ID   DHYS_HALSA              Reviewed;         330 AA.
AC   Q9HPX2;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Probable deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=dys; Synonyms=dhs; OrderedLocusNames=VNG_1432G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
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DR   EMBL; AE004437; AAG19745.1; -; Genomic_DNA.
DR   PIR; E84297; E84297.
DR   RefSeq; WP_010903042.1; NC_002607.1.
DR   AlphaFoldDB; Q9HPX2; -.
DR   SMR; Q9HPX2; -.
DR   STRING; 64091.VNG_1432G; -.
DR   PaxDb; Q9HPX2; -.
DR   EnsemblBacteria; AAG19745; AAG19745; VNG_1432G.
DR   GeneID; 5952974; -.
DR   KEGG; hal:VNG_1432G; -.
DR   PATRIC; fig|64091.14.peg.1095; -.
DR   HOGENOM; CLU_039781_0_0_2; -.
DR   InParanoid; Q9HPX2; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   PhylomeDB; Q9HPX2; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000000554; Chromosome.
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   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.
DR   TIGRFAMs; TIGR00321; dhys; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT   CHAIN           1..330
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134492"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  36381 MW;  AC24691133BEFC97 CRC64;
     MTGDDADETH ENVVPGSDED LDTPDVRGYD FSGEFDFFEL LDSYATTGFQ ASHLADAVDI
     TREMREDDAT IYLTLTSNIV SSGLREVVAH LVRENYVDVI ITTSGSLTED IIKTAKPFKM
     GEWDVDEAAL REEGINRLGN IFVPSDRYVW LEEYLYDFFE EFFADQKVRT PTAFARELGA
     TLDDEDSILK NAADNDIPVF CPALTDAEIG NFLYYYRQGY DSEVGIEILD DYDALIEEGL
     LADTTGLICV GAGVPKHHAI MTNLFRGGAD YAVYISTGME GDGSLSGAPP EEAVSWGKIK
     DEDAEPNYAL IEAEATLVFP LLVAGAFENP