DHYS_THEGJ
ID DHYS_THEGJ Reviewed; 336 AA.
AC C5A5L0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=TGAM_1020;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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}.
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DR EMBL; CP001398; ACS33522.1; -; Genomic_DNA.
DR RefSeq; WP_015858636.1; NC_012804.1.
DR AlphaFoldDB; C5A5L0; -.
DR SMR; C5A5L0; -.
DR STRING; 593117.TGAM_1020; -.
DR PaxDb; C5A5L0; -.
DR EnsemblBacteria; ACS33522; ACS33522; TGAM_1020.
DR GeneID; 7988077; -.
DR KEGG; tga:TGAM_1020; -.
DR PATRIC; fig|593117.10.peg.1016; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_0_0_2; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 35308at2157; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001488; 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..336
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_1000203450"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ SEQUENCE 336 AA; 38115 MW; A6C4B8BE6C6C6212 CRC64;
MTEPKDIVLK ESEEVEGTPI EGPWLDEVSS LEEVLDYYER IGFQATHLGK AIEIWKKVEE
KRARGEEVRV FLGYTSNIIS SGLREIIAWL VKEGKVDVIV TTAGGIEEDF IKALKPFILG
DWNVNDALMR EKGINRIGNI FVPNDRYIEF EKYMIPFFER VLEIEKERGK PLTASEFIYE
MGRFMDEKLG KEKEKSVIYW AYKRNVPIFC PAITDGSIGD MLYFFKEERG DRELIIDIAN
DIVKLNNLAV TAKETASIIL GGSLPKHAII NANLFRGGTD YAIYVTTAIP WDGSLSGAPP
SEGVSWGKIR AKADYVEIWA DATLVFPLLV WKVMRS