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P47120

- DOHH_YEAST

UniProt

P47120 - DOHH_YEAST

Protein

Deoxyhypusine hydroxylase

Gene

LIA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.UniRule annotation

    Catalytic activityi

    [eIF5A]-deoxyhypusine + AH2 + O2 = [eIF5A]-hypusine + A + H2O.1 PublicationUniRule annotation

    Cofactori

    Binds 2 Fe2+ ions per subunit.1 PublicationUniRule annotation

    pH dependencei

    Optimum pH is 7.5. Active from pH 6 to 10.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Iron 1
    Metal bindingi80 – 801Iron 1
    Metal bindingi112 – 1121Iron 1
    Metal bindingi113 – 1131Iron 1
    Metal bindingi237 – 2371Iron 2
    Metal bindingi238 – 2381Iron 2
    Metal bindingi270 – 2701Iron 2
    Metal bindingi271 – 2711Iron 2

    GO - Molecular functioni

    1. deoxyhypusine monooxygenase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. microtubule cytoskeleton organization Source: SGD
    2. peptidyl-lysine modification to peptidyl-hypusine Source: SGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Hypusine biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31703-MONOMER.
    UniPathwayiUPA00354.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyhypusine hydroxylaseUniRule annotation (EC:1.14.99.29UniRule annotation)
    Short name:
    DOHHUniRule annotation
    Alternative name(s):
    Deoxyhypusine dioxygenaseUniRule annotation
    Deoxyhypusine monooxygenaseUniRule annotation
    Ligand of eIF5A protein 1UniRule annotation
    Gene namesi
    Name:LIA1UniRule annotation
    Synonyms:MMD1
    Ordered Locus Names:YJR070C
    ORF Names:J1814
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR070c.
    SGDiS000003831. LIA1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
    Mutagenesisi80 – 801E → A: Abolishes enzyme activity and impairs iron-binding. 1 Publication
    Mutagenesisi112 – 1121H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
    Mutagenesisi113 – 1131E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
    Mutagenesisi116 – 1161E → A: Abolishes substrate-binding and enzyme activity. 1 Publication
    Mutagenesisi116 – 1161E → D: Reduces enzyme activity by 97%. 1 Publication
    Mutagenesisi237 – 2371H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
    Mutagenesisi238 – 2381E → A: Abolishes substrate-binding, enzyme activity, and impairs iron-binding. 1 Publication
    Mutagenesisi270 – 2701H → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
    Mutagenesisi271 – 2711E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
    Mutagenesisi274 – 2741E → A: Abolishes substrate-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 325324Deoxyhypusine hydroxylasePRO_0000203100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 PublicationUniRule annotation
    Modified residuei126 – 1261Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphothreonine1 Publication
    Modified residuei281 – 2811Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP47120.
    PaxDbiP47120.
    PeptideAtlasiP47120.

    Expressioni

    Gene expression databases

    GenevestigatoriP47120.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HYP2P233012EBI-25526,EBI-9033

    Protein-protein interaction databases

    BioGridi33827. 67 interactions.
    DIPiDIP-2829N.
    IntActiP47120. 6 interactions.
    MINTiMINT-539495.
    STRINGi4932.YJR070C.

    Structurei

    3D structure databases

    ProteinModelPortaliP47120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati77 – 10327HEAT-like PBS-type 1Add
    BLAST
    Repeati110 – 13627HEAT-like PBS-type 2Add
    BLAST
    Repeati202 – 23130HEAT-like PBS-type 3Add
    BLAST
    Repeati235 – 26127HEAT-like PBS-type 4Add
    BLAST
    Repeati268 – 29427HEAT-like PBS-type 5Add
    BLAST

    Sequence similaritiesi

    Belongs to the deoxyhypusine hydroxylase family.UniRule annotation
    Contains 5 HEAT-like PBS-type repeats.UniRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1413.
    GeneTreeiENSGT00500000044957.
    HOGENOMiHOG000248665.
    KOiK06072.
    OMAiRESCQVA.
    OrthoDBiEOG7QC85Z.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    HAMAPiMF_03101. Deoxyhypusine_hydroxylase.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR027517. Deoxyhypusine_hydroxylase.
    IPR004155. PBS_lyase_HEAT.
    [Graphical view]
    PfamiPF03130. HEAT_PBS. 3 hits.
    [Graphical view]
    SMARTiSM00567. EZ_HEAT. 5 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P47120-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE    50
    FATKPEEAKK AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV 100
    MLDQNQEPMV RHEAAEALGA LGDKDSLDDL NKAAKEDPHV AVRETCELAI 150
    NRINWTHGGA KDKENLQQSL YSSIDPAPPL PLEKDATIPE LQALLNDPKQ 200
    PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA YVFGQIGSPA 250
    AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR 300
    ESCIVALDMY DYENSNELEY APTAN 325
    Length:325
    Mass (Da):36,165
    Last modified:February 1, 1996 - v1
    Checksum:iAB36A73B40466CD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49570 Genomic DNA. Translation: CAA89598.1.
    L47993 Genomic DNA. Translation: AAB39296.1.
    BK006943 Genomic DNA. Translation: DAA08857.1.
    PIRiS57089.
    RefSeqiNP_012604.1. NM_001181728.1.

    Genome annotation databases

    EnsemblFungiiYJR070C; YJR070C; YJR070C.
    GeneIDi853534.
    KEGGisce:YJR070C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49570 Genomic DNA. Translation: CAA89598.1 .
    L47993 Genomic DNA. Translation: AAB39296.1 .
    BK006943 Genomic DNA. Translation: DAA08857.1 .
    PIRi S57089.
    RefSeqi NP_012604.1. NM_001181728.1.

    3D structure databases

    ProteinModelPortali P47120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33827. 67 interactions.
    DIPi DIP-2829N.
    IntActi P47120. 6 interactions.
    MINTi MINT-539495.
    STRINGi 4932.YJR070C.

    Proteomic databases

    MaxQBi P47120.
    PaxDbi P47120.
    PeptideAtlasi P47120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR070C ; YJR070C ; YJR070C .
    GeneIDi 853534.
    KEGGi sce:YJR070C.

    Organism-specific databases

    CYGDi YJR070c.
    SGDi S000003831. LIA1.

    Phylogenomic databases

    eggNOGi COG1413.
    GeneTreei ENSGT00500000044957.
    HOGENOMi HOG000248665.
    KOi K06072.
    OMAi RESCQVA.
    OrthoDBi EOG7QC85Z.

    Enzyme and pathway databases

    UniPathwayi UPA00354 .
    BioCyci YEAST:G3O-31703-MONOMER.

    Miscellaneous databases

    NextBioi 974236.
    PROi P47120.

    Gene expression databases

    Genevestigatori P47120.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    HAMAPi MF_03101. Deoxyhypusine_hydroxylase.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR027517. Deoxyhypusine_hydroxylase.
    IPR004155. PBS_lyase_HEAT.
    [Graphical view ]
    Pfami PF03130. HEAT_PBS. 3 hits.
    [Graphical view ]
    SMARTi SM00567. EZ_HEAT. 5 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
      Huang M.-E., Manus V., Chuat J.-C., Galibert F.
      Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
      Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
      Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme."
      Park J.-H., Aravind L., Wolff E.C., Kaevel J., Kim Y.S., Park M.H.
      Proc. Natl. Acad. Sci. U.S.A. 103:51-56(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-187 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site."
      Cano V.S., Medrano F.J., Park M.H., Valentini S.R.
      Amino Acids 38:479-490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF HIS-79; GLU-80; HIS-112; GLU-113; GLU-116; HIS-237; GLU-238; HIS-270; GLU-271 AND GLU-274, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiDOHH_YEAST
    AccessioniPrimary (citable) accession number: P47120
    Secondary accession number(s): D6VWP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 39900 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3