DPH1_BOVIN
ID DPH1_BOVIN Reviewed; 438 AA.
AC Q3SYT1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE EC=2.5.1.108 {ECO:0000250|UniProtKB:Q5NCQ5};
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in elongation
CC factor 2 (By similarity). DPH1 and DPH2 transfer a 3-amino-3-
CC carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a
CC histidine residue, the reaction is assisted by a reduction system
CC comprising DPH3 and a NADH-dependent reductase (By similarity).
CC {ECO:0000250|UniProtKB:P40487, ECO:0000250|UniProtKB:Q5NCQ5}.
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:Q5NCQ5};
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 (By
CC similarity). Interacts with DPH2 and RBM8A.
CC {ECO:0000250|UniProtKB:P40487, ECO:0000250|UniProtKB:Q5NCQ5,
CC ECO:0000250|UniProtKB:Q9BZG8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5NCQ5,
CC ECO:0000250|UniProtKB:Q9BZG8}. Cytoplasm {ECO:0000250|UniProtKB:Q5NCQ5,
CC ECO:0000250|UniProtKB:Q9BZG8}. Note=Punctate, primarily perinuclear
CC localization. {ECO:0000250|UniProtKB:Q5NCQ5,
CC ECO:0000250|UniProtKB:Q9BZG8}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC103408; AAI03409.1; -; mRNA.
DR RefSeq; NP_001070367.1; NM_001076899.2.
DR AlphaFoldDB; Q3SYT1; -.
DR SMR; Q3SYT1; -.
DR STRING; 9913.ENSBTAP00000012340; -.
DR PaxDb; Q3SYT1; -.
DR PRIDE; Q3SYT1; -.
DR GeneID; 534099; -.
DR KEGG; bta:534099; -.
DR CTD; 1801; -.
DR eggNOG; KOG2648; Eukaryota.
DR InParanoid; Q3SYT1; -.
DR OrthoDB; 750182at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 PANTHER; PTHR10762; PTHR10762; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..438
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 1"
FT /id="PRO_0000307881"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 342
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5NCQ5"
SQ SEQUENCE 438 AA; 47978 MW; 4F9139327E1D26D4 CRC64;
MAALVAAEAA ESCSRNGPGR GRAPRGRLAN QIPAEILNNP QLQAAIQVLP SNYNFEVPKT
IWRIQQAQAK KVALQMPEGL LLFACTIVDI LERFTEAEVM VMGDVTYGAC CVDDFTARAL
GADFLVHYGH SCLVPMDTSA QDFRVLYVFV DIRIDTAHLL DSIRLTFPPA SALALVSTIQ
FVSTLQAAAQ ELKAEYRVSV PQCKPLSPGE ILGCTSPCLP KEVEAVVYLG DGRFHLESVM
IANPNISAYR YDPYSKVLSR EHYDHQRMQA NRQEAIATAR SAKSWGLILG TLGRQGSPKI
LEHLESRLQA LGLPFVRLLL SEIFPSKLSL LPEVDVWVQV ACPRLSIDWG TAFPKPLLTP
YEAAVALRDI SWQQPYPMDF YASSSLGPWT VNHGRDRLLQ VPGRLALGKV QGGPARPSPA
AACEACSCRD EEVSPIAL
