DOHH_CHICK
ID DOHH_CHICK Reviewed; 299 AA.
AC Q5ZIP3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 {ECO:0000255|HAMAP-Rule:MF_03101}; ORFNames=RCJMB04_24i7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720741; CAG32400.1; -; mRNA.
DR RefSeq; NP_001026584.1; NM_001031413.1.
DR AlphaFoldDB; Q5ZIP3; -.
DR SMR; Q5ZIP3; -.
DR STRING; 9031.ENSGALP00000028167; -.
DR PaxDb; Q5ZIP3; -.
DR Ensembl; ENSGALT00000028221; ENSGALP00000028167; ENSGALG00000017524.
DR GeneID; 427066; -.
DR KEGG; gga:427066; -.
DR CTD; 83475; -.
DR VEuPathDB; HostDB:geneid_427066; -.
DR eggNOG; KOG0567; Eukaryota.
DR GeneTree; ENSGT00500000044957; -.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q5ZIP3; -.
DR OMA; CIQILNR; -.
DR OrthoDB; 1441854at2759; -.
DR PhylomeDB; Q5ZIP3; -.
DR Reactome; R-GGA-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q5ZIP3; -.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000017524; Expressed in granulocyte and 14 other tissues.
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; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
PE 2: Evidence at transcript level;
KW Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..299
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000248578"
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: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 207
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 240
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 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"
SQ SEQUENCE 299 AA; 32875 MW; FD601C3D353DAE86 CRC64;
MVTEEEVTAI GRTLLDAAQP LPARFRALFT LRNLGGPAAI DCIVRGFADS SALLKHELAF
CLGQMRDRAA IPALLGVLQD SQQEPMVRHE AGEALGAIGD PEVLDVLRRY SEDPVVEVAE
TCQLAVRRLE WLQEHGEEPG SSPYRSVDPA PPAEETDVAT LRAVLLDESR PLFDRYRAMF
ALRNLGGRDA VLALADGLRA GSALFRHEIG YVLGQMQDEA CVPQLTAALR SRAENPMVRH
ECAEALGSIA RPSCLETLRA FAQDEERVVR ESCEVALDMY EYENGPQFQY ADGLCRLQA
