthine synthase {ECO:0000256|HAMAP-Rule:MF_01084};
DE EC=2.1.1.98 {ECO:0000256|HAMAP-Rule:MF_01084};
DE AltName: Full=Diphthamide biosynthesis methyltransferase {ECO:0000256|HAMAP-Rule:MF_01084};
GN Name=dphB {ECO:0000256|HAMAP-Rule:MF_01084};
GN ORFNames=CP556_13190 {ECO:0000313|EMBL:PGF16981.1};
OS Natrinema sp. CBA1119.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1608465 {ECO:0000313|EMBL:PGF16981.1, ECO:0000313|Proteomes:UP000223005};
RN [1] {ECO:0000313|EMBL:PGF16981.1, ECO:0000313|Proteomes:UP000223005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1119 {ECO:0000313|EMBL:PGF16981.1,
RC ECO:0000313|Proteomes:UP000223005};
RA Roh S.W., Kim Y.B., Kim J.Y.;
RT "Genome sequences of Natrinema thermophila CBA1119T.";
RL Submitted (OCT-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_01084};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156, ECO:0000256|HAMAP-Rule:MF_01084}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01084}.
CC -!- SIMILARITY: Belongs to the diphthine synthase family.
CC {ECO:0000256|ARBA:ARBA00006729, ECO:0000256|HAMAP-Rule:MF_01084}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGF16981.1}.
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DR EMBL; PDBS01000001; PGF16981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7GVR6; -.
DR OrthoDB; 39139at2157; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000223005; Unassembled WGS sequence.
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:protein histidyl modification to diphthamide; IEA:UniProtKB-UniRule.
DR CDD; cd11647; DHP5_DphB; 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 NCBIfam; TIGR00522; dph5; 1.
DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036432; Diphthine_synth; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01084};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01084};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01084}.
FT DOMAIN 1..218
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01084,
FT ECO:0000256|PIRSR:PIRSR036432-1"
SQ SEQUENCE 257 AA; 27912 MW; 59C04EA840181E64 CRC64;
MLTFIGLGLY DERSITVEGR DALRAADRVY AEFYTSQLIG TTIDDLESYH DLEIEVRDRA
GVEQHPDDML TAAEDEDVAF LTAGDTMIST THVDLRLRAH DRGIETRVLH GVTAQTATSA
LTGLQNYRFG KATTLPFPYA HGAEGLPASV TETIDDNRAD GLHTVVYLDI KAEREEYMTA
DIGADLLAEE YPDLAGVVVA RAGSPDPLVE AGTMTELADQ EFGDPLHLLV IPGECHLLEA
DALVELAGAD RDVLEIA
//
