ID   DHYS_SOLLC              Reviewed;         381 AA.
AC   Q9AXR0;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Deoxyhypusine synthase;
DE            EC=2.5.1.46;
GN   Name=DHS;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Match; TISSUE=Leaf;
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   -!- TISSUE SPECIFICITY: Expressed in open and senescing flowers, but barely
CC       detectable in flower buds. Very low in fruits, until they began to
CC       soften. Not detectable in cotyledons after 5 days of germination, but
CC       reached a peak by day 15 when the chlorophyll levels began to decline.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during senescence.
CC   -!- INDUCTION: Up-regulated by osmotic stress and chilling.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF296077; AAG53641.1; -; mRNA.
DR   RefSeq; NP_001234495.1; NM_001247566.1.
DR   AlphaFoldDB; Q9AXR0; -.
DR   SMR; Q9AXR0; -.
DR   STRING; 4081.Solyc02g080800.2.1; -.
DR   PaxDb; Q9AXR0; -.
DR   PRIDE; Q9AXR0; -.
DR   GeneID; 543666; -.
DR   KEGG; sly:543666; -.
DR   eggNOG; KOG2924; Eukaryota.
DR   HOGENOM; CLU_039781_0_0_1; -.
DR   InParanoid; Q9AXR0; -.
DR   OrthoDB; 883558at2759; -.
DR   PhylomeDB; Q9AXR0; -.
DR   BioCyc; MetaCyc:MON-13916; -.
DR   BRENDA; 2.5.1.46; 3101.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9AXR0; baseline.
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..381
FT                   /note="Deoxyhypusine synthase"
FT                   /id="PRO_0000134476"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..138
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         320..321
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         326..328
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..341
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..355
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  42127 MW;  22B87574FD882988 CRC64;
     MGEALKYSIM DSVRSVVFKE SENLEGSCTK IEGYDFNKGV NYAELIKSMV STGFQASNLG
     DAIAIVNQML DWRLSHELPT EDCSEEERDV AYRESVTCKI FLGFTSNLVS SGVRDTVRYL
     VQHRMVDVVV TTAGGIEEDL IKCLAPTYKG DFSLPGASLR SKGLNRIGNL LVPNDNYCKF
     ENWIIPVFDQ MYEEQINEKV LWTPSKVIAR LGKEINDETS YLYWAYKNRI PVFCPGLTDG
     SLGDMLYFHS FKKGDPDNPD LNPGLVIDIV GDIRAMNGEA VHAGLRKTGM IILGGGLPKH
     HVCNANMMRN GADFAVFINT AQEFDGSDSG ARPDEAVSWG KIRGGAKTVK VHCDATIAFP
     ILVAETFAAK SKEFSQIRCQ V