DHYS_HALS3
ID DHYS_HALS3 Reviewed; 330 AA.
AC B0R5L2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=OE_3059F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(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; AM774415; CAP14029.1; -; Genomic_DNA.
DR RefSeq; WP_010903042.1; NC_010364.1.
DR AlphaFoldDB; B0R5L2; -.
DR SMR; B0R5L2; -.
DR EnsemblBacteria; CAP14029; CAP14029; OE_3059F.
DR GeneID; 5952974; -.
DR KEGG; hsl:OE_3059F; -.
DR HOGENOM; CLU_039781_0_0_2; -.
DR OMA; FWSYFCQ; -.
DR PhylomeDB; B0R5L2; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001321; 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..330
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_1000096914"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ SEQUENCE 330 AA; 36381 MW; AC24691133BEFC97 CRC64;
MTGDDADETH ENVVPGSDED LDTPDVRGYD FSGEFDFFEL LDSYATTGFQ ASHLADAVDI
TREMREDDAT IYLTLTSNIV SSGLREVVAH LVRENYVDVI ITTSGSLTED IIKTAKPFKM
GEWDVDEAAL REEGINRLGN IFVPSDRYVW LEEYLYDFFE EFFADQKVRT PTAFARELGA
TLDDEDSILK NAADNDIPVF CPALTDAEIG NFLYYYRQGY DSEVGIEILD DYDALIEEGL
LADTTGLICV GAGVPKHHAI MTNLFRGGAD YAVYISTGME GDGSLSGAPP EEAVSWGKIK
DEDAEPNYAL IEAEATLVFP LLVAGAFENP
