DHYS_PYRHO
ID DHYS_PYRHO Reviewed; 342 AA.
AC O50105;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Probable deoxyhypusine synthase;
DE Short=DHS;
DE EC=2.5.1.46;
GN Name=dys; OrderedLocusNames=PH1397;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30503.1; -; Genomic_DNA.
DR PIR; G71012; G71012.
DR RefSeq; WP_010885484.1; NC_000961.1.
DR PDB; 7CMC; X-ray; 2.20 A; A/B/C/D=1-342.
DR PDBsum; 7CMC; -.
DR AlphaFoldDB; O50105; -.
DR SMR; O50105; -.
DR STRING; 70601.3257820; -.
DR EnsemblBacteria; BAA30503; BAA30503; BAA30503.
DR GeneID; 1443722; -.
DR KEGG; pho:PH1397; -.
DR eggNOG; arCOG04142; Archaea.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 35308at2157; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; Hypusine biosynthesis; NAD; Transferase.
FT CHAIN 1..342
FT /note="Probable deoxyhypusine synthase"
FT /id="PRO_0000134505"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7CMC"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 144..167
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:7CMC"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:7CMC"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7CMC"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:7CMC"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:7CMC"
SQ SEQUENCE 342 AA; 39011 MW; 679FA642DBDB941F CRC64;
MKAKDIVLKK SEKIEGVEVK GPWLDDAQSL EEVVSYYYRI GFQATHLGRA IEIWRKVEEK
RERGEEIRVF LGYTSNIISS GLREIIAWLV KEKKVDVIVT TAGGVEEDFI KSLKPFILGD
WEVDDAELRK KGVNRIGNIF VPNDRYIEFE KYMIPFFERV LKIEEKLSRP LTASEFIYEM
GRYMDEKLGK EKEKSVIYWA YKNNIPIFCP AITDGSIGDM LYFFKEERRD SRLIIDIAND
IVKLNNLAIT AKETASIILG GSLPKHAIIN ANLFRGGTDY AIYISTAVPW DGSLSGAPPR
EGVSWGKIKA KADYVEVWGD ATLIFPILVW MVMKARGQGY AQ
