DHYS1_ARCFU
ID DHYS1_ARCFU Reviewed; 301 AA.
AC O28088;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable deoxyhypusine synthase 1;
DE Short=DHS 1;
DE EC=2.5.1.46;
GN Name=dys1; OrderedLocusNames=AF_2195;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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}.
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DR EMBL; AE000782; AAB89061.1; -; Genomic_DNA.
DR PIR; C69524; C69524.
DR RefSeq; WP_010879684.1; NC_000917.1.
DR AlphaFoldDB; O28088; -.
DR SMR; O28088; -.
DR STRING; 224325.AF_2195; -.
DR EnsemblBacteria; AAB89061; AAB89061; AF_2195.
DR GeneID; 24795944; -.
DR KEGG; afu:AF_2195; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_1_0_2; -.
DR OMA; EARSWGK; -.
DR OrthoDB; 35308at2157; -.
DR PhylomeDB; O28088; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000002199; 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.
DR TIGRFAMs; TIGR00321; dhys; 1.
PE 3: Inferred from homology;
KW Hypusine biosynthesis; NAD; Reference proteome; Transferase.
FT CHAIN 1..301
FT /note="Probable deoxyhypusine synthase 1"
FT /id="PRO_0000134490"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 33348 MW; 4330CBD62853FF38 CRC64;
MRVTSPEIQR GIKVSELLDM FGSTAFNARR LGEAAKICEE MVKSDSFVFL TLAGAMIPAG
MRKIVAGMMQ NGFISSLVTT GANIVHEIVE SLGIGHEIGS CYVDDTALAE ESINRIYDVF
VGQEAFERVE EFLSGIIEGL DGIYTTYEFL WEVGKRIPDE RSFLRIAAER EIPVFCPTLH
DSIAGLHMTI YRKNLQIDFF RDVSRIIDFC FQKRKMGVIV VGGGVPKNFT LQAMLLAEGF
DYAVQITTDS PQWGGLSGAT LEEAKSWCKL KPDAKAVTVY CDATIALPML YAYLLDRCGE
S