DOHH_DROPS
ID DOHH_DROPS Reviewed; 302 AA.
AC Q297S2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=nero {ECO:0000255|HAMAP-Rule:MF_03101}; Synonyms=l(3)s1921;
GN ORFNames=GA15318;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(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. Essential for
CC organismal viability and plays a role in a wide number of important
CC processes such as cell growth and proliferation, and regulates
CC induction of autophagy and protein synthesis. Has a role in eIF-5A-
CC mediated translational control. {ECO:0000255|HAMAP-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: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03101}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03101}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03101}. Note=In larval imaginal disk and Garland cells.
CC {ECO:0000255|HAMAP-Rule:MF_03101}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_03101}.
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DR EMBL; CM000070; EAL28133.1; -; Genomic_DNA.
DR RefSeq; XP_001358990.1; XM_001358953.3.
DR AlphaFoldDB; Q297S2; -.
DR SMR; Q297S2; -.
DR STRING; 7237.FBpp0284128; -.
DR EnsemblMetazoa; FBtr0285690; FBpp0284128; FBgn0075338.
DR GeneID; 4801977; -.
DR KEGG; dpo:Dpse_GA15318; -.
DR eggNOG; KOG0567; Eukaryota.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q297S2; -.
DR OMA; CIQILNR; -.
DR PhylomeDB; Q297S2; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0075338; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; ISS:UniProtKB.
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; IPR004155; PBS_lyase_HEAT.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hypusine biosynthesis; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..302
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000248583"
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:0000255|HAMAP-Rule:MF_03101"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 209
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 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ SEQUENCE 302 AA; 33500 MW; D9E573536774B6B0 CRC64;
MVSQEQIEAI GGVLNNKDRP LKERFRALFT LKNIGGKTAI DAISKAFDDD SALLKHELAY
CLGQMQDPTA LEILTKVLKD TTQEPMVRHE AAEAMGAIGH ADVLAILEEY KKDPVVEVAE
TCAIALDRVR WLQSGQQVAD NNPYASVDPS PPTAGDKSVA ELKAIYLDAK QTLFDRYRAM
FSLRNLCTEE SVLAIAEGLK DSSALFRHEV AFVLGQLQEP CSIPYLQENL EDHKENEMVR
HECAEALGAI ATDDCIQILT RYADDEKRVV KESCVIALDM CEYENSPEFQ YADGLSKLDG
TK
