DOHH_DANRE
ID DOHH_DANRE Reviewed; 305 AA.
AC Q7ZUX6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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; ORFNames=zgc:56338;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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: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; BC046086; AAH46086.1; -; mRNA.
DR RefSeq; NP_955857.1; NM_199563.2.
DR AlphaFoldDB; Q7ZUX6; -.
DR SMR; Q7ZUX6; -.
DR STRING; 7955.ENSDARP00000011317; -.
DR PaxDb; Q7ZUX6; -.
DR GeneID; 321732; -.
DR KEGG; dre:321732; -.
DR CTD; 83475; -.
DR ZFIN; ZDB-GENE-030131-451; dohh.
DR eggNOG; KOG0567; Eukaryota.
DR InParanoid; Q7ZUX6; -.
DR OrthoDB; 1441854at2759; -.
DR PhylomeDB; Q7ZUX6; -.
DR Reactome; R-DRE-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q7ZUX6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..305
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000248579"
FT REPEAT 54..80
FT /note="HEAT-like PBS-type 1"
FT REPEAT 87..113
FT /note="HEAT-like PBS-type 2"
FT REPEAT 178..204
FT /note="HEAT-like PBS-type 3"
FT REPEAT 209..235
FT /note="HEAT-like PBS-type 4"
FT REPEAT 242..268
FT /note="HEAT-like PBS-type 5"
FT REGION 137..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 211
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 244
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 245
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"
SQ SEQUENCE 305 AA; 33919 MW; 6F82EDCEE1AD9662 CRC64;
MANDKDIAAV GSILVNTKQD LTTRFRALFT LRNLGGAEAV KWISEAFVDE SALLKHELAY
CLGQMQDESA IPTLEAVLKD TNQEPMVRHE AGEALGAIGN PKVLELLKKY AEDPVIEVAE
TCQLAVKRLE WLMNGGEQTK DGTDENPYCS VDPAPPAQRK SVPELRTQLL DETLPLFDRY
RAMFALRNLG TEEAVLALGD GLQCSSALFR HEIGYVLGQI QHEASIPQLQ AALEKMDENA
MVRHECAEAL GSIGKEPCVQ ILERYRKDQE RVVKESCEVA LDMLEYENSS QFQYADGLLR
LQSAH
