DHYS_METS5
ID DHYS_METS5 Reviewed; 310 AA.
AC A4YHK6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Msed_1753;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(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}.
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DR EMBL; CP000682; ABP95908.1; -; Genomic_DNA.
DR RefSeq; WP_012021695.1; NC_009440.1.
DR AlphaFoldDB; A4YHK6; -.
DR SMR; A4YHK6; -.
DR STRING; 399549.Msed_1753; -.
DR EnsemblBacteria; ABP95908; ABP95908; Msed_1753.
DR GeneID; 5104753; -.
DR GeneID; 59457129; -.
DR KEGG; mse:Msed_1753; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_1_0_2; -.
DR OMA; FWSYFCQ; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000000242; 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.
PE 3: Inferred from homology;
KW Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_1000071529"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ SEQUENCE 310 AA; 35171 MW; A4AD94318DD44C03 CRC64;
MRREDILVEE VQDITLDDLR GSSLLEVYNK IYGFSAESIY RGSRILKRIV SECDLRFISF
TANLVSTGLR GLFADMIRRG YFNMVVTTGG TIDHDIARSF GGKYYKGSFE FSDEELRKIN
VHRLGNILIP FEDYGGMVEN AVNRILPPLV KEKREWSVYE LLWEFGKRIE DKHSILRAAY
ETNTPIIVPG VVDGSFGTNL FIQSQFTGLR INLFEDMRLI KDRVFSSKMA GALLIGGGIS
KHHTIWWNQF RDGLDYAVYL TTAQEFDGSL SGARPREAIS WNKIRENAEQ AVIYADATLA
LPILATSLIS
