ID   DHYS_DIACA              Reviewed;         373 AA.
AC   Q9AXQ8;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Deoxyhypusine synthase;
DE            EC=2.5.1.46;
GN   Name=DHS;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower;
RX   PubMed=11278418; DOI=10.1074/jbc.m008544200;
RA   Wang T.-W., Lu L., Wang D., Thompson J.E.;
RT   "Isolation and characterization of senescence-induced cDNAs encoding
RT   deoxyhypusine synthase and eucaryotic translation initiation factor 5A from
RT   tomato.";
RL   J. Biol. Chem. 276:17541-17549(2001).
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;
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF296080; AAG53644.1; -; mRNA.
DR   AlphaFoldDB; Q9AXQ8; -.
DR   SMR; Q9AXQ8; -.
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..373
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134475"
FT   ACT_SITE        336
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         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         315..316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         321..323
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         330..336
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..350
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  41126 MW;  D410956C043B647C CRC64;
     MEDANHDSVA SAHSAAFKKS ENLEGKSVKI EGYDFNQGVN YSKLLQSFAS NGFQASNLGD
     AIEVVNHMLD WSLADEAPVD DCSEEERDPK FRESVKCKVF LGFTSNLISS GVRDTIRYLV
     QHHMVDVIVT TTGGIEEDLI KGRSIKCLAP TFKGDFALPG AQLRSKGLNR IGNLLVPNDN
     YCKFEDWIIP ILDKMLEEQI SEKILWTPSK LIGRLGREIN DESSYLYWAF KNNIPVFCPG
     LTDGSLGDML YFHSFRNPGL IVDVVQDIRA VNGEAVHAAP RKTGMIILGG GLPKHHICNA
     NMMRNGADYA VFINTAEEFD GSDSGARPDE AISWGKISGS AKTVKVHCDA TIAFPLLVAE
     TFAAKREKER KSC