ID   DHYS2_METMA             Reviewed;         345 AA.
AC   Q8Q051;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Probable deoxyhypusine synthase 2;
DE            Short=DHS 2;
DE            EC=2.5.1.46;
GN   Name=dys2; OrderedLocusNames=MM_0287;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM29983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM29983.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015410997.1; NC_003901.1.
DR   AlphaFoldDB; Q8Q051; -.
DR   SMR; Q8Q051; -.
DR   STRING; 192952.MM_0287; -.
DR   EnsemblBacteria; AAM29983; AAM29983; MM_0287.
DR   GeneID; 44086518; -.
DR   GeneID; 66134982; -.
DR   KEGG; mma:MM_0287; -.
DR   PATRIC; fig|192952.21.peg.354; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; YTSSPGD; -.
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..345
FT                   /note="Probable deoxyhypusine synthase 2"
FT                   /id="PRO_0000134498"
FT   ACT_SITE        292
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   345 AA;  38042 MW;  8772506516B76A9D CRC64;
     MHHNVFTNTP TIPIDVKDRS VSELMDGMLR TGFQGRKLAE SVQAWSNMLK EKDTTVLMGL
     SGAMVPAGMR RVISYLIRER MIDCLVSTGA NLFHDSHEAL GRKHYVGSHL ANDEKLFEHG
     VDRIYDVFAV EEEFRNADNL IADFAEEIGE ISCSSREFMY LLGKELVRRG AAEDSIVVSA
     YRHNVPIFVP ALSDSSIGIG LTIARRRGLK LEIDQIKDVD EITQIVEKSG HTGVVYVGGG
     VPKNFIQQTE VIASILGMDV PGHEYAIQYT SDSPHWGGLS GCTFDEAVSW GKVAAQAKKV
     QVFVDATIAL PIVAHALHEK TRGVKRTAPV FSWDGPEGLE IAYNE