ID T0MHY6_9MICR Unreviewed; 245 AA.
AC T0MHY6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
GN ORFNames=NAPIS_ORF01851 {ECO:0000313|EMBL:EQB60585.1};
OS Vairimorpha apis BRL 01.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=1037528 {ECO:0000313|EMBL:EQB60585.1, ECO:0000313|Proteomes:UP000053780};
RN [1] {ECO:0000313|EMBL:EQB60585.1, ECO:0000313|Proteomes:UP000053780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL 01 {ECO:0000313|EMBL:EQB60585.1,
RC ECO:0000313|Proteomes:UP000053780};
RX PubMed=23829473; DOI=10.1186/1471-2164-14-451;
RA Chen Yp., Pettis J.S., Zhao Y., Liu X., Tallon L.J., Sadzewicz L.D., Li R.,
RA Zheng H., Huang S., Zhang X., Hamilton M.C., Pernal S.F.,
RA Melathopoulos A.P., Yan X., Evans J.D.;
RT "Genome sequencing and comparative genomics of honey bee microsporidia,
RT Nosema apis reveal novel insights into host-parasite interactions.";
RL BMC Genomics 14:451-451(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes four methylations of the modified target histidine residue in
CC translation elongation factor 2 (EF-2), to form an intermediate called
CC diphthine methyl ester. The four successive methylation reactions
CC represent the second step of diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl
CC ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA-
CC COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314;
CC Evidence={ECO:0000256|ARBA:ARBA00000054};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the diphthine synthase family.
CC {ECO:0000256|ARBA:ARBA00006729}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE647271; EQB60585.1; -; Genomic_DNA.
DR AlphaFoldDB; T0MHY6; -.
DR VEuPathDB; MicrosporidiaDB:NAPIS_ORF01851; -.
DR HOGENOM; CLU_066040_1_0_1; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000053780; Unassembled WGS sequence.
DR GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd11647; DHP5_DphB; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053780};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR036432-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..213
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|PIRSR:PIRSR036432-1"
FT BINDING 111..112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
SQ SEQUENCE 245 AA; 28341 MW; F5C0DDA53CB12DCB CRC64;
MLYIIGTGLH SYKDISIRSI EILKKCKKIY FENYTSIQQA PICELSNFLN KKIYILDRNS
VETEEMFFEE SKYDDISILV VGTPMFATTH TGLLITAKQL NIKVEVIHNA SIQNVLGCLG
LYSYNFGKTI SIPYFTDTWK PRSFLDNINQ NRKINLHTLC LLDIKVDENR FMTANEALKQ
ILMFDDIHEN FKVFVIARFG SPDQVIKYDT IKALIEKDFG NPLHSIVIPG EMDVIEKEMV
EFLFN
//
