DHYS_ARATH
ID DHYS_ARATH Reviewed; 368 AA.
AC Q9FI94; Q9ASU5; Q9C5Y5;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Deoxyhypusine synthase;
DE EC=2.5.1.46;
GN Name=DHS; OrderedLocusNames=At5g05920; ORFNames=K18J17_7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=11278418; DOI=10.1074/jbc.m008544200;
RA Wang T.-W., Lu L., Wang D., Thompson J.E.;
RT "Isolation and characterization of senescence-induced cDNAs encoding
RT deoxyhypusine synthase and eucaryotic translation initiation factor 5A from
RT tomato.";
RL J. Biol. Chem. 276:17541-17549(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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. Also
CC able to produce homospermidine from putrescine (By similarity).
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;
CC -!- PATHWAY: Protein modification; eIF5A hypusination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FI94-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32840.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF296078; AAG53642.2; -; mRNA.
DR EMBL; AB017060; BAB10797.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90939.1; -; Genomic_DNA.
DR EMBL; AF361828; AAK32840.1; ALT_FRAME; mRNA.
DR EMBL; AY056066; AAL06966.1; -; mRNA.
DR EMBL; AY087829; AAM65382.1; -; mRNA.
DR RefSeq; NP_196211.1; NM_120674.4. [Q9FI94-1]
DR AlphaFoldDB; Q9FI94; -.
DR SMR; Q9FI94; -.
DR STRING; 3702.AT5G05920.1; -.
DR iPTMnet; Q9FI94; -.
DR PaxDb; Q9FI94; -.
DR PRIDE; Q9FI94; -.
DR ProteomicsDB; 222019; -. [Q9FI94-1]
DR EnsemblPlants; AT5G05920.1; AT5G05920.1; AT5G05920. [Q9FI94-1]
DR GeneID; 830477; -.
DR Gramene; AT5G05920.1; AT5G05920.1; AT5G05920. [Q9FI94-1]
DR KEGG; ath:AT5G05920; -.
DR Araport; AT5G05920; -.
DR TAIR; locus:2153664; AT5G05920.
DR eggNOG; KOG2924; Eukaryota.
DR HOGENOM; CLU_039781_0_0_1; -.
DR InParanoid; Q9FI94; -.
DR OMA; FWSYFCQ; -.
DR OrthoDB; 883558at2759; -.
DR PhylomeDB; Q9FI94; -.
DR BioCyc; ARA:AT5G05920-MON; -.
DR BRENDA; 2.5.1.46; 399.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q9FI94; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI94; baseline and differential.
DR Genevisible; Q9FI94; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034038; F:deoxyhypusine synthase activity; IBA:GO_Central.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
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 2: Evidence at transcript level;
KW Alternative splicing; Hypusine biosynthesis; NAD; Reference proteome;
KW Transferase.
FT CHAIN 1..368
FT /note="Deoxyhypusine synthase"
FT /id="PRO_0000134473"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 104..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 130..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 135..136
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 309..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 315..317
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 324..330
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 343..344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 29
FT /note="E -> Q (in Ref. 1; AAG53642)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Missing (in Ref. 4; AAK32840)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="T -> P (in Ref. 1; AAG53642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41064 MW; 491D9DF362DAB002 CRC64;
MEDDRVFSSV HSTVFKESES LEGKCDKIEG YDFNQGVDYP KLMRSMLTTG FQASNLGEAI
DVVNQMLDWR LADETTVAED CSEEEKNPSF RESVKCKIFL GFTSNLVSSG VRDTIRYLVQ
HHMVDVIVTT TGGVEEDLIK CLAPTFKGDF SLPGAYLRSK GLNRIGNLLV PNDNYCKFED
WIIPIFDEML KEQKEENVLW TPSKLLARLG KEINNESSYL YWAYKMNIPV FCPGLTDGSL
GDMLYFHSFR TSGLIIDVVQ DIRAMNGEAV HANPKKTGMI ILGGGLPKHH ICNANMMRNG
ADYAVFINTG QEFDGSDSGA RPDEAVSWGK IRGSAKTVKV YCDATIAFPL LVAETFATKR
DQTCESKT
