ID   DHYS_PYRAE              Reviewed;         292 AA.
AC   Q8ZT09;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Probable deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=dys; OrderedLocusNames=PAE3487;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64954.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZT09; -.
DR   SMR; Q8ZT09; -.
DR   STRING; 178306.PAE3487; -.
DR   EnsemblBacteria; AAL64954; AAL64954; PAE3487.
DR   KEGG; pai:PAE3487; -.
DR   PATRIC; fig|178306.9.peg.2626; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   InParanoid; Q8ZT09; -.
DR   OMA; FWSYFCQ; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000002439; 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.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT   CHAIN           1..292
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134503"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  31633 MW;  A284749D69B5DD7A CRC64;
     MREIIELYRK VGGFQALHVA EAYDVLKEAV EAADVRFLSF TGNLVATGLR EFIADAIRRR
     LFNVVVTTAG ALDHDIAKSM GAVYAPGSFD LDDVDLAAKG YHRLGNVVIK KEEYGPLVEK
     FILAHCEKLW GKTLATYELA YLLGAELPED SILGAAARAG AKVFVPGIVD GAVGTALMTC
     NDLARTKRGG SRAFIDVLKD EEELREIVHN SKKLAALIVG GGISKHHVIW WAQFKGGLDY
     VVYISTAVEY DGSLSGARPR EAISWGKVKP SAKSVFIFAD ATLVLPVLLK AL