ID   DHYS_SULTO              Reviewed;         311 AA.
AC   Q971T3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Probable deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=dys; OrderedLocusNames=STK_12930;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(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.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
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; BA000023; BAB66337.1; -; Genomic_DNA.
DR   RefSeq; WP_010979315.1; NC_003106.2.
DR   AlphaFoldDB; Q971T3; -.
DR   SMR; Q971T3; -.
DR   STRING; 273063.STK_12930; -.
DR   EnsemblBacteria; BAB66337; BAB66337; STK_12930.
DR   GeneID; 1459295; -.
DR   KEGG; sto:STK_12930; -.
DR   PATRIC; fig|273063.9.peg.1454; -.
DR   eggNOG; arCOG04142; Archaea.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001015; 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; Reference proteome; Transferase.
FT   CHAIN           1..311
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134509"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  35303 MW;  0EF21510E2550CDA CRC64;
     MKREELLVEE IKDLTLEELK GYADFYKILD KVYGFTAESV VRGVKILKDM IKEADLRFLS
     FTANLVSTGL RGLFADLIKQ GYFNVIITTG GTIDHDIARS FGGKYYKGLF EYDDSMLREL
     EIHRLGNILV PMESYGKVIE DVVRKYMNEI VSIKKEWPVY ELLWEFGKRI SDENSILKAA
     YEKKVPIIVP GIIDGSFGTN LFIYSQFTQL KLNLFEDMKL IKDLIFSCKK SGALIIGGGI
     SKHHTIWWNQ FKDGLDYAIY ITTAQEYDGS LSGAKPREAI SWNKIKPTSE NVVIYGDATI
     ILPILSASLL G