ID   DHYSL_LEIDO             Reviewed;         379 AA.
AC   A4ZZ93;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Inactive deoxyhypusine synthase;
DE   AltName: Full=Deoxyhypusine synthase-like protein;
DE   AltName: Full=Deoxyhypusine synthase-like protein from chromosome 20 {ECO:0000303|PubMed:19880510};
DE            Short=DHSL20 {ECO:0000303|PubMed:19880510};
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABP65295.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 3D-STRUCTURE MODELING, AND MUTAGENESIS
RP   OF LEU-344.
RX   PubMed=19880510; DOI=10.1074/jbc.m109.048850;
RA   Chawla B., Jhingran A., Singh S., Tyagi N., Park M.H., Srinivasan N.,
RA   Roberts S.C., Madhubala R.;
RT   "Identification and characterization of a novel deoxyhypusine synthase in
RT   Leishmania donovani.";
RL   J. Biol. Chem. 285:453-463(2010).
CC   -!- SIMILARITY: Belongs to the deoxyhypusine synthase family.
CC       {ECO:0000255}.
CC   -!- CAUTION: Although similar to deoxyhypusine synthase, lacks the active
CC       site Lys at position 344 and does not show deoxyhypusine synthase
CC       activity. Converting Leu-344 to a lysine does not restore activity.
CC       {ECO:0000305}.
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DR   EMBL; EF512031; ABP65295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4ZZ93; -.
DR   SMR; A4ZZ93; -.
DR   VEuPathDB; TriTrypDB:LdBPK_200270.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_200007500; -.
DR   VEuPathDB; TriTrypDB:LDHU3_20.0290; -.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:InterPro.
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.
PE   1: Evidence at protein level;
KW   NAD.
FT   CHAIN           1..379
FT                   /note="Inactive deoxyhypusine synthase"
FT                   /id="PRO_0000419759"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         141..143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         146..147
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         261
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         302
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         307
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         323..324
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         329..331
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         338..344
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   BINDING         357..358
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P49366"
FT   MUTAGEN         344
FT                   /note="L->K: Still catalytically inactive."
FT                   /evidence="ECO:0000269|PubMed:19880510"
SQ   SEQUENCE   379 AA;  40799 MW;  B74EE9B1B4F55AA4 CRC64;
     MLASVPAPRP AKKDSAASRR KSASKSTGAA VKDGSSARVS ASGAAESPKQ SCAQVHGVDF
     QSLVHATQEE TLRAVVSSLP TTGLQATQIG RARQLVQQIL HHRSPEDRVF LAYTSNMISC
     GLRDTFTYLA RERLVDCFIS SAGGIEEDVI KCGGSTLLGQ FGQDGRALRR RGINRIGNLL
     VPNDNYCWFE DFFTPVLESV QEAQRASRWK THTAPSEIIE AMGAAIAKNH PDTCTSSLVY
     WCYRNGISVF SPAFTDGSMG DMIYFYNFSH KGLVVDPLED VVRLRKLAAK ERGRNLAIVL
     GGGLPKHHLL RNVPMDAVVM VTTGLEADGC VSSGVLADDV ACGLLREETE TVRVQGDATV
     VFPLMLIAET AATREGAAA