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Database: UniProt
Entry: A0A1Q3EHY4_LENED
LinkDB: A0A1Q3EHY4_LENED
Original site: A0A1Q3EHY4_LENED 
ID   A0A1Q3EHY4_LENED        Unreviewed;       331 AA.
AC   A0A1Q3EHY4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000256|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000256|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
GN   Name=LIA1 {ECO:0000256|HAMAP-Rule:MF_03101};
GN   ORFNames=LENED_008745 {ECO:0000313|EMBL:GAW06796.1};
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW06796.1, ECO:0000313|Proteomes:UP000188533};
RN   [1] {ECO:0000313|EMBL:GAW06796.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW06796.1,
RC   ECO:0000313|Proteomes:UP000188533};
RG   Lentinula edodes genome sequencing consortium;
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW06796.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW06796.1,
RC   ECO:0000313|Proteomes:UP000188533};
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RT   "A genome survey and senescence transcriptome analysis in Lentinula
RT   edodes.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000068, ECO:0000256|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000256|ARBA:ARBA00005041, ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03101}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAW06796.1}.
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DR   EMBL; BDGU01000348; GAW06796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3EHY4; -.
DR   STRING; 5353.A0A1Q3EHY4; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000188533; Unassembled WGS sequence.
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   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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   PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR   PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR   Pfam; PF13646; HEAT_2; 2.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03101};
KW   Hypusine biosynthesis {ECO:0000256|ARBA:ARBA00023256, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_03101}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03101};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03101}; Reference proteome {ECO:0000313|Proteomes:UP000188533}.
FT   REPEAT          73..113
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         93
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         232
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         233
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   331 AA;  36479 MW;  F21D2F0523756EB0 CRC64;
     MSLSATQLKA LEDSLLNTSG KVLLHDRFRS LFTLKSLKNE DSIRIISKGF QDSSALLKHE
     LAYCLGQIKN PLALPVLESV LRNPSEDPMV RHEAAEAMGA ISTTDSIPIL KQYLSDPDRS
     VRETCEIAIA KIEWDKTEEG AENEEATRDE NRLPLYTSID PAPATSGLLT GAPRPEEISQ
     TKIDELRDNL LDVNRALFER YRAMFALRNI GSPAAVDALA AGFSDDSALF KHEIAFVFGQ
     LLSPHSVPCL IEVLQNSTES DMVRHEAAEA LGGIATPEVL PHLKEWVARD DAPVVVRESC
     QVALDMWEYE NSGDFQYANG LESTSTLISV L
//
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