ID   DHYS1_METMA             Reviewed;         317 AA.
AC   Q8PV89;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Probable deoxyhypusine synthase 1;
DE            Short=DHS 1;
DE            EC=2.5.1.46;
GN   Name=dys1; OrderedLocusNames=MM_2082;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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: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; AE008384; AAM31778.1; -; Genomic_DNA.
DR   RefSeq; WP_011034014.1; NC_003901.1.
DR   AlphaFoldDB; Q8PV89; -.
DR   SMR; Q8PV89; -.
DR   STRING; 192952.MM_2082; -.
DR   EnsemblBacteria; AAM31778; AAM31778; MM_2082.
DR   GeneID; 1480424; -.
DR   KEGG; mma:MM_2082; -.
DR   PATRIC; fig|192952.21.peg.2390; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; EARSWGK; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000000595; 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; Reference proteome; Transferase.
FT   CHAIN           1..317
FT                   /note="Probable deoxyhypusine synthase 1"
FT                   /id="PRO_0000134497"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  34422 MW;  883A44523FF28DF1 CRC64;
     MDFGASAKNL STPVKGAKIV PNMTVDELVK EYAGCAFGAG RLAEAVDIYY EMLASGKTTK
     FFGLAGAMTP AGMRNIIADL IRDGYIDVLV TTGANMVHDT VEALGLHHYK GSDCANDIQL
     RHECIDRIYD VYLPDQHFTD LEEFLQGVYS GLPQENLSIR QVLTEIGKNL DDDSSILKTA
     AEMGVPVYCP ALQDSVIGLQ AWLYKEGNPL HVDAFADMHE FMDICYGAES AGTMLLGGGV
     PKNYILQSML VTPRSFDYAI QLTMDRPETG GLSGATLDEA QSWGKVGEDA KSVTVYADST
     ITLPLIVSAV RTRLSKR