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DHYS_THEVO
ID   DHYS_THEVO              Reviewed;         310 AA.
AC   Q97BN6;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Probable deoxyhypusine synthase;
DE            Short=DHS;
DE            EC=2.5.1.46;
GN   Name=dys; OrderedLocusNames=TV0419; ORFNames=TVG0406345;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59561.1; -; Genomic_DNA.
DR   RefSeq; WP_010916676.1; NC_002689.2.
DR   AlphaFoldDB; Q97BN6; -.
DR   SMR; Q97BN6; -.
DR   STRING; 273116.14324634; -.
DR   EnsemblBacteria; BAB59561; BAB59561; BAB59561.
DR   GeneID; 1440934; -.
DR   KEGG; tvo:TVG0406345; -.
DR   eggNOG; arCOG04142; Archaea.
DR   HOGENOM; CLU_039781_1_0_2; -.
DR   OMA; FWSYFCQ; -.
DR   OrthoDB; 35308at2157; -.
DR   PhylomeDB; Q97BN6; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001017; 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.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; NAD; Transferase.
FT   CHAIN           1..310
FT                   /note="Probable deoxyhypusine synthase"
FT                   /id="PRO_0000134511"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34951 MW;  8B9BF56AC930F920 CRC64;
     MDRKELLSKP VQDLRIDGNT TLSNLMAQFS NIGGFTAAKL YEAHSIISDM FLEDNTTFLS
     FPADIISTGL RGLINDVVKR KLVDVIITTS GTLDHDIART FGKYYCGSFN YSDVELREIN
     INRLGNVLVP DESYGELIEE KVMEQLEKLY SIKKEWATVD LIKEIGLSIN NESSILYNAA
     KNDIPIFVPG ITDGSFGSQL WSFYEQHHDF KINLLEDEHR LSDIIFDAKK TGAIMVGGGI
     SKHHTIWWNQ FRDGLDYAVY ITTAQEYDGS LSGAKLEEAI SWKKVRPNAR FVNIYGDATV
     IMPILMAPFL
 
 
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