DHYS_ASHGO
ID DHYS_ASHGO Reviewed; 382 AA.
AC Q75EW4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=DYS1; OrderedLocusNames=AAL036W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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;
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; AE016814; AAS50330.1; -; Genomic_DNA.
DR RefSeq; NP_982506.1; NM_207859.1.
DR AlphaFoldDB; Q75EW4; -.
DR SMR; Q75EW4; -.
DR STRING; 33169.AAS50330; -.
DR EnsemblFungi; AAS50330; AAS50330; AGOS_AAL036W.
DR GeneID; 4618497; -.
DR KEGG; ago:AGOS_AAL036W; -.
DR eggNOG; KOG2924; Eukaryota.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; Q75EW4; -.
DR OMA; FWSYFCQ; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000000591; Chromosome I.
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 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; Reference proteome; Transferase.
FT CHAIN 1..382
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134480"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 108..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 134..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139..140
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 329..330
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 335..337
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 344..350
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 363..364
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 41984 MW; B674D54C4066F144 CRC64;
MSNNDETVLG HLADHVFKHS GPIPESFVEV KGIDYSKPDA IDMRASDLIK SMKTMGFQAS
SLGQACDIID EMRAWRGKHI DELDEYSRKG SFDENGFQKS TIFLGYTSNL ISSGLRETLR
YLVQHNMVSA IVTTAGGVEE DIIKCLAPTY LGEFTLKGAA LRDKGMNRIG NLLVPNNNYC
KFEEWIVPIL DAMLAEQEAY VAQQGKDCLG VNTDVDSPIW TPSKLCDRLG KEINDESSVL
YWAHKNKIPV FCPAITDGSI GDMLFLHTFR ASPQQLRLDL VADIRKINSM SMEASQAGMI
ILGGGLIKHH IANACLMRNG ADYAVYINTG QEFDGSDAGA RPDEAVSWGK IKVEAKSVKV
YADVTTVFPL IVAATFANGK KN
