DOHH_PLAVS
ID DOHH_PLAVS Reviewed; 346 AA.
AC A5JZ19; M5B5E1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Deoxyhypusine hydroxylase {ECO:0000303|PubMed:23505486};
DE Short=DOHH {ECO:0000303|PubMed:23505486};
DE EC=1.14.99.29 {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:23505486};
DE AltName: Full=Deoxyhypusine dioxygenase {ECO:0000250|UniProtKB:P47120};
DE AltName: Full=Deoxyhypusine monooxygenase {ECO:0000250|UniProtKB:P47120};
GN Name=dohh {ECO:0000312|EMBL:CAP62402.1}; ORFNames=PVX_121970;
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAP62402.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=Salvador I {ECO:0000312|EMBL:CAP62402.1};
RX PubMed=23505486; DOI=10.1371/journal.pone.0058318;
RA Atemnkeng V.A., Pink M., Schmitz-Spanke S., Wu X.J., Dong L.L., Zhao K.H.,
RA May C., Laufer S., Langer B., Kaiser A.;
RT "Deoxyhypusine hydroxylase from Plasmodium vivax, the neglected human
RT malaria parasite: molecular cloning, expression and specific inhibition by
RT the 5-LOX inhibitor zileuton.";
RL PLoS ONE 8:E58318-E58318(2013).
RN [2] {ECO:0000312|EMBL:EDL47230.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000312|EMBL:EDL47230.1};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
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:23505486}.
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:23505486};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P47120,
CC ECO:0000255|HAMAP-Rule:MF_03101};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P47120,
CC ECO:0000255|HAMAP-Rule:MF_03101};
CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC Rule:MF_03101, ECO:0000269|PubMed:23505486}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the intraerythrocytic cycle,
CC with highest levels during the ring, mature trophozoite and mature
CC schizont stages and lower levels during the young trophozoite and young
CC schizont stages. {ECO:0000269|PubMed:23505486}.
CC -!- MISCELLANEOUS: Inhibited by the drug zileuton in vitro.
CC {ECO:0000269|PubMed:23505486}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000255}.
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DR EMBL; AM931168; CAP62402.1; -; mRNA.
DR EMBL; AAKM01000001; EDL47230.1; -; Genomic_DNA.
DR RefSeq; XP_001616957.1; XM_001616907.1.
DR AlphaFoldDB; A5JZ19; -.
DR SMR; A5JZ19; -.
DR STRING; 126793.A5JZ19; -.
DR EnsemblProtists; EDL47230; EDL47230; PVX_121970.
DR GeneID; 5476266; -.
DR KEGG; pvx:PVX_121970; -.
DR VEuPathDB; PlasmoDB:PVX_121970; -.
DR InParanoid; A5JZ19; -.
DR OMA; CIQILNR; -.
DR PhylomeDB; A5JZ19; -.
DR BRENDA; 1.14.99.29; 4894.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000008333; Chromosome 14.
DR Proteomes; UP000008333; Unassembled WGS sequence.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-UniRule.
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; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..346
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000423886"
FT REPEAT 71..100
FT /note="HEAT-like PBS-type 1"
FT /evidence="ECO:0000255"
FT REPEAT 104..133
FT /note="HEAT-like PBS-type 2"
FT /evidence="ECO:0000255"
FT REPEAT 213..242
FT /note="HEAT-like PBS-type 3"
FT /evidence="ECO:0000255"
FT REPEAT 246..275
FT /note="HEAT-like PBS-type 4"
FT /evidence="ECO:0000255"
FT REPEAT 279..320
FT /note="HEAT-like PBS-type 5"
FT /evidence="ECO:0000255"
FT BINDING 75
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 108
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 109
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 250
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 283
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 284
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 346 AA; 39009 MW; 50CF90FB000B42BE CRC64;
MTGSTHNGGS RLIQYEDSSN KEFIRKYLVE TRNEFIEKQM RALYECREIY KDDIDEVINI
LTYALENNDS VLLRHEVAYV IGQISNEKCN DILIKLLNDT EENLMVRHEA AEGLAAIGSD
SNIEVIKKFL NDEKVEVRET CELALSSLLE KNKYAVCSCS NKDSIKEAIK KKRNDEFVSK
KFNTIDPVVF TSSGNAKSVD ALIEDLNNEA VPLKLRYEAL FKLRDMETDV SINALGEVLI
KDKKSAIFRH EVAFVLGQAL HLNSLKYLIS SLQNVGEHEM VRHEVALALG SLGSLNINSQ
EYKNVQSEII STLKTFSKDA CRVVAESCLV GLDYIAENLN MAIEVN
