DHYS_SACS2
ID DHYS_SACS2 Reviewed; 312 AA.
AC Q97ZF1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Probable deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=dys; OrderedLocusNames=SSO0967;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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:0000250}.
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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK41241.1; -; Genomic_DNA.
DR PIR; B90248; B90248.
DR RefSeq; WP_009992414.1; NC_002754.1.
DR AlphaFoldDB; Q97ZF1; -.
DR SMR; Q97ZF1; -.
DR STRING; 273057.SSO0967; -.
DR EnsemblBacteria; AAK41241; AAK41241; SSO0967.
DR GeneID; 44129899; -.
DR KEGG; sso:SSO0967; -.
DR PATRIC; fig|273057.12.peg.966; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_1_0_2; -.
DR InParanoid; Q97ZF1; -.
DR OMA; FWSYFCQ; -.
DR PhylomeDB; Q97ZF1; -.
DR BRENDA; 2.5.1.46; 6163.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; IBA:GO_Central.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IBA:GO_Central.
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..312
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_0000134508"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 35050 MW; A9072CE18825A2D9 CRC64;
MINREDLLKN PVEDITLSDL KKYNDIVSVF DKIYGFSSEG IVNGSKILKE MIKNADLRFL
SFTANLVSTG LRGLFADLIK KGYFNIVVTT GGTIDHDLAR SFGGVYYKGS FDIDDTMLKD
LEIHRLGNVL VPFESYGKVI EDVVRKFLPE ITKDRKEISA YELLWEFGKR ITDSNSILRA
AYDKNVPIIV PGILDGSFGT NLFIQSQFLN FRINLFEDMR LIKDLIFSSK KSGALIIGGG
ISKHHTIWWN QFKDGLNYAI YITTAQEYDG SLSGAKPREA ISWNKIRPDA KHVTIYGDAT
IIVPILAASL LS