DHYS_YEAST
ID DHYS_YEAST Reviewed; 387 AA.
AC P38791; D3DL17;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Deoxyhypusine synthase {ECO:0000303|PubMed:8612813};
DE Short=DHS {ECO:0000303|PubMed:8612813};
DE EC=2.5.1.46 {ECO:0000269|PubMed:7629166};
GN Name=DYS1 {ECO:0000303|PubMed:8612813}; OrderedLocusNames=YHR068W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=131;
RX PubMed=8612813; DOI=10.1016/0014-5793(96)00310-9;
RA Sasaki K., Abid M.R., Miyazaki M.;
RT "Deoxyhypusine synthase gene is essential for cell viability in the yeast
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 384:151-154(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=7629166; DOI=10.1074/jbc.270.31.18408;
RA Kang K.R., Wolff E.C., Park M.H., Folk J.E., Chung S.I.;
RT "Identification of YHR068w in Saccharomyces cerevisiae chromosome VIII as a
RT gene for deoxyhypusine synthase. Expression and characterization of the
RT enzyme.";
RL J. Biol. Chem. 270:18408-18412(1995).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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:0000269|PubMed:7629166, ECO:0000269|PubMed:8612813}.
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:0000269|PubMed:7629166};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC {ECO:0000269|PubMed:7629166}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7629166}.
CC -!- INTERACTION:
CC P38791; P23301: HYP2; NbExp=4; IntAct=EBI-5871, EBI-9033;
CC -!- MISCELLANEOUS: Present with 7600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; D78185; BAA11253.1; -; Genomic_DNA.
DR EMBL; U00061; AAB68377.1; -; Genomic_DNA.
DR EMBL; AY558282; AAS56608.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06761.1; -; Genomic_DNA.
DR PIR; S46698; S46698.
DR RefSeq; NP_011935.1; NM_001179198.1.
DR AlphaFoldDB; P38791; -.
DR SMR; P38791; -.
DR BioGRID; 36500; 115.
DR DIP; DIP-2788N; -.
DR IntAct; P38791; 7.
DR MINT; P38791; -.
DR STRING; 4932.YHR068W; -.
DR iPTMnet; P38791; -.
DR MaxQB; P38791; -.
DR PaxDb; P38791; -.
DR PRIDE; P38791; -.
DR EnsemblFungi; YHR068W_mRNA; YHR068W; YHR068W.
DR GeneID; 856465; -.
DR KEGG; sce:YHR068W; -.
DR SGD; S000001110; DYS1.
DR VEuPathDB; FungiDB:YHR068W; -.
DR eggNOG; KOG2924; Eukaryota.
DR GeneTree; ENSGT00390000008063; -.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; P38791; -.
DR OMA; FWSYFCQ; -.
DR BioCyc; YEAST:YHR068W-MON; -.
DR Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:P38791; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38791; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; IDA:SGD.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IDA:SGD.
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 1: Evidence at protein level;
KW Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134488"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 108..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 134..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 139..140
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 262
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 309
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 329..330
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 335..337
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 344..350
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P49366"
FT BINDING 363..364
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49366"
SQ SEQUENCE 387 AA; 42892 MW; 330BE1F5BF305F46 CRC64;
MSDINEKLPE LLQDAVLKAS VPIPDDFVKV QGIDYSKPEA TNMRATDLIE AMKTMGFQAS
SVGTACEIID SMRSWRGKHI DELDDHEKKG CFDEEGYQKT TIFMGYTSNL ISSGVRETLR
YLVQHKMVDA VVTSAGGVEE DLIKCLAPTY LGEFALKGKS LRDQGMNRIG NLLVPNDNYC
KFEEWIVPIL DKMLEEQDEY VKKHGADCLE ANQDVDSPIW TPSKMIDRFG KEINDESSVL
YWAHKNKIPI FCPSLTDGSI GDMLFFHTFK ASPKQLRVDI VGDIRKINSM SMAAYRAGMI
ILGGGLIKHH IANACLMRNG ADYAVYINTG QEYDGSDAGA RPDEAVSWGK IKAEAKSVKL
FADVTTVLPL IVAATFASGK PIKKVKN
