DOHH_BOVIN
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 03-AUG-2022, entry version 92.
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,
CC ECO:0000255|HAMAP-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}.
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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; Q0VC53; -.
DR PRIDE; Q0VC53; -.
DR Ensembl; ENSBTAT00000006935; ENSBTAP00000006935; ENSBTAG00000005272.
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; CIQILNR; -.
DR OrthoDB; 1441854at2759; -.
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 tissues.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IBA:GO_Central.
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 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
