DHYS_SULIM
ID DHYS_SULIM Reviewed; 312 AA.
AC C3MYN2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
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=M1425_1256;
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001400; ACP38011.1; -; Genomic_DNA.
DR RefSeq; WP_012711264.1; NC_012588.1.
DR AlphaFoldDB; C3MYN2; -.
DR SMR; C3MYN2; -.
DR EnsemblBacteria; ACP38011; ACP38011; M1425_1256.
DR GeneID; 7814465; -.
DR GeneID; 8761185; -.
DR KEGG; sia:M1425_1256; -.
DR HOGENOM; CLU_039781_1_0_2; -.
DR OMA; FWSYFCQ; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001350; 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; Transferase.
FT CHAIN 1..312
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_1000203447"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00153"
SQ SEQUENCE 312 AA; 34946 MW; F47C7C3439B2D6E6 CRC64;
MINREDLLKN PVEDIALSDL EKYSDIVNVF DKIYGFSSEG IVRGSKILKE MIKDADLRFL
SFTANLVSTG LRGLFADLVK RGYFNIIVTT GGTIDHDLAR SFGGVYYKGS FDIDDAMLKD
LEIHRLGNVL VPFESYGKVI EEIVRKFLPE IAKDKKEIPA YELLWEFGKR ISDSNSILRA
AYEKKVPVIV PGIVDGSFGT NLFIQSQFLN FKINLFEDMR LIKDLVFSCK KSGALIIGGG
ISKHHTIWWN QFKDGLDYAV YVTTAQEYDG SLSGAKPREA ISWNKIRPNA KHATIYGDAT
IIVPILAASL LS