ID F1MGR8_BOVIN Unreviewed; 438 AA.
AC F1MGR8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000256|ARBA:ARBA00021915};
DE EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221};
DE AltName: Full=Diphthamide biosynthesis protein 1 {ECO:0000256|ARBA:ARBA00032574};
DE AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000256|ARBA:ARBA00032789};
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000256|ARBA:ARBA00031690};
GN Name=DPH1 {ECO:0000313|Ensembl:ENSBTAP00000012340.2,
GN ECO:0000313|VGNC:VGNC:28178};
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 {ECO:0000313|Ensembl:ENSBTAP00000012340.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000012340.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012340.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000012340.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012340.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001323};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010173}.
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DR AlphaFoldDB; F1MGR8; -.
DR SMR; F1MGR8; -.
DR Ensembl; ENSBTAT00000012340.3; ENSBTAP00000012340.2; ENSBTAG00000009376.4.
DR VEuPathDB; HostDB:ENSBTAG00000009376; -.
DR VGNC; VGNC:28178; DPH1.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_037146_1_2_1; -.
DR InParanoid; F1MGR8; -.
DR OMA; PGQVLGC; -.
DR TreeFam; TF105746; -.
DR Reactome; R-BTA-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000009376; Expressed in adenohypophysis and 105 other cell types or tissues.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IBA:GO_Central.
DR Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1.
DR Gene3D; 3.40.50.11850; Diphthamide synthesis DPH1/DPH2 domain 2; 1.
DR Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 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 NCBIfam; TIGR00322; diphth2_R; 1.
DR PANTHER; PTHR10762:SF1; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 1; 1.
DR PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 438 AA; 47950 MW; 5D8316E27CE008C9 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 NRQEAIATAQ SAKSWGLILG TLGRQGSPKI
LEHLESRLQA LGLPFVRLLL SEIFPSKLSL LPEVDVWVQV ACPRLSIDWG TAFPKPLLTP
YEAAVALRDI SWQQPYPMDF YASSSLGPWT VNHGRDRLLQ VPGRLALGKV QGGPARPSPA
AACEACSCRD EEVSPIAL
//
