DHYS_PYRAB
ID DHYS_PYRAB Reviewed; 335 AA.
AC Q9V0N5; G8ZGV5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Probable deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=dys; OrderedLocusNames=PYRAB07540; ORFNames=PAB0511;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248285; CAB49668.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70150.1; -; Genomic_DNA.
DR PIR; C75119; C75119.
DR AlphaFoldDB; Q9V0N5; -.
DR SMR; Q9V0N5; -.
DR STRING; 272844.PAB0511; -.
DR EnsemblBacteria; CAB49668; CAB49668; PAB0511.
DR KEGG; pab:PAB0511; -.
DR PATRIC; fig|272844.11.peg.794; -.
DR eggNOG; arCOG04142; Archaea.
DR HOGENOM; CLU_039781_0_0_2; -.
DR OMA; FWSYFCQ; -.
DR PhylomeDB; Q9V0N5; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Transferase.
FT CHAIN 1..335
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_0000134502"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 37997 MW; 3DE853F38029EC55 CRC64;
MKAKDIVLKK SEEIEGLAIE GPWLDEVESL EGVISYYEKI GFQATHLGKA VKIWRKVEEK
RKGGEEVRVF LGYTSNIVSS GLREIIAWLV KERKVDVIVT TAGGIEEDFI KTLKPFILGD
WEVNDAELRE KGINRIGNIF VPNDRYIEFE KYMVPFFERI LDIERKLKRP LTASEFIYEM
GRYMDEVLGK EKEKSIIYWA YKRDVPIFCP AITDGSIGDM LYFFKEERHD SKLVIDIAND
IVKLNNLAIT AKETASIILG GSLPKHAIIN ANLFRGGTDY AIYISTAVPW DGSLSGAPPS
EGVSWGKIKA KADYVEIWAD ATLVFPILVW MVMKA