ID DOHH_BOVIN Reviewed; 303 AA. AC Q0VC53; A5H2K6; A5H2K8; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 101. 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, ECO:0000269|PubMed:17391984}; DE AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101}; DE AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101}; GN Name=DOHH {ECO:0000255|HAMAP-Rule:MF_03101}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND RP MUTAGENESIS OF GLU-57. RC TISSUE=Brain; RX PubMed=17391984; DOI=10.1016/j.pep.2007.02.009; RA Huang J.-K., Cui Y., Chen C.-H., Clampitt D., Lin C.-T., Wen L.; RT "Molecular cloning and functional expression of bovine deoxyhypusine RT hydroxylase cDNA and homologs."; RL Protein Expr. Purif. 54:126-133(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L- CC lysine intermediate produced by deoxyhypusine synthase/DHPS on a CC critical lysine of the eukaryotic translation initiation factor 5A/eIF- CC 5A. This is the second step of the post-translational modification of CC that lysine into an unusual amino acid residue named hypusine. CC Hypusination is unique to mature eIF-5A factor and is essential for its CC function. {ECO:0000255|HAMAP-Rule:MF_03101, CC ECO:0000269|PubMed:17391984}. 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, ECO:0000269|PubMed:17391984}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- CC Rule:MF_03101}; CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9BU89, CC ECO:0000255|HAMAP-Rule:MF_03101}; CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP- CC Rule:MF_03101, ECO:0000269|PubMed:17391984}. 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; DQ990881; ABL86660.1; -; mRNA. DR EMBL; DQ990882; ABL86661.1; -; mRNA. DR EMBL; DQ990883; ABL86662.1; -; mRNA. DR EMBL; BC120351; AAI20352.1; -; mRNA. DR RefSeq; NP_001069354.1; NM_001075886.1. DR RefSeq; XP_005209005.1; XM_005208948.2. DR RefSeq; XP_010805282.1; XM_010806980.1. DR AlphaFoldDB; Q0VC53; -. DR SMR; Q0VC53; -. DR STRING; 9913.ENSBTAP00000006935; -. DR PaxDb; 9913-ENSBTAP00000006935; -. DR Ensembl; ENSBTAT00000006935.6; ENSBTAP00000006935.5; ENSBTAG00000005272.6. DR GeneID; 526521; -. DR KEGG; bta:526521; -. DR CTD; 83475; -. DR VEuPathDB; HostDB:ENSBTAG00000005272; -. DR VGNC; VGNC:28164; DOHH. DR eggNOG; KOG0567; Eukaryota. DR GeneTree; ENSGT00500000044957; -. DR HOGENOM; CLU_053974_0_0_1; -. DR InParanoid; Q0VC53; -. DR OMA; GQLQEPC; -. DR OrthoDB; 5474306at2759; -. DR TreeFam; TF105626; -. DR BRENDA; 1.14.99.29; 908. DR Reactome; R-BTA-204626; Hypusine synthesis from eIF5A-lysine. DR UniPathway; UPA00354; -. DR Proteomes; UP000009136; Chromosome 7. DR Bgee; ENSBTAG00000005272; Expressed in tongue muscle and 103 other cell types or tissues. DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. 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 1: Evidence at protein level; KW Acetylation; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1..303 FT /note="Deoxyhypusine hydroxylase" FT /id="PRO_0000326490" FT REPEAT 23..49 FT /note="HEAT-like PBS-type 1" FT REPEAT 54..80 FT /note="HEAT-like PBS-type 2" FT REPEAT 87..113 FT /note="HEAT-like PBS-type 3" FT REPEAT 175..201 FT /note="HEAT-like PBS-type 4" FT REPEAT 206..232 FT /note="HEAT-like PBS-type 5" FT REPEAT 239..265 FT /note="HEAT-like PBS-type 6" FT BINDING 56 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT BINDING 89 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT BINDING 90 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT BINDING 208 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT BINDING 241 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT BINDING 242 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP- FT Rule:MF_03101" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9BU89" FT MUTAGEN 57 FT /note="E->G: Loss of deoxyhypusine monooxygenase activity." FT /evidence="ECO:0000269|PubMed:17391984" FT CONFLICT 266 FT /note="P -> S (in Ref. 1; ABL86660/ABL86661/ABL86662)" FT /evidence="ECO:0000305" SQ SEQUENCE 303 AA; 33261 MW; 4487BA5BDFC61AB9 CRC64; MVTEQEVEAV GQTLVDPGQP LQARFRALFT LRGLGGPVAI SWISRAFDDD SALLKHELAY CLGQMQDRRA IPVLLDVLRD TRQEPMVRHE AGEALGAIGD PEVLEILKQY STDPVVEVAE TCQLAVRRLE WLQQHGGESA VRGPYLSVDP APPAEERDLG QLREALLDEA RPLFDRYRAM FALRDAGGKE AALALAEGLR CGSALFRHEI GYVLGQMQHE AAVPQLAAAL AQPTENPMVR HECAEALGAI ARPACLAALR AHVADPERVV RESCEVALDM YEYETGSTFQ YADGLERLRS PLS //