ID   DHYS_IGNH4              Reviewed;         319 AA.
AC   A8AA61;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Igni_0631;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU81813.1; -; Genomic_DNA.
DR   RefSeq; WP_011998665.1; NC_009776.1.
DR   AlphaFoldDB; A8AA61; -.
DR   SMR; A8AA61; -.
DR   STRING; 453591.Igni_0631; -.
DR   EnsemblBacteria; ABU81813; ABU81813; Igni_0631.
DR   GeneID; 5562987; -.
DR   KEGG; iho:Igni_0631; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   PhylomeDB; A8AA61; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000000262; 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..319
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_1000011351"
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ   SEQUENCE   319 AA;  35351 MW;  E62C35A6CE7A07D2 CRC64;
     MNREDFIKEP VEDIRVSERD TVADLIEKYC KVHGFTAADV CRAVEVLSEG LRNSDLRFLS
     FTANLVATGL RGLLAQMVRS GYFDVVVTTC GTLDHDVARS LGHKYYKGYF EADDVVLAKS
     DIHRLGNVFI PVENYGPPVE RLVKDVLREL GKTMVAPYEL IWEVGKRLSD ENSILRAAWE
     RKVPVIVPGI TDGAFGTAIF TYSEELKLQG KDFCLDVLAD EKLLSDMVFS SKRSAALVVG
     GGISKHHVIW WNQFKGGLDY AVYLTTAQEY DGSLSGARPR EAITWGKLKP EGRSATVYGD
     ATVLLPIIWA GVLAKVQKA