ID   DHYS_PYRCJ              Reviewed;         295 AA.
AC   A3MVC9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Pcal_1171;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000561; ABO08596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MVC9; -.
DR   SMR; A3MVC9; -.
DR   STRING; 410359.Pcal_1171; -.
DR   EnsemblBacteria; ABO08596; ABO08596; Pcal_1171.
DR   KEGG; pcl:Pcal_1171; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; FWSYFCQ; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001431; 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..295
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_1000011353"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ   SEQUENCE   295 AA;  32193 MW;  E2D170672123BA7C CRC64;
     MREVVELYKR IGGFQALHVA QAYEVLKEAL GEADVRFFSF TGNLVATGLR EIIAEALRER
     LFNVVVTTAG ALDHDIAKAM GASYRPGSFD LDDYELAEKG LHRLGNVVIS REEYGPYVEK
     FVLQRCERLW GRSLATYELA EEFGRDLPED SILGAAARAG VKVFVPGIVD GAVGTALLTC
     NDLARVRRGG ARLVVDVLKD EEALREIVHG GKRLAALIVG GGISKHHVIW WAQFKGGLDY
     VVYISTAVEY DGSLSGARPR EAVSWGKVKP TAKSVYVYAD ATLVLPILLK ALCGK