AC   MF_03101;
DC   Protein; auto
TR   HAMAP; MF_03101; -; 1; level=0
XX
Names: Deoxyhypusine_hydroxylase
XX
ID   DOHH
case <OC:Saccharomyces>
DE   RecName: Full=Deoxyhypusine hydroxylase;
DE            Short=DOHH;
DE            EC=1.14.99.29;
DE   AltName: Full=Deoxyhypusine dioxygenase;
DE   AltName: Full=Deoxyhypusine monooxygenase;
DE   AltName: Full=Ligand of eIF5A protein 1;
else
DE   RecName: Full=Deoxyhypusine hydroxylase;
DE            Short=DOHH;
DE            EC=1.14.99.29;
DE   AltName: Full=Deoxyhypusine dioxygenase;
DE   AltName: Full=Deoxyhypusine monooxygenase;
end case
case <OC:Vertebrata>
GN   Name=DOHH;
else case <OC:Caenorhabditis>
GN   Name=dohh-1; Synonyms=tag-242;
else case <OC:Drosophilidae>
GN   Name=nero;
else case <OC:Fungi>
GN   Name=LIA1;
end case
XX
case <OC:Drosophilidae>
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate to form hypusine, an essential post-translational
CC       modification only found in mature eIF-5A factor. Essential for
CC       organismal viability and plays a role in a wide number of important
CC       processes such as cell growth and proliferation, and regulates
CC       induction of autophagy and protein synthesis. Has a role in eIF-5A-
CC       mediated translational control.
else
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate to form hypusine, an essential post-translational
CC       modification only found in mature eIF-5A factor.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-
CC         hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144,
CC         Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657,
CC         ChEBI:CHEBI:91175; EC=1.14.99.29;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 2 Fe(2+) ions per subunit.;
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
case <OC:Fungi>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
else case <OC:Drosophilidae>
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Note=In larval imaginal disk and
CC       Garland cells.
end case
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
XX
DR   PROSITE; PS50077; HEAT_REPEAT; 1-2; trigger=no
DR   Pfam; PF03130; HEAT_PBS; 3-5; trigger=yes
DR   Pfam; PF02985; HEAT; 1; trigger=no
XX
KW   Hypusine biosynthesis
KW   Iron
KW   Metal-binding
KW   Monooxygenase
KW   Oxidoreductase
case <OC:Fungi>
KW   Cytoplasm
KW   Nucleus
end case
case <OC:Drosophilidae>
KW   Endoplasmic reticulum
KW   Membrane
end case
case <FTTag:acetyl>
KW   Acetylation
end case
XX
GO   GO:0019135; F:deoxyhypusine monooxygenase activity
GO   GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine
case <OC:Fungi>
GO   GO:0005737; C:cytoplasm
GO   GO:0005634; C:nucleus
end case
case <OC:Drosophilidae>
GO   GO:0042406; C:extrinsic component of endoplasmic reticulum membrane
end case
XX
FT   From: DOHH_HUMAN (Q9BU89)
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         57
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         89
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         208
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         241
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   From: DOHH_YEAST (P47120)
case <OC:Saccharomyces>
FT   INIT_MET        1
FT                   /note="Removed"
FT   Condition: M
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT   Tag: acetyl; Condition: S
end case
XX
Size: 282-411;
Related: None;
Template: Q9BU89; P47120; Q9V9U4;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ORYSJ
Plasmid: None
Comments: None
XX
# Revision 1.13 2022/11/19
//