DHYS_THEAC
ID DHYS_THEAC Reviewed; 310 AA.
AC Q9HL74;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Probable deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=dys; OrderedLocusNames=Ta0356;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445064; CAC11500.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048161540.1; NC_002578.1.
DR AlphaFoldDB; Q9HL74; -.
DR SMR; Q9HL74; -.
DR STRING; 273075.Ta0356; -.
DR EnsemblBacteria; CAC11500; CAC11500; CAC11500.
DR GeneID; 1455972; -.
DR KEGG; tac:Ta0356; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_1_0_2; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 35308at2157; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001024; 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_0000134510"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 34980 MW; DD9A8EC31A5DD904 CRC64;
MDRKELLSRP VRDLSITADT RLGDLMDQFS SIGGFTAAKI HEAYEIIKDM FSEDNTTFLS
FPADIISTGL RGLINEVVKR KLVDVIITTS GTLDHDIART YRNYYCGSFS YSDIELRDLG
INRLGNVLVP DESYGEIIEE KVMESLEKLY AKKKEWATVD LIHEVGLDIN SESSIIYNAA
KNNIPVFVPG ITDGSFGSQL WSFYEQHHDF KINLLEDEHR LSDIIFDAKK TGAIMIGGGI
SKHHTIWWNQ FRDGLDYAVY VTTAQEYDGS LSGAKLEEAI SWKKVRPDAR YVNVYGDATV
IMPVLLAPFL