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Database: UniProt
Entry: DOHH_ASPOR
LinkDB: DOHH_ASPOR
Original site: DOHH_ASPOR 
ID   DOHH_ASPOR              Reviewed;         339 AA.
AC   Q2UMQ8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-NOV-2023, entry version 109.
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; ORFNames=AO090001000660;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE57157.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007154; BAE57157.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001819159.2; XM_001819107.2.
DR   AlphaFoldDB; Q2UMQ8; -.
DR   SMR; Q2UMQ8; -.
DR   STRING; 510516.Q2UMQ8; -.
DR   VEuPathDB; FungiDB:AO090001000660; -.
DR   OMA; GQLQEPC; -.
DR   OrthoDB; 5474306at2759; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000006564; Chromosome 2.
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; 5.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW   Nucleus; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..339
FT                   /note="Deoxyhypusine hydroxylase"
FT                   /id="PRO_0000283657"
FT   REPEAT          71..97
FT                   /note="HEAT-like PBS-type 1"
FT   REPEAT          104..130
FT                   /note="HEAT-like PBS-type 2"
FT   REPEAT          200..233
FT                   /note="HEAT-like PBS-type 3"
FT   REPEAT          238..264
FT                   /note="HEAT-like PBS-type 4"
FT   REPEAT          271..298
FT                   /note="HEAT-like PBS-type 5"
FT   REGION          159..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         241
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         273
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT   BINDING         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   339 AA;  36986 MW;  D7CF8BAA0F916D3D CRC64;
     MASSAVDQPE GVDETILTLR KVLVNESEPL ARRFRALFSL KYIACLQPPT EKTLPAIQAI
     AAGFTSSSAL LKHELAYCLG QTRNPDAVSY LLEVVKNTEQ DAMCRHEAAE GLGALGFDTS
     LDVLKALRDD EKEEDVIRET CDIAVDRILW ENSEERKSEK LKPSDFTSID PAPPLPMASS
     QPSISDLEKT LLDTKLPLFQ RYRAMFALRD LASPPDLPTA VEAVEALAKG LKDPSALFRH
     EVAFVFGQLC HPASVPSLTE TLSDQKEMGM VRHEAAEALG SLGDVEGVED TLKKFLNDPE
     QVVRDSIIVA LDMAEYEKNG EMEYALVPDS AAPAAVSAA
//
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