ID   DHYS_METKA              Reviewed;         297 AA.
AC   Q8TXD7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=MK0737;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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: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; AE009439; AAM01951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TXD7; -.
DR   SMR; Q8TXD7; -.
DR   STRING; 190192.MK0737; -.
DR   EnsemblBacteria; AAM01951; AAM01951; MK0737.
DR   KEGG; mka:MK0737; -.
DR   PATRIC; fig|190192.8.peg.777; -.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; EARSWGK; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001826; 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..297
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134496"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ   SEQUENCE   297 AA;  32475 MW;  489065D5A3131867 CRC64;
     MKRETFRYRG DMDLDGFLRE MERVGALGAG RLGRAARILE KMWSSDDVTV LLTVAGPAVA
     GGLGELFERL IREGLVDAVI TSGANVVHDA LDALGGIHVC LGERNVDGYG RVHDTHIPTE
     AFEKFEHFMR EVLSDLSGRV SCRELLWEMG KRLESGFLRA AADEGVPIYS PGILDSMVGL
     HVWIHSQDHD FHLDLVDDMH HLADLVFEAE ELGAIILGGS VPKHFAMGAA MLRGGLDYAV
     QITMDRPETG SLSGAPLEEG KSWEKVREDA EVATIVGDYL IIFPLLASGV MQRLGIV