ID   DHYS_TOBAC              Reviewed;         379 AA.
AC   Q9SC80;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Deoxyhypusine synthase;
DE            EC=2.5.1.46;
GN   Name=DHS1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=10542236; DOI=10.1074/jbc.274.45.32040;
RA   Ober D., Hartmann T.;
RT   "Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and
RT   bacterial expression of an enzyme with extended substrate specificity.";
RL   J. Biol. Chem. 274:32040-32047(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   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ242017; CAB62400.1; -; mRNA.
DR   RefSeq; NP_001312549.1; NM_001325620.1.
DR   AlphaFoldDB; Q9SC80; -.
DR   SMR; Q9SC80; -.
DR   STRING; 4097.Q9SC80; -.
DR   PRIDE; Q9SC80; -.
DR   GeneID; 107796463; -.
DR   KEGG; ag:CAB62400; -.
DR   KEGG; nta:107796463; -.
DR   BioCyc; MetaCyc:MON-13914; -.
DR   BRENDA; 2.5.1.46; 3645.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034038; F:deoxyhypusine synthase activity; IBA:GO_Central.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..379
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134479"
FT   ACT_SITE        339
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         293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         318..319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         324..326
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         333..339
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         352..353
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42083 MW;  90D17971CC6341B2 CRC64;
     MGEALNVMES VRSIVFKESE NLEGSATKIE GYDFNKGVNY AELFKSMAST GFQAANLGDA
     IQIVNQMLDW RLSHEQPMED CSEEERDVAY RESVTCKIFL GFTSNLVSSG VRDTIRYLVQ
     HRMVDVVVTT AGGIEEDLIK CLAPTYKGDF SLPGAVLRSK GLNRIGNLLV PNDNYCKFEN
     WIIPIFDQMY EEQIKEKVLW TPSKVIARLA KEINDETSYL YWAYKNRIPV FCPGLTDGSL
     GDMLYFHSFK KGDPDNPDLN PGLIIDIVGD IRAMNSEAVH AGSRKTGMII LGGGLPKHHV
     CNANMMRNGA DFAVYINTAQ EFDGSDSGAR PDEAVSWGKI RGGAKTVKVH CDATIAFPIL
     VAETFAAKRK ELSHIRCQV