DOHH_RAT
ID DOHH_RAT Reviewed; 302 AA.
AC Q5PPJ4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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:0000250|UniProtKB:Q9BU89, 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=Dohh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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:0000250|UniProtKB:Q99LN9, 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;
CC Evidence={ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
CC Rule:MF_03101};
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.
CC {ECO:0000250|UniProtKB:Q9BU89, 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; BC087658; AAH87658.1; -; mRNA.
DR RefSeq; NP_001020177.1; NM_001025006.1.
DR RefSeq; XP_006240999.1; XM_006240937.2.
DR RefSeq; XP_006241000.1; XM_006240938.2.
DR RefSeq; XP_006241001.1; XM_006240939.2.
DR AlphaFoldDB; Q5PPJ4; -.
DR SMR; Q5PPJ4; -.
DR BioGRID; 260793; 1.
DR STRING; 10116.ENSRNOP00000005640; -.
DR jPOST; Q5PPJ4; -.
DR PaxDb; Q5PPJ4; -.
DR PRIDE; Q5PPJ4; -.
DR Ensembl; ENSRNOT00000112038; ENSRNOP00000093565; ENSRNOG00000004259.
DR GeneID; 314644; -.
DR KEGG; rno:314644; -.
DR UCSC; RGD:1304783; rat.
DR CTD; 83475; -.
DR RGD; 1304783; Dohh.
DR eggNOG; KOG0567; Eukaryota.
DR GeneTree; ENSGT00500000044957; -.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q5PPJ4; -.
DR OMA; CIQILNR; -.
DR OrthoDB; 1441854at2759; -.
DR PhylomeDB; Q5PPJ4; -.
DR TreeFam; TF105626; -.
DR Reactome; R-RNO-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q5PPJ4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004259; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; Q5PPJ4; RN.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW Acetylation; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..302
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000248577"
FT REPEAT 54..80
FT /note="HEAT-like PBS-type 1"
FT REPEAT 87..113
FT /note="HEAT-like PBS-type 2"
FT REPEAT 175..201
FT /note="HEAT-like PBS-type 3"
FT REPEAT 206..232
FT /note="HEAT-like PBS-type 4"
FT REPEAT 239..265
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: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"
SQ SEQUENCE 302 AA; 33077 MW; B29216591C11523D CRC64;
MVTEQEVEAI GKTLVDSTQP LQARFRALFT LRGLGGPDAI SWISRGFEDS SALLKHELAY
CLGQMRDPRA IPVLVSVLQD RNQEPMVRHE AGEALGAIGN PKVLGLLKQY STDPVVEVAE
TCQLAVRRLE WLQQHPGEAT CAGPYLSVDP APPAAEGDVG RLRETLLDEA QPLFERYRAM
FALRNVGGKE AALALAEGLK CGSALFRHEV GYVLGQLQHE AAVSELAATL ARTTESPMVR
HECAEALGAI ARPACLAALR EYITDPERVV RESCEVALDM YEYENGQDFQ YADGLERLRP
PP
