DOHH_LENED
ID DOHH_LENED Reviewed; 330 AA.
AC Q96WP5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101};
DE Short=DOHH {ECO:0000255|HAMAP-Rule:MF_03101};
DE EC=1.14.99.29 {ECO:0000255|HAMAP-Rule:MF_03101};
DE AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
GN Name=LIA1 {ECO:0000255|HAMAP-Rule:MF_03101}; Synonyms=mfbC;
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15388965; DOI=10.1271/bbb.68.1898;
RA Miyazaki Y., Sakuragi T., Yamazaki T., Shishido K.;
RT "Target genes of the developmental regulator PRIB of the mushroom Lentinula
RT edodes.";
RL Biosci. Biotechnol. Biochem. 68:1898-1905(2004).
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. {ECO:0000255|HAMAP-
CC Rule:MF_03101}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03101};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03101};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03101};
CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC Rule:MF_03101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03101}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03101}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_03101}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB067692; BAB62528.1; -; mRNA.
DR AlphaFoldDB; Q96WP5; -.
DR SMR; Q96WP5; -.
DR UniPathway; UPA00354; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; -; 2.
DR HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR Pfam; PF03130; HEAT_PBS; 1.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW Nucleus; Oxidoreductase; Repeat.
FT CHAIN 1..330
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000283668"
FT REPEAT 57..83
FT /note="HEAT-like PBS-type 1"
FT REPEAT 90..116
FT /note="HEAT-like PBS-type 2"
FT REPEAT 199..225
FT /note="HEAT-like PBS-type 3"
FT REPEAT 263..289
FT /note="HEAT-like PBS-type 4"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ SEQUENCE 330 AA; 36124 MW; 451028387237CE22 CRC64;
MSLSATQLKA LEDSVLNTSG KVLLHDRVRA LFTLKSLKNE DAIRIISKGF QDSAALLKHE
LAYCLGQIRN PLALPVLESV LRNPSEDPMV RHEAAEAMGA ISTADSIPIL KQYLSDPDRS
VRETCEIAIA KIEWDKTEEG AKNDKATRDE NRLPLYTSID PAPATSGLLT GAPRPEEISQ
TKIDELRDNL LDVNRPLFER YRAMFALRNI GSPAAVDALA AGFSGDSALF KHEIAFVFGQ
LLSPHSVPCL IEVLQNSPES DMVRHEAAEA LGGIATPEVL PPLKEWVARD DAPVVVRESC
QVALDLWEYE NSGDFQYANG LESPSTPISV
