Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Deoxyhypusine hydroxylase

Gene

LIA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.UniRule annotation1 Publication

Cofactori

Fe2+UniRule annotation1 PublicationNote: Binds 2 Fe2+ ions per subunit.UniRule annotation1 Publication

pH dependencei

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

Pathway:ieIF5A hypusination

This protein is involved in the pathway eIF5A hypusination, which is part of Protein modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway eIF5A hypusination and in Protein modification.

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

  • deoxyhypusine monooxygenase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • microtubule cytoskeleton organization Source: SGD
  • peptidyl-lysine modification to peptidyl-hypusine Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Hypusine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31703-MONOMER.
ReactomeiREACT_324287. Hypusine synthesis from eIF5A-lysine.
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 Componenti: Chromosome X

Organism-specific databases

CYGDiYJR070c.
EuPathDBiFungiDB:YJR070C.
SGDiS000003831. LIA1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 – 11RemovedUniRule annotation1 Publication
Chaini2 – 325324Deoxyhypusine hydroxylasePRO_0000203100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotation1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei187 – 1871Phosphothreonine1 Publication
Modified residuei281 – 2811Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP47120.
PaxDbiP47120.
PeptideAtlasiP47120.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP47120.
SMRiP47120. Positions 95-121, 186-215, 221-310.
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.
InParanoidiP47120.
KOiK06072.
OMAiHEAAVPQ.
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

        10         20         30         40         50
MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE
60 70 80 90 100
FATKPEEAKK AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV
110 120 130 140 150
MLDQNQEPMV RHEAAEALGA LGDKDSLDDL NKAAKEDPHV AVRETCELAI
160 170 180 190 200
NRINWTHGGA KDKENLQQSL YSSIDPAPPL PLEKDATIPE LQALLNDPKQ
210 220 230 240 250
PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA YVFGQIGSPA
260 270 280 290 300
AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR
310 320
ESCIVALDMY DYENSNELEY APTAN
Length:325
Mass (Da):36,165
Last modified:February 1, 1996 - v1
Checksum:iAB36A73B40466CD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP47120.
SMRiP47120. Positions 95-121, 186-215, 221-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP47120.
PaxDbiP47120.
PeptideAtlasiP47120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYJR070c.
EuPathDBiFungiDB:YJR070C.
SGDiS000003831. LIA1.

Phylogenomic databases

eggNOGiCOG1413.
GeneTreeiENSGT00500000044957.
HOGENOMiHOG000248665.
InParanoidiP47120.
KOiK06072.
OMAiHEAAVPQ.
OrthoDBiEOG7QC85Z.

Enzyme and pathway databases

UniPathwayiUPA00354.
BioCyciYEAST:G3O-31703-MONOMER.
ReactomeiREACT_324287. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

NextBioi974236.
PROiP47120.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.