DOHH_HUMAN
ID DOHH_HUMAN Reviewed; 302 AA.
AC Q9BU89; O75265;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000303|PubMed:16533814};
DE Short=hDOHH {ECO:0000303|PubMed:19706422};
DE EC=1.14.99.29 {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:16371467, ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422};
DE AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE AltName: Full=HEAT-like repeat-containing protein 1 {ECO:0000303|PubMed:19706422};
GN Name=DOHH {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000312|HGNC:HGNC:28662};
GN Synonyms=HLRC1 {ECO:0000303|PubMed:19706422};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR,
RP MUTAGENESIS OF HIS-56; GLU-57; HIS-89; GLU-90; HIS-207; GLU-208; HIS-240
RP AND GLU-241, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16533814; DOI=10.1074/jbc.m601081200;
RA Kim Y.S., Kang K.R., Wolff E.C., Bell J.K., McPhie P., Park M.H.;
RT "Deoxyhypusine hydroxylase is an Fe(II)-dependent, HEAT-repeat enzyme.
RT Identification of amino acid residues critical for Fe(II) binding and
RT catalysis.";
RL J. Biol. Chem. 281:13217-13225(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=16371467; DOI=10.1073/pnas.0509348102;
RA Park J.-H., Aravind L., Wolff E.C., Kaevel J., Kim Y.S., Park M.H.;
RT "Molecular cloning, expression, and structural prediction of deoxyhypusine
RT hydroxylase: a HEAT-repeat-containing metalloenzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:51-56(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=19706422; DOI=10.1073/pnas.0904553106;
RA Vu V.V., Emerson J.P., Martinho M., Kim Y.S., Munck E., Park M.H.,
RA Que L. Jr.;
RT "Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell
RT growth, activates O(2) with a nonheme diiron center.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14814-14819(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9] {ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-289 IN COMPLEX WITH IRON,
RP COFACTOR, AND MUTAGENESIS OF MET-86 AND MET-237.
RX PubMed=25865244; DOI=10.1016/j.str.2015.03.002;
RA Han Z., Sakai N., Bottger L.H., Klinke S., Hauber J., Trautwein A.X.,
RA Hilgenfeld R.;
RT "Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine
RT Hydroxylase, an Oxygenase Involved in Hypusination.";
RL Structure 23:882-892(2015).
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 (PubMed:16533814, PubMed:16371467, PubMed:19706422). Hypusination is
CC unique to mature eIF-5A factor and is essential for its function (By
CC similarity). {ECO:0000250|UniProtKB:Q99LN9, ECO:0000255|HAMAP-
CC Rule:MF_03101, ECO:0000269|PubMed:16371467,
CC ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422}.
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:16371467,
CC ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422,
CC ECO:0000269|PubMed:25865244, ECO:0007744|PDB:4D4Z,
CC ECO:0007744|PDB:4D50};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422,
CC ECO:0000269|PubMed:25865244, ECO:0007744|PDB:4D4Z,
CC ECO:0007744|PDB:4D50};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-8.5 at 37 degrees Celsius.
CC {ECO:0000269|PubMed:16533814};
CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC Rule:MF_03101, ECO:0000269|PubMed:16371467,
CC ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:19706422}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_03101}.
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DR EMBL; AC005551; AAC33193.1; -; Genomic_DNA.
DR EMBL; AC093052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002817; AAH02817.1; -; mRNA.
DR EMBL; BC009863; AAH09863.1; -; mRNA.
DR CCDS; CCDS12108.1; -.
DR RefSeq; NP_001138637.1; NM_001145165.1.
DR RefSeq; NP_112594.1; NM_031304.4.
DR PDB; 4D4Z; X-ray; 1.70 A; A/B=1-289.
DR PDB; 4D50; X-ray; 1.70 A; A/B=1-289.
DR PDBsum; 4D4Z; -.
DR PDBsum; 4D50; -.
DR AlphaFoldDB; Q9BU89; -.
DR SMR; Q9BU89; -.
DR BioGRID; 123662; 30.
DR IntAct; Q9BU89; 7.
DR STRING; 9606.ENSP00000398882; -.
DR BindingDB; Q9BU89; -.
DR ChEMBL; CHEMBL4523441; -.
DR GlyGen; Q9BU89; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BU89; -.
DR PhosphoSitePlus; Q9BU89; -.
DR BioMuta; DOHH; -.
DR DMDM; 74733193; -.
DR EPD; Q9BU89; -.
DR jPOST; Q9BU89; -.
DR MassIVE; Q9BU89; -.
DR MaxQB; Q9BU89; -.
DR PaxDb; Q9BU89; -.
DR PeptideAtlas; Q9BU89; -.
DR PRIDE; Q9BU89; -.
DR ProteomicsDB; 79065; -.
DR Antibodypedia; 23208; 47 antibodies from 16 providers.
DR DNASU; 83475; -.
DR Ensembl; ENST00000427575.6; ENSP00000398882.1; ENSG00000129932.10.
DR Ensembl; ENST00000672935.1; ENSP00000500806.1; ENSG00000129932.10.
DR GeneID; 83475; -.
DR KEGG; hsa:83475; -.
DR MANE-Select; ENST00000427575.6; ENSP00000398882.1; NM_001145165.2; NP_001138637.1.
DR UCSC; uc002lxs.4; human.
DR CTD; 83475; -.
DR DisGeNET; 83475; -.
DR GeneCards; DOHH; -.
DR HGNC; HGNC:28662; DOHH.
DR HPA; ENSG00000129932; Low tissue specificity.
DR MIM; 611262; gene.
DR neXtProt; NX_Q9BU89; -.
DR OpenTargets; ENSG00000129932; -.
DR PharmGKB; PA142671678; -.
DR VEuPathDB; HostDB:ENSG00000129932; -.
DR eggNOG; KOG0567; Eukaryota.
DR GeneTree; ENSGT00500000044957; -.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q9BU89; -.
DR OMA; CIQILNR; -.
DR OrthoDB; 1441854at2759; -.
DR PhylomeDB; Q9BU89; -.
DR TreeFam; TF105626; -.
DR BioCyc; MetaCyc:HS05318-MON; -.
DR BRENDA; 1.14.99.29; 2681.
DR PathwayCommons; Q9BU89; -.
DR Reactome; R-HSA-204626; Hypusine synthesis from eIF5A-lysine.
DR SignaLink; Q9BU89; -.
DR UniPathway; UPA00354; -.
DR BioGRID-ORCS; 83475; 472 hits in 1084 CRISPR screens.
DR GenomeRNAi; 83475; -.
DR Pharos; Q9BU89; Tbio.
DR PRO; PR:Q9BU89; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BU89; protein.
DR Bgee; ENSG00000129932; Expressed in inferior vagus X ganglion and 210 other tissues.
DR ExpressionAtlas; Q9BU89; baseline and differential.
DR Genevisible; Q9BU89; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IMP:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IMP: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; IPR021133; HEAT_type_2.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..302
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000248575"
FT REPEAT 54..80
FT /note="HEAT-like PBS-type 1"
FT REPEAT 87..113
FT /note="HEAT-like PBS-type 2"
FT REPEAT 174..200
FT /note="HEAT-like PBS-type 3"
FT REPEAT 205..231
FT /note="HEAT-like PBS-type 4"
FT REPEAT 238..264
FT /note="HEAT-like PBS-type 5"
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 ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:16533814, ECO:0000269|PubMed:25865244,
FT ECO:0007744|PDB:4D4Z, ECO:0007744|PDB:4D50"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MUTAGEN 56
FT /note="H->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 57
FT /note="E->A: Loss of deoxyhypusine monooxygenase activity.
FT No effect on iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 86
FT /note="M->A: Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:25865244"
FT MUTAGEN 86
FT /note="M->L: No effect on iron-binding. Loss of iron-
FT binding; when associated with L-237."
FT /evidence="ECO:0000269|PubMed:25865244"
FT MUTAGEN 89
FT /note="H->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 90
FT /note="E->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 207
FT /note="H->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 208
FT /note="E->A: Loss of deoxyhypusine monooxygenase activity.
FT No effect on iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 237
FT /note="M->L: Decreased iron-binding. Loss of iron-binding;
FT when associated with L-86."
FT /evidence="ECO:0000269|PubMed:25865244"
FT MUTAGEN 240
FT /note="H->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT MUTAGEN 241
FT /note="E->A: Loss of deoxyhypusine monooxygenase activity.
FT Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:16533814"
FT HELIX 1..15
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:4D4Z"
FT HELIX 267..282
FT /evidence="ECO:0007829|PDB:4D4Z"
SQ SEQUENCE 302 AA; 32904 MW; CDA86E5549B98A2F CRC64;
MVTEQEVDAI GQTLVDPKQP LQARFRALFT LRGLGGPGAI AWISQAFDDD SALLKHELAY
CLGQMQDARA IPMLVDVLQD TRQEPMVRHE AGEALGAIGD PEVLEILKQY SSDPVIEVAE
TCQLAVRRLE WLQQHGGEPA AGPYLSVDPA PPAEERDVGR LREALLDESR PLFERYRAMF
ALRNAGGEEA ALALAEGLHC GSALFRHEVG YVLGQLQHEA AVPQLAAALA RCTENPMVRH
ECAEALGAIA RPACLAALQA HADDPERVVR ESCEVALDMY EHETGRAFQY ADGLEQLRGA
PS
