ID   DHYS_MUSAC              Reviewed;         376 AA.
AC   Q9AXQ9;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Deoxyhypusine synthase;
DE            EC=2.5.1.46;
GN   Name=DHS;
OS   Musa acuminata (Banana) (Musa cavendishii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=4641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
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; AF296079; AAG53643.1; -; mRNA.
DR   AlphaFoldDB; Q9AXQ9; -.
DR   SMR; Q9AXQ9; -.
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..376
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134477"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..144
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         317..318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         323..325
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..338
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         351..352
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41585 MW;  232066CE839A04A3 CRC64;
     MEGGAAGGQR DRETLDAVRS VVFKPSVSLE EKRFPRVQGY DFNRGCDLIG LLDSISSTGF
     QASNLGDAID VINQMIDWRL SHDAPTEDCS EEERNLAYRQ SVTCKIFLGF TSNLVSSGIR
     EIIRFLVQHR MVEVLVTTAG GIEEDLIKCL APTYKGDFSL PGSYLRSKGL NRIGNLLVPN
     DNYCKFEDWI MPILDQMLLE QTTENVVWTP SKVIARLGKE INDESSYLYW AYKNNVSVYC
     PALTDGSLGD MLYCHSVRNP GLLIDIVQDI RAMNGEAVHV GLRKTGVIIL GGGLPKHHIC
     NANMFRNGAD YAVYVNTAQE FDGSDSGAEP DEAISWGKIK GSAKTIKVHC DATIAFPLLV
     AATFARKFQE RNNKLA