DHYS_RAT
ID DHYS_RAT Reviewed; 369 AA.
AC Q6AY53;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=Dhps;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 critical lysine residue of the eIF-5A
CC precursor protein to form the intermediate deoxyhypusine residue. This
CC is the first step of the post-translational modification of that lysine
CC into an unusual amino acid residue named hypusine. Hypusination is
CC unique to mature eIF-5A factor and is essential for its function.
CC {ECO:0000250|UniProtKB:P49366}.
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; BC079188; AAH79188.1; -; mRNA.
DR RefSeq; NP_001004207.1; NM_001004207.1.
DR AlphaFoldDB; Q6AY53; -.
DR SMR; Q6AY53; -.
DR IntAct; Q6AY53; 1.
DR MINT; Q6AY53; -.
DR STRING; 10116.ENSRNOP00000005656; -.
DR BindingDB; Q6AY53; -.
DR ChEMBL; CHEMBL2539; -.
DR jPOST; Q6AY53; -.
DR PaxDb; Q6AY53; -.
DR PRIDE; Q6AY53; -.
DR Ensembl; ENSRNOT00000005656; ENSRNOP00000005656; ENSRNOG00000004219.
DR GeneID; 288923; -.
DR KEGG; rno:288923; -.
DR CTD; 1725; -.
DR RGD; 1303326; Dhps.
DR eggNOG; KOG2924; Eukaryota.
DR GeneTree; ENSGT00390000008063; -.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; Q6AY53; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 883558at2759; -.
DR PhylomeDB; Q6AY53; -.
DR TreeFam; TF300625; -.
DR Reactome; R-RNO-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q6AY53; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000004219; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q6AY53; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0046203; P:spermidine catabolic process; IDA:RGD.
DR GO; GO:0008216; P:spermidine metabolic process; ISO:RGD.
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 2: Evidence at transcript level;
KW Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134470"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 131..133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 136..137
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 308..309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 323..329
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 342..343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 40705 MW; 8707A21A9E8D5202 CRC64;
MEGTPSGAAP SSALAAVLKH SSALPPESAQ VQGYDFNRGV DYHALLEAYG TTGFQATNFG
RAVQQVNAMI EKKLEPLAVD EDHHEDLTQS RRPLTGCTIF LGYTSNLISS GIRETIRYLV
QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNDNYCKFE
DWLMPILDQM VQEQNTEGVK WTPSKMISRL GKEINNPESV YYWAHKNHIP VLSPALTDGS
LGDMIFFHSY KNPGLVLDIV EDLRLINMQA IFAKRTGMII LGGGVVKHHI ANANLMRNGA
DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RMDAQPVKVY ADASLVFPLL VAETFAQKAD
AFRAEKNED
