ID   DHYS_SULIL              Reviewed;         312 AA.
AC   C3MPN8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Probable deoxyhypusine synthase {ECO:0000255|HAMAP-Rule:MF_00153};
DE            Short=DHS {ECO:0000255|HAMAP-Rule:MF_00153};
DE            EC=2.5.1.46 {ECO:0000255|HAMAP-Rule:MF_00153};
GN   Name=dys {ECO:0000255|HAMAP-Rule:MF_00153}; OrderedLocusNames=LS215_1343;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00153}.
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:0000255|HAMAP-Rule:MF_00153};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00153};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC       Rule:MF_00153}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00153}.
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DR   EMBL; CP001399; ACP35351.1; -; Genomic_DNA.
DR   RefSeq; WP_012711264.1; NC_012589.1.
DR   AlphaFoldDB; C3MPN8; -.
DR   SMR; C3MPN8; -.
DR   EnsemblBacteria; ACP35351; ACP35351; LS215_1343.
DR   GeneID; 7814465; -.
DR   GeneID; 8761185; -.
DR   KEGG; sis:LS215_1343; -.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001747; Chromosome.
DR   GO; GO:0034038; F:deoxyhypusine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.910.10; -; 1.
DR   HAMAP; MF_00153; DHS; 1.
DR   InterPro; IPR022899; Deoxyhypus_synthase_arc.
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.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; NAD; Transferase.
FT   CHAIN           1..312
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_1000203446"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ   SEQUENCE   312 AA;  34946 MW;  F47C7C3439B2D6E6 CRC64;
     MINREDLLKN PVEDIALSDL EKYSDIVNVF DKIYGFSSEG IVRGSKILKE MIKDADLRFL
     SFTANLVSTG LRGLFADLVK RGYFNIIVTT GGTIDHDLAR SFGGVYYKGS FDIDDAMLKD
     LEIHRLGNVL VPFESYGKVI EEIVRKFLPE IAKDKKEIPA YELLWEFGKR ISDSNSILRA
     AYEKKVPVIV PGIVDGSFGT NLFIQSQFLN FKINLFEDMR LIKDLVFSCK KSGALIIGGG
     ISKHHTIWWN QFKDGLDYAV YVTTAQEYDG SLSGAKPREA ISWNKIRPNA KHATIYGDAT
     IIVPILAASL LS