ID   DHYS_AERPE              Reviewed;         310 AA.
AC   Q9YE72;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Probable deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=dys; OrderedLocusNames=APE_0698.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA79674.2; -; Genomic_DNA.
DR   PIR; B72659; B72659.
DR   AlphaFoldDB; Q9YE72; -.
DR   SMR; Q9YE72; -.
DR   STRING; 272557.APE_0698.1; -.
DR   PRIDE; Q9YE72; -.
DR   EnsemblBacteria; BAA79674; BAA79674; APE_0698.1.
DR   KEGG; ape:APE_0698.1; -.
DR   PATRIC; fig|272557.25.peg.501; -.
DR   eggNOG; arCOG04142; Archaea.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000002518; 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..310
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134489"
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33845 MW;  30AABF21D3620C39 CRC64;
     MEEVRDCRLE EGLSVEGLVE CYRDIHGFMA GHLAEAVEVL REGLEASSVR VLTFTGNLVA
     TGLRGVLAQL IDGGLFNVVF TTAGALDHDI ARFMGGKYLK GRFEADDTEL HRRGVHRLGN
     VFIPVESYGP LVERFVRTLA EQAAGVRGEW GVYELLRLAG SLMEGDRDSI LAAAARRGVD
     VFVPGWPDGA FGTSLFMERQ RGTSITVDYF RDMARLADIF FPQEGEAAAL IVGGGISKHH
     AIWWSQFRGG LDYAVYVTTA VEYDGSLSGA HPREAVSWGK IKESSRRVVV YGDATITLPV
     IAYCLLHGCG