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Database: UniProt
Entry: I1R4B8_ORYGL
LinkDB: I1R4B8_ORYGL
Original site: I1R4B8_ORYGL 
ID   I1R4B8_ORYGL            Unreviewed;       319 AA.
AC   I1R4B8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000256|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000256|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA12G0037400.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA12G0037400.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate to form hypusine, an essential post-translational
CC       modification only found in mature eIF-5A factor. {ECO:0000256|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:0000256|ARBA:ARBA00000068, ECO:0000256|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000256|ARBA:ARBA00005041, ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03101}.
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DR   AlphaFoldDB; I1R4B8; -.
DR   STRING; 4538.I1R4B8; -.
DR   EnsemblPlants; ORGLA12G0037400.1; ORGLA12G0037400.1; ORGLA12G0037400.
DR   Gramene; ORGLA12G0037400.1; ORGLA12G0037400.1; ORGLA12G0037400.
DR   eggNOG; KOG0567; Eukaryota.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   OMA; HGDGPRC; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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   PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR   PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR   Pfam; PF13646; HEAT_2; 2.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis {ECO:0000256|ARBA:ARBA00023256, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03101}.
FT   BINDING         68
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         69
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         102
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         256
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         257
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   319 AA;  34354 MW;  C30FC57226F5DBE8 CRC64;
     MESAEVAASS TFGPTPEMEK FLCDLLLDTA QPIAERFRAL FSLRNLHGDG PRCALLQAAR
     DSSNLLAHEA AFALGQMQDA EAIPALEAVL KDLSLHPIVR HEAAEALGAI GLEKSIPLLE
     ESLAADPAVE VQETCELALR RIEQQKNAGV SESTTISPFL SVDPALPAKQ GLSVHQLREI
     LLNEQESMYE RYAALFALRN DSGDAAVSAI VAALGAKSAL LKHEVAYVLG QLQNKAASDA
     LSTVLKNVDE HPMVRHEAAE ALGSIADQES IALLEEFAKD PEPIVSQSCE VALSMLEYER
     SGKSFEFLFL QTPGVQQES
//
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