DOHH_YEAST
ID DOHH_YEAST Reviewed; 325 AA.
AC P47120; D6VWP1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
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};
DE AltName: Full=Ligand of eIF5A protein 1 {ECO:0000255|HAMAP-Rule:MF_03101};
GN Name=LIA1 {ECO:0000255|HAMAP-Rule:MF_03101}; Synonyms=MMD1;
GN OrderedLocusNames=YJR070C; ORFNames=J1814;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT "Linking genome and proteome by mass spectrometry: large-scale
RT identification of yeast proteins from two dimensional gels.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN [5]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16371467; DOI=10.1073/pnas.0509348102;
RA Park J.-H., Aravind L., Wolff E.C., Kaevel J., Kim Y.S., Park M.H.;
RT "Molecular cloning, expression, and structural prediction of deoxyhypusine
RT hydroxylase: a HEAT-repeat-containing metalloenzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:51-56(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-187 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP FUNCTION, COFACTOR, MUTAGENESIS OF HIS-79; GLU-80; HIS-112; GLU-113;
RP GLU-116; HIS-237; GLU-238; HIS-270; GLU-271 AND GLU-274, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19956996; DOI=10.1007/s00726-009-0407-8;
RA Cano V.S., Medrano F.J., Park M.H., Valentini S.R.;
RT "Evidence for conformational changes in the yeast deoxyhypusine hydroxylase
RT Lia1 upon iron displacement from its active site.";
RL Amino Acids 38:479-490(2010).
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, ECO:0000269|PubMed:16371467,
CC ECO:0000269|PubMed:19956996}.
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:16371467};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:19956996};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:19956996};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 6 to 10.
CC {ECO:0000269|PubMed:19956996};
CC -!- PATHWAY: Protein modification; eIF5A hypusination. {ECO:0000255|HAMAP-
CC Rule:MF_03101}.
CC -!- INTERACTION:
CC P47120; P23301: HYP2; NbExp=2; IntAct=EBI-25526, EBI-9033;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03101,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 39900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_03101}.
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DR EMBL; Z49570; CAA89598.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39296.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08857.1; -; Genomic_DNA.
DR PIR; S57089; S57089.
DR RefSeq; NP_012604.1; NM_001181728.1.
DR AlphaFoldDB; P47120; -.
DR SMR; P47120; -.
DR BioGRID; 33827; 248.
DR DIP; DIP-2829N; -.
DR IntAct; P47120; 10.
DR MINT; P47120; -.
DR STRING; 4932.YJR070C; -.
DR iPTMnet; P47120; -.
DR MaxQB; P47120; -.
DR PaxDb; P47120; -.
DR PRIDE; P47120; -.
DR EnsemblFungi; YJR070C_mRNA; YJR070C; YJR070C.
DR GeneID; 853534; -.
DR KEGG; sce:YJR070C; -.
DR SGD; S000003831; LIA1.
DR VEuPathDB; FungiDB:YJR070C; -.
DR eggNOG; KOG0567; Eukaryota.
DR HOGENOM; CLU_053974_0_0_1; -.
DR InParanoid; P47120; -.
DR OMA; CIQILNR; -.
DR BioCyc; YEAST:G3O-31703-MON; -.
DR Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine.
DR UniPathway; UPA00354; -.
DR PRO; PR:P47120; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47120; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:SGD.
DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IDA:SGD.
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 Acetylation; Cytoplasm; Hypusine biosynthesis; Iron; Metal-binding;
KW Monooxygenase; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:9298649"
FT CHAIN 2..325
FT /note="Deoxyhypusine hydroxylase"
FT /id="PRO_0000203100"
FT REPEAT 77..103
FT /note="HEAT-like PBS-type 1"
FT REPEAT 110..136
FT /note="HEAT-like PBS-type 2"
FT REPEAT 202..231
FT /note="HEAT-like PBS-type 3"
FT REPEAT 235..261
FT /note="HEAT-like PBS-type 4"
FT REPEAT 268..294
FT /note="HEAT-like PBS-type 5"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 271
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03101,
FT ECO:0000269|PubMed:9298649"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 79
FT /note="H->A: Abolishes both iron-binding and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 80
FT /note="E->A: Abolishes enzyme activity and impairs iron-
FT binding."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 112
FT /note="H->A: Abolishes both iron-binding and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 113
FT /note="E->A: Abolishes iron-binding, substrate-binding, and
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 116
FT /note="E->A: Abolishes substrate-binding and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 116
FT /note="E->D: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 237
FT /note="H->A: Abolishes both iron-binding and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 238
FT /note="E->A: Abolishes substrate-binding, enzyme activity,
FT and impairs iron-binding."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 270
FT /note="H->A: Abolishes iron-binding, substrate-binding, and
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 271
FT /note="E->A: Abolishes iron-binding, substrate-binding, and
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:19956996"
FT MUTAGEN 274
FT /note="E->A: Abolishes substrate-binding."
FT /evidence="ECO:0000269|PubMed:19956996"
SQ SEQUENCE 325 AA; 36165 MW; AB36A73B40466CD5 CRC64;
MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE FATKPEEAKK
AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV MLDQNQEPMV RHEAAEALGA
LGDKDSLDDL NKAAKEDPHV AVRETCELAI NRINWTHGGA KDKENLQQSL YSSIDPAPPL
PLEKDATIPE LQALLNDPKQ PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA
YVFGQIGSPA AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR
ESCIVALDMY DYENSNELEY APTAN
