DOHH_SCHPO
ID DOHH_SCHPO Reviewed; 318 AA.
AC Q9P6K9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
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; Synonyms=mmd1; ORFNames=SPAC30C2.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=14767070; DOI=10.1091/mbc.e03-06-0371;
RA Weir B.A., Yaffe M.P.;
RT "Mmd1p, a novel, conserved protein essential for normal mitochondrial
RT morphology and distribution in the fission yeast Schizosaccharomyces
RT pombe.";
RL Mol. Biol. Cell 15:1656-1665(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; CU329670; CAB90789.1; -; Genomic_DNA.
DR RefSeq; NP_594654.1; NM_001020083.2.
DR AlphaFoldDB; Q9P6K9; -.
DR SMR; Q9P6K9; -.
DR BioGRID; 277967; 10.
DR STRING; 4896.SPAC30C2.02.1; -.
DR MaxQB; Q9P6K9; -.
DR PaxDb; Q9P6K9; -.
DR EnsemblFungi; SPAC30C2.02.1; SPAC30C2.02.1:pep; SPAC30C2.02.
DR GeneID; 2541465; -.
DR KEGG; spo:SPAC30C2.02; -.
DR PomBase; SPAC30C2.02; -.
DR VEuPathDB; FungiDB:SPAC30C2.02; -.
DR eggNOG; KOG0567; Eukaryota.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; Q9P6K9; -.
DR OMA; CIQILNR; -.
DR PhylomeDB; Q9P6K9; -.
DR Reactome; R-SPO-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:Q9P6K9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; ISO:PomBase.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IC:PomBase.
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; IPR000225; Armadillo.
DR InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR SMART; SM00567; EZ_HEAT; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase;
KW Nucleus; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..318
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000283672"
FT REPEAT 96..122
FT /note="HEAT-like PBS-type 1"
FT REPEAT 194..220
FT /note="HEAT-like PBS-type 2"
FT REPEAT 225..251
FT /note="HEAT-like PBS-type 3"
FT REPEAT 258..284
FT /note="HEAT-like PBS-type 4"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101"
SQ SEQUENCE 318 AA; 35689 MW; 8A4BDE165C767282 CRC64;
MSSEPVPQAV IDELERVLVN LDKSNPLSFR YRALFSLNAL AKKGDKRAVD AIYKAFIDDS
ELLKHEMAYV MGQSGQQYAV QPLINIVNDL DQQVMVRHEA AEALGALGFT ESLPVLEKYY
KEDPLAPIRE TCELAIARIQ WKNGLDKNNE KITPSMYDSV VDPAPPMPDH EQDVKSEVAK
LRSEIVDQNL PLFYRYRVMF RLRNIGNEEA VLALTDGFKD PSPLFRHEIA FVFGQMIAPA
SVPALIKVLE NTEEVPMVRH EAAEALGGIA NDECLPVLKK FSKDDVRVVA ESCIVALDMI
EYEKSGDMEY AYIPKVSA
