ID   DHYS_METVS              Reviewed;         335 AA.
AC   A6URC0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Mevan_1142;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-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; CP000742; ABR55042.1; -; Genomic_DNA.
DR   RefSeq; WP_012065957.1; NC_009634.1.
DR   AlphaFoldDB; A6URC0; -.
DR   SMR; A6URC0; -.
DR   STRING; 406327.Mevan_1142; -.
DR   EnsemblBacteria; ABR55042; ABR55042; Mevan_1142.
DR   GeneID; 5325756; -.
DR   KEGG; mvn:Mevan_1142; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_0_0_2; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001107; 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.
DR   TIGRFAMs; TIGR00321; dhys; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; NAD; Transferase.
FT   CHAIN           1..335
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_1000011352"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ   SEQUENCE   335 AA;  37875 MW;  4B888F17B2164264 CRC64;
     MSDPKNVIFK ESECLEGIFI EGPDFDKDID LKAVLTDYYE KIGFQATHLG KAVKIWKKIE
     KLKKEEEMVV FLGYTSNMVS SGLRELISYL VRHKKVDVLV TTAGGIEEDF IKCIKPFVLG
     DWNLNGAILR EKGINRIGNV FVPNDRYIEF ETYMTRFFDI LSKKQNSENK ILSASEFCFE
     LGKFMDENLG NEKEKSIVYH AYKNKIPIFC PAITDGSIGD MLYFYKKNEK DGNLLIDVAN
     DIVKLNDMAI DANKTACIVL GGSLPKHSII NANLFREGTD YAIYITTAIP WDGSLSGAPP
     EEGVSWGKIQ EKADFVEIWA DATIVFPMLV YGVFK