DPH1_ENCCU
ID DPH1_ENCCU Reviewed; 347 AA.
AC Q8SUZ5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE EC=2.5.1.108 {ECO:0000250|UniProtKB:P40487};
DE AltName: Full=Diphthamide biosynthesis protein 1;
DE AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000305};
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000305};
GN Name=DPH1; OrderedLocusNames=ECU07_0980;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in elongation
CC factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group
CC from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction
CC is assisted by a reduction system comprising DPH3 and a NADH-dependent
CC reductase, predominantly CBR1. {ECO:0000250|UniProtKB:P40487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-
CC methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108;
CC Evidence={ECO:0000250|UniProtKB:P40487};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P40487};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P40487};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC predominantly CBR1. {ECO:0000250|UniProtKB:P40487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40487}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL590447; CAD25630.2; -; Genomic_DNA.
DR RefSeq; NP_586026.1; NM_001041648.1.
DR AlphaFoldDB; Q8SUZ5; -.
DR SMR; Q8SUZ5; -.
DR STRING; 284813.Q8SUZ5; -.
DR GeneID; 859456; -.
DR KEGG; ecu:ECU07_0980; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_0980; -.
DR HOGENOM; CLU_037146_1_1_1; -.
DR InParanoid; Q8SUZ5; -.
DR OrthoDB; 750182at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000000819; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11850; -; 1.
DR Gene3D; 3.40.50.11860; -; 1.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042264; DPH1/DPH2_2.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR InterPro; IPR035435; DPH1/DPH2_euk_archaea.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR PIRSF; PIRSF004967; DPH1; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..347
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 1"
FT /id="PRO_0000083374"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
SQ SEQUENCE 347 AA; 39759 MW; 4BEE0FB15C2DF5CA CRC64;
MVVLKQEEVP ECLRYLPRNY NFETGKVLRT IRRLGAKRVT LQFPDGLLRY SFVIMDVIEK
YTGAECILLN DVVYGGCCID DESIASDLLV HYGHSCLVPV GEMSTKVLYI FVDIRIDIDH
AAEMIRRNFQ GKIGVIGTIQ FNSSINRLKR VLDEERGGVE CTLPQIRPLS SGEVLGCTAP
KIEGVSAVIS IGDGRFHLEG AMIRNPHLRF YKYCPFSRRM TQESYDHSTM LSDRKSEIRK
AFSGRSFGVI LGSLGRQGNR SILRSVVDRL KEYDVYLIML DEISPKKLER YNFIDSFVQI
SCPRLSIDWG KLFKKPLLTP FEVFYSGGEY LMDYYSREGS GEWKNYR
