ID   DHYS2_ARCFU             Reviewed;         298 AA.
AC   O27984;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Probable deoxyhypusine synthase 2;
DE            Short=DHS 2;
DE            EC=2.5.1.46;
GN   Name=dys2; OrderedLocusNames=AF_2300;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB88953.1; -; Genomic_DNA.
DR   PIR; D69537; D69537.
DR   RefSeq; WP_010879789.1; NC_000917.1.
DR   AlphaFoldDB; O27984; -.
DR   SMR; O27984; -.
DR   STRING; 224325.AF_2300; -.
DR   EnsemblBacteria; AAB88953; AAB88953; AF_2300.
DR   GeneID; 1485532; -.
DR   KEGG; afu:AF_2300; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; YTSSPGD; -.
DR   OrthoDB; 35308at2157; -.
DR   PhylomeDB; O27984; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000002199; 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..298
FT                   /note="Probable deoxyhypusine synthase 2"
FT                   /id="PRO_0000134491"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  33015 MW;  E9E7ADE0C751E33B CRC64;
     MARTGFQGRK LGEAFEIWTE MLREENITIL MGLSGAMVPA GMRKIIAWLI RNRYIDVLVS
     TGANLFHDIH EAMGFRHFMG SEHVNDCKLF EEGIDRIHDV FAYEKEFNVI DYTLAEIISE
     MSGVMSSREF LEEIAGRLNV KDRNSIVIAA YESKVPIFSP AIADSSIGIA AALAKREVVI
     DTIRDVEELT EIVVNSEKTG VIYVGGGVPK NFIQQTEVVA RLKGYDVRGH EYAIQITTDV
     PQFGGLSGCT FEEGVSWGKI SGKAKKVQVN CDATIALPVL AHGLIGIRRQ KYPIFNGL