DHYS_THEON
ID DHYS_THEON Reviewed; 335 AA.
AC B6YVB1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=TON_0701;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000855; ACJ16189.1; -; Genomic_DNA.
DR RefSeq; WP_012571661.1; NC_011529.1.
DR AlphaFoldDB; B6YVB1; -.
DR SMR; B6YVB1; -.
DR STRING; 523850.TON_0701; -.
DR PRIDE; B6YVB1; -.
DR EnsemblBacteria; ACJ16189; ACJ16189; TON_0701.
DR GeneID; 7017002; -.
DR KEGG; ton:TON_0701; -.
DR PATRIC; fig|523850.10.peg.704; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_0_0_2; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 35308at2157; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000002727; 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; Transferase.
FT CHAIN 1..335
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_1000096915"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ SEQUENCE 335 AA; 38173 MW; 2DC7DABC7DA9EBE7 CRC64;
MTEPKDIVLK ESEEIEGTPI EGPWLDEVRI LEEVIDYYHR IGFQATHLGR AIEIWKKVEE
KRASGEEVRV FLGYTSNIVS SGLRELIAWL VKEGKVDVIV TTAGGVEEDF IKALKPFILG
DWYVNDAEMR EKGINRIGNI FVPNDRYIEF EKYMIPFFER VLEMEKERGK PLTASEFIYE
MGRFMDEKLG KEKERSIIYW AYKRNVPIFC PAITDGSIGD MLYFFKEERG DRELIIDVAN
DIVKLNNLAV TAKETASIIL GGSLPKHAII NANLFRGGTD YAIYVTTAIP WDGSLSGAPP
SEGVSWGKIR AKADYVEIWA DATLVFPVLV WKVMR