DOHH_KLULA
ID DOHH_KLULA Reviewed; 322 AA.
AC Q6CV81;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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: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=LIA1 {ECO:0000255|HAMAP-Rule:MF_03101};
GN OrderedLocusNames=KLLA0B14080g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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: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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03101};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03101};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03101};
CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC Rule:MF_03101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03101}.
CC Nucleus {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; CR382122; CAH02551.1; -; Genomic_DNA.
DR RefSeq; XP_452158.1; XM_452158.1.
DR AlphaFoldDB; Q6CV81; -.
DR SMR; Q6CV81; -.
DR STRING; 28985.XP_452158.1; -.
DR EnsemblFungi; CAH02551; CAH02551; KLLA0_B14080g.
DR GeneID; 2897036; -.
DR KEGG; kla:KLLA0_B14080g; -.
DR eggNOG; KOG0567; Eukaryota.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q6CV81; -.
DR OMA; CIQILNR; -.
DR UniPathway; UPA00354; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:EnsemblFungi.
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; IPR021133; HEAT_type_2.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR SMART; SM00567; EZ_HEAT; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW Nucleus; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..322
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000283667"
FT REPEAT 76..102
FT /note="HEAT-like PBS-type 1"
FT REPEAT 109..135
FT /note="HEAT-like PBS-type 2"
FT REPEAT 267..293
FT /note="HEAT-like PBS-type 3"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ SEQUENCE 322 AA; 36359 MW; F0D713105D85C20D CRC64;
MSTNFEKHFE VDVDNCSLEQ LRDILVNNSG KAPLANRFRA LFNLKGHAEE FASKPEDALK
ATQYLAEAFG DESELLKHEV AYVLGQTKNM AGAPLLRDVL ADDKQQCMVR HEAAEALGAL
NDVDSLDILE KYFKEDPLLE IRQTCELAID RIKWETSEEG RREALQESLY SSIDPAPPFS
LEKDYKIQEL KDILNDQNRP LFERYRAMFR LRDIGNDEAC LALASGFDDP SALFKHEIAY
VFGQICNPVV VPHLKEVLAR PEEAPMVRHE AAEALGSIAT DDVLPVLKEH LKDSDSVVRE
SAIVALDMYE YENSNDLEYA PV
