ID   DHYS_BRANA              Reviewed;         368 AA.
AC   Q6RJS2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Deoxyhypusine synthase;
DE            EC=2.5.1.46;
GN   Name=DHS;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang T.-W., Wu W., Zhang C.-G., Thompson J.E.;
RT   "Suppression of deoxyhypusine synthase expression in canola using
RT   Agrobacterium tumefaciens-mediated transformation.";
RL   Submitted (DEC-2003) 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 specific lysine residue of the eIF-5A
CC       precursor protein to form the intermediate deoxyhypusine residue. Also
CC       able to produce homospermidine from putrescine (By similarity).
CC       {ECO:0000250}.
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; AY496434; AAR91928.1; -; mRNA.
DR   AlphaFoldDB; Q6RJS2; -.
DR   SMR; Q6RJS2; -.
DR   UniPathway; UPA00354; -.
DR   GO; GO:0034038; F:deoxyhypusine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-KW.
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; Transferase.
FT   CHAIN           1..368
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134474"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..136
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..310
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         315..317
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         324..330
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         343..344
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  41162 MW;  E8B62D427FF6C51F CRC64;
     MEEDRVLSSV HSTVFKESES LEGKCDKIEG YDFNQGVNYP KLLRSMLTTG FQASNLGDVI
     DVVNQMLEWR LSDETIAPED CSEEEKDPAY RESVKCKIFL GFTSNLVSSG VRETIRYLVQ
     HHMVDVIVTT TGGVEEDLIK CLAPTFKGDF SLPGAYLRSK GLNRIGNLLV PNDNYCKFED
     WIIPIFDQML KEQKEESVLW TPSKLLARLG KEINNESSYL YWAYKMNIPV FCRGLTDGSL
     GDMLYFHSFR TSGLVIDVVQ DIRAMNGEAV HATPRKTGMI ILGGGLPKHH ICNANMMRNG
     ADYAVFINTG QEFDGSDSGA RPDEAVSWGK IRGSAKTVKV YCDATIAFPL LVAETFASKR
     EQSCEHKT