ID   DHYS_CAEEL              Reviewed;         371 AA.
AC   Q9XXJ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Deoxyhypusine synthase {ECO:0000250|UniProtKB:P49366};
DE            Short=DHS {ECO:0000250|UniProtKB:P49366};
DE            EC=2.5.1.46 {ECO:0000250|UniProtKB:P49366};
GN   Name=dhps-1 {ECO:0000312|WormBase:Y17G7B.4};
GN   ORFNames=Y17G7B.4 {ECO:0000312|WormBase:Y17G7B.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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 critical lysine residue of the eIF-5A
CC       precursor protein to form the intermediate deoxyhypusine residue. This
CC       is the first step of the post-translational modification of that lysine
CC       into an unusual amino acid residue named hypusine. Hypusination is
CC       unique to mature eIF-5A factor and is essential for its function.
CC       {ECO:0000250|UniProtKB:P49366}.
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         Evidence={ECO:0000250|UniProtKB:P49366};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:P49366};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000250|UniProtKB:P49366}.
CC   -!- INTERACTION:
CC       Q9XXJ0; P34563: iff-1; NbExp=3; IntAct=EBI-322139, EBI-327278;
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AL023828; CAA19451.1; -; Genomic_DNA.
DR   PIR; T26497; T26497.
DR   RefSeq; NP_496557.1; NM_064156.3.
DR   AlphaFoldDB; Q9XXJ0; -.
DR   SMR; Q9XXJ0; -.
DR   BioGRID; 40144; 4.
DR   DIP; DIP-27454N; -.
DR   IntAct; Q9XXJ0; 2.
DR   STRING; 6239.Y17G7B.4; -.
DR   EPD; Q9XXJ0; -.
DR   PaxDb; Q9XXJ0; -.
DR   PeptideAtlas; Q9XXJ0; -.
DR   EnsemblMetazoa; Y17G7B.4.1; Y17G7B.4.1; WBGene00012460.
DR   GeneID; 174840; -.
DR   KEGG; cel:CELE_Y17G7B.4; -.
DR   UCSC; Y17G7B.4; c. elegans.
DR   CTD; 174840; -.
DR   WormBase; Y17G7B.4; CE19037; WBGene00012460; dhps-1.
DR   eggNOG; KOG2924; Eukaryota.
DR   GeneTree; ENSGT00390000008063; -.
DR   HOGENOM; CLU_039781_0_0_1; -.
DR   InParanoid; Q9XXJ0; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 883558at2759; -.
DR   PhylomeDB; Q9XXJ0; -.
DR   Reactome; R-CEL-204626; Hypusine synthesis from eIF5A-lysine.
DR   SignaLink; Q9XXJ0; -.
DR   UniPathway; UPA00354; -.
DR   PRO; PR:Q9XXJ0; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00012460; Expressed in germ line (C elegans) and 4 other tissues.
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   1: Evidence at protein level;
KW   Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT   CHAIN           1..371
FT                   /note="Deoxyhypusine synthase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000134471"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         112..116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         138..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         143..144
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         250
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         296
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         316..317
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         322..324
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         331..337
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         350..351
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
SQ   SEQUENCE   371 AA;  40468 MW;  5CF01303045AC89F CRC64;
     MSTNEAAASQ EDIALAQGAV LVKSCQVPDG SIPIRGFDFS TASGPDFSLS AILSSYMSTG
     FQATHLAQAI QQVNQMLSLR DTPLTCDDDE KLFPYPEGRQ KRSCTIFLGY TSNLVTSGLR
     EVLRYCVQRN LVDCIVTSAG GIEEDLIKCL KPSYLGTFTM DGAKLRSNGM NRAGNVLIPN
     DNYCAFEDWL MPILDECLVE QEEKHLNWTP SKLIQRLGER IGDESSILYW AAKHRIPVFC
     PALTDGSLGD MLYFHSVKSS PGLRVDIVED VRHINTIAVK SFKTGSIILG GGVVKHHINN
     ANLMRNGADH TVYINTGQEF DGSDSGAQPD EAVSWGKVKP SAGAVKVHAE ATLVFPLLVA
     ETFAKHEGHK D