ID   DPH1_XENLA              Reviewed;         439 AA.
AC   Q6GPQ5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 58.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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.
CC       {ECO:0000250|UniProtKB:P40487}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5NCQ5}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q5NCQ5}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH73057.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; BC073057; AAH73057.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6GPQ5; -.
DR   SMR; Q6GPQ5; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000186698; Genome assembly.
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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..439
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 1"
FT                   /id="PRO_0000307886"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         216
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         344
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
SQ   SEQUENCE   439 AA;  49004 MW;  C9A407F0D9671839 CRC64;
     MEPERNESGT PSVAVTPAAP INAGRAPVRR VANQIPDEIA HNPLLLEAMK VLPENYNFEI
     PKTIWRIQQA SAKRVALQMP EGLLMFACAI ADIIERFTSA ETVVMGDVTY GACCVDDYTA
     QALGADFMVH YGHSCLIPID ATHGVRMLYV FVDIKIDTSH FVDTIRFNFQ AGASLALVST
     VQFVSALQAA RQALQTDYNV TVPQCKPLSP GEILGCTSPR LNKSVDAVVY LGDGRFHLES
     VMISNPDTKA YRYDPYSKVF SREYYDHSTM LRHRGEAISV ATNAKTWGLI LGTLGRQGSP
     KIMEHLESRL QALGCRYVRL LLSEIFPNKL KLFAEVEVWV QVACPRLSID WGTAFSKPLL
     TPYEASVALK EAEWQLTYPM DFYANESLGP WTVNHESHRP TRATVRRTQK PEQRKLQCTD
     VGATVEECPC QEKVETKTE