ID DOHH_ASPF1 Reviewed; 335 AA. AC A1DFW7; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 04-NOV-2026, entry version 106. 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=NFIA_082210; OS Aspergillus fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Neosartorya fischeri). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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; Evidence={ECO:0000255|HAMAP- CC 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; DS027696; EAW18274.1; -; Genomic_DNA. DR RefSeq; XP_001260171.1; XM_001260170.1. DR AlphaFoldDB; A1DFW7; -. DR SMR; A1DFW7; -. DR STRING; 331117.A1DFW7; -. DR EnsemblFungi; NFIA_082210_t1; EAW18274.1; NFIA_082210. DR GeneID; 4586728; -. DR KEGG; nfi:NFIA_082210; -. DR VEuPathDB; FungiDB:NFIA_082210; -. DR eggNOG; KOG0567; Eukaryota. DR HOGENOM; CLU_053974_0_0_1; -. DR OMA; AACEDPH; -. DR OrthoDB; 421002at2759; -. DR UniPathway; UPA00354; -. DR Proteomes; UP000006702; 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:0008612; P:peptidyl-hypusine biosynthetic process; IEA:UniProtKB-UniRule. 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; 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. PE 3: Inferred from homology; KW Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; KW Nucleus; Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1..335 FT /note="Deoxyhypusine hydroxylase" FT /id="PRO_0000283669" 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 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 335 AA; 36482 MW; C0385EE7460F5FCE CRC64; MSPSATDTTE GVDPTILTLR KVLTSESEPL ARRFRALFSL KHLACLQPPT EKTLPAIQAI AAAFTSPSAL LKHELAYCLG QTRNPESVPF LQQVAKDTEQ DTMCRHEAAE ALGALGYEDS LEILKALRDN QNESDVIRET CDIAVDRILW ENSEARKAEK LKTSDFTSID PAPPLPMTAS EPSIPEIEKT LLDTSLPLFL RYRAMFALRD LASPPDLPTA TRAVEALAKG LKDPSALFRH EIAFVFGQLC HPASIPSLTE ALSNQSEAGM VRHEAAEALG SLGDCEGVEE TLRKFLNDPE QVVRDSVIVA LDMAEYEKNG EVEYALVPDA GVAAA //