DHYS_BOVIN
ID DHYS_BOVIN Reviewed; 369 AA.
AC Q6EWQ6; Q3MHI1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=DHPS; Synonyms=DYS;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=15354351; DOI=10.1080/10425170310001652174;
RA Huang J.K., Tsai S., Huang G.H., Sershon V.C., Alley A.M., Wen L.;
RT "Molecular cloning of bovine eIF5A and deoxyhypusine synthase cDNA.";
RL DNA Seq. 15:26-32(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine
CC and the subsequent transfer of the butylamine moiety of spermidine to
CC the epsilon-amino group of a critical lysine residue of the eIF-5A
CC precursor protein to form the intermediate deoxyhypusine residue. This
CC is the first step of the post-translational modification of that lysine
CC into an unusual amino acid residue named hypusine. Hypusination is
CC unique to mature eIF-5A factor and is essential for its function.
CC {ECO:0000250|UniProtKB:P49366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-
CC deoxyhypusine + propane-1,3-diamine; Xref=Rhea:RHEA:33299, Rhea:RHEA-
CC COMP:10143, Rhea:RHEA-COMP:10144, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:82657; EC=2.5.1.46;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; AJ577610; CAE12195.1; -; mRNA.
DR EMBL; BC105230; AAI05231.1; -; mRNA.
DR RefSeq; NP_001003657.1; NM_001003657.1.
DR AlphaFoldDB; Q6EWQ6; -.
DR SMR; Q6EWQ6; -.
DR STRING; 9913.ENSBTAP00000008200; -.
DR PaxDb; Q6EWQ6; -.
DR PRIDE; Q6EWQ6; -.
DR Ensembl; ENSBTAT00000008200; ENSBTAP00000008200; ENSBTAG00000006247.
DR GeneID; 444988; -.
DR KEGG; bta:444988; -.
DR CTD; 1725; -.
DR VEuPathDB; HostDB:ENSBTAG00000006247; -.
DR VGNC; VGNC:28038; DHPS.
DR eggNOG; KOG2924; Eukaryota.
DR GeneTree; ENSGT00390000008063; -.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; Q6EWQ6; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 883558at2759; -.
DR TreeFam; TF300625; -.
DR BRENDA; 2.5.1.46; 908.
DR Reactome; R-BTA-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000006247; Expressed in retina and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IBA:GO_Central.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0008216; P:spermidine metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.910.10; -; 1.
DR InterPro; IPR002773; Deoxyhypusine_synthase.
DR InterPro; IPR036982; Deoxyhypusine_synthase_sf.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR PANTHER; PTHR11703; PTHR11703; 1.
DR Pfam; PF01916; DS; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR TIGRFAMs; TIGR00321; dhys; 1.
PE 2: Evidence at transcript level;
KW Hypusine biosynthesis; NAD; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..369
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134468"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 131..133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 136..137
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 308..309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 323..329
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 342..343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT CONFLICT 12
FT /note="A -> P (in Ref. 1; CAE12195)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="M -> T (in Ref. 1; CAE12195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41029 MW; 9CA28A6AFDBD21FC CRC64;
MEGPQEREVP AAALAAVLKH SSALPFETAQ VRGYDFNRGV DYRALLEAFS TTGFQATNFG
RAVQQVNAMI EKKLEPLSED EDQHADLTQS RRPLTGCTIF LGYTSNLISS GIRETIRYLV
QHNMVDVLVT TAGGVEEDFI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNDNYCKFE
DWLMPILDQM VLEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VLSPALTDGS
LGDMIFFHSY KNPGLVLDIV EDLKLINTQA IFAKRTGMII LGGGMVKHHI ANANLMRNGA
DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RMDAQPVKVY ADASLVFPLL VAETFAQKVD
AFMPEKNED
