DHYS_NEUCR
ID DHYS_NEUCR Reviewed; 353 AA.
AC P49365; Q7RVI5; Q9P3J1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=dys-1; ORFNames=B7F21.30, NCU05418;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7592594; DOI=10.1074/jbc.270.41.23984;
RA Tao Y., Chen K.Y.;
RT "Molecular cloning and functional expression of Neurospora deoxyhypusine
RT synthase cDNA and identification of yeast deoxyhypusine synthase cDNA.";
RL J. Biol. Chem. 270:23984-23987(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP PROTEIN SEQUENCE OF 109-126; 151-171; 217-236 AND 290-305, AND
RP CHARACTERIZATION.
RX PubMed=7814398; DOI=10.1074/jbc.270.1.383;
RA Tao Y., Chen K.Y.;
RT "Purification of deoxyhypusine synthase from Neurospora crassa to
RT homogeneity by substrate elution affinity chromatography.";
RL J. Biol. Chem. 270:383-386(1995).
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 -!- 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 -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
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DR EMBL; U22400; AAC49075.1; -; mRNA.
DR EMBL; AL389901; CAB97475.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA34005.1; -; Genomic_DNA.
DR PIR; T47195; T47195.
DR PIR; T51022; T51022.
DR RefSeq; XP_963241.1; XM_958148.2.
DR AlphaFoldDB; P49365; -.
DR SMR; P49365; -.
DR STRING; 5141.EFNCRP00000006511; -.
DR PRIDE; P49365; -.
DR EnsemblFungi; EAA34005; EAA34005; NCU05418.
DR GeneID; 3879389; -.
DR KEGG; ncr:NCU05418; -.
DR VEuPathDB; FungiDB:NCU05418; -.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; P49365; -.
DR OMA; FWSYFCQ; -.
DR BRENDA; 2.5.1.46; 3627.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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 1: Evidence at protein level;
KW Direct protein sequencing; Hypusine biosynthesis; NAD; Reference proteome;
KW Transferase.
FT CHAIN 1..353
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134485"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 90..94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121..122
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 300..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 306..308
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 315..321
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 334..335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 245
FT /note="K -> E (in Ref. 1; AAC49075)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="A -> S (in Ref. 1; AAC49075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38942 MW; A290B0D00022DD13 CRC64;
MADNQIPSSV ADAVLVKSIE MPEGSQKVEE LDFNKFKGRP ITVDDLLQGM KHMGFQASSM
CEAVRIINEM RAYRDPTTSE KTTIFLGYTS NLISSGLRGT LRYLVQHKHV SAIVTTAGGI
EEDFIKCLGD TYMSSFSAVG ADLRSKGLNR IGNLVVPNSN YCAFEDWVVP ILDKMLEEQE
ASRGTENEIN WTPSKVIHRL GKEINDERSV YYWAWKNDIP VFCPALTDGS LGDMLYFHTF
KASPKQLRID IVEDIRKINT IAVRAKRAGM IILGGGIVKH HIANACLMRN GAESAVYINT
AQEFDGSDAG ARPDEAVSWG KIKVGADAVK VYMEATAAFP FIVANTFAKE DGL
