ID   DHYS_SENVE              Reviewed;         371 AA.
AC   Q9SC14;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=DHS1;
OS   Senecio vernalis (Spring groundsel).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Senecioneae;
OC   Senecioninae; Senecio.
OX   NCBI_TaxID=93496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10611289; DOI=10.1073/pnas.96.26.14777;
RA   Ober D., Hartmann T.;
RT   "Homospermidine synthase, the first pathway-specific enzyme of
RT   pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14777-14782(1999).
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.
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   -!- TISSUE SPECIFICITY: Expressed in shoot tips.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ238622; CAB65461.1; -; mRNA.
DR   AlphaFoldDB; Q9SC14; -.
DR   SMR; Q9SC14; -.
DR   KEGG; ag:CAB65461; -.
DR   BRENDA; 2.5.1.46; 5675.
DR   SABIO-RK; Q9SC14; -.
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..371
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134478"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..139
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         312..313
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         318..320
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         327..333
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         346..347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  41387 MW;  6E2AA956E6629CEE CRC64;
     MEESMKQASV MENLRSVVFK ESESLEGTCA KIRGYDFNNG IDYSQILKSM VSTGFQASNL
     GDAIETVNQM LDWRLSHEQV TEDCSQEEKN PTYRESIKCK IFLGFTSNLI SSGVRDIIRY
     LVQHHMVDVI VTTTGGIEED LIKCLADTFK GEFSLPGAEL RSKGLNRIGN LLVPNDNYCK
     FEDWIIPIFD QMLEEQKAKN VLWTPSKLIM RLGKEINNES SYLYWAYKND IPVFCPGLTD
     GSLGDMLYFH TFRNPGLIVD VVQDIRAINS EAVHANPRKT GMIILGGGLP KHHICNANMM
     RNGADYAVFI NTAQEFDGSD SGARPDEAVS WGKIRGSAKS VKVHCDATIA FPLLVAETFA
     AKREQSAEPS S