Deoxyhypusine hydroxylase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P47120 (DOHH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Deoxyhypusine hydroxylase
Short name=DOHH
EC=1.14.99.29

Alternative name(s):
Deoxyhypusine dioxygenase
Deoxyhypusine monooxygenase
Ligand of eIF5A protein 1

Gene names

Name:	LIA1
Synonyms:	MMD1
Ordered Locus Names:	YJR070C
ORF Names:	J1814

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Ref.8 Ref.12
Catalytic activity	Protein N(6)-(4-aminobutyl)-L-lysine + AH₂ + O₂ = protein N(6)-((R)-4-amino-2-hydroxybutyl)-L-lysine + A + H₂O. Ref.8
Cofactor	Binds 2 Fe²⁺ ions per subunit. Ref.12
Pathway	Protein modification; eIF5A hypusination. HAMAP-Rule MF_03101
Subcellular location	Cytoplasm. Nucleus Ref.6.
Miscellaneous	Present with 39900 molecules/cell in log phase SD medium. HAMAP-Rule MF_03101
Sequence similarities	Belongs to the deoxyhypusine hydroxylase family. Contains 5 HEAT-like PBS-type repeats.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5. Active from pH 6 to 10. Ref.12

Ontologies

Keywords
Biological process	Hypusine biosynthesis
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule cytoskeleton organization Inferred from genetic interaction PubMed 14767070. Source: SGD peptidyl-lysine modification to hypusine Inferred from direct assay Ref.8. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: SGD nucleus Inferred from direct assay Ref.6. Source: SGD
Molecular_function	deoxyhypusine monooxygenase activity Inferred from direct assay Ref.8. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ARO8	P53090	1	EBI-25526,EBI-2042933
GLN1	P32288	1	EBI-25526,EBI-7665
IPP1	P00817	1	EBI-25526,EBI-9338
MRK1	P50873	1	EBI-25526,EBI-2069747
OYE2	Q03558	1	EBI-25526,EBI-12729
RNR2	P09938	1	EBI-25526,EBI-15240

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP-Rule MF_03101

Chain

2 – 325

324

Deoxyhypusine hydroxylase HAMAP-Rule MF_03101

PRO_0000203100

Regions

Repeat

77 – 103

HEAT-like PBS-type 1 HAMAP-Rule MF_03101

Repeat

110 – 136

HEAT-like PBS-type 2 HAMAP-Rule MF_03101

Repeat

202 – 231

HEAT-like PBS-type 3 HAMAP-Rule MF_03101

Repeat

235 – 261

HEAT-like PBS-type 4 HAMAP-Rule MF_03101

Repeat

268 – 294

HEAT-like PBS-type 5 HAMAP-Rule MF_03101

Sites

Metal binding

Iron 1

Metal binding

Iron 1

Metal binding

112

Iron 1

Metal binding

113

Iron 1

Metal binding

237

Iron 2

Metal binding

238

Iron 2

Metal binding

270

Iron 2

Metal binding

271

Iron 2

Amino acid modifications

Modified residue

N-acetylserine Ref.5

Modified residue

169

Phosphoserine Ref.11

Modified residue

281

Phosphoserine Ref.9 Ref.10 Ref.11

Experimental info

Mutagenesis

H → A: Abolishes both iron-binding and enzyme activity. Ref.12

Mutagenesis

E → A: Abolishes enzyme activity and impairs iron-binding. Ref.12

Mutagenesis

112

H → A: Abolishes both iron-binding and enzyme activity. Ref.12

Mutagenesis

113

E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12

Mutagenesis

116

E → A: Abolishes substrate-binding and enzyme activity. Ref.12

Mutagenesis

116

E → D: Reduces enzyme activity by 97%. Ref.12

Mutagenesis

237

H → A: Abolishes both iron-binding and enzyme activity. Ref.12

Mutagenesis

238

E → A: Abolishes substrate-binding, enzyme activity, and impairs iron-binding. Ref.12

Mutagenesis

270

H → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12

Mutagenesis

271

E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12

Mutagenesis

274

E → A: Abolishes substrate-binding. Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P47120 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AB36A73B40466CD5
Show »

FASTA

325

36,165

        10         20         30         40         50         60 
MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE FATKPEEAKK 

        70         80         90        100        110        120 
AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV MLDQNQEPMV RHEAAEALGA 

       130        140        150        160        170        180 
LGDKDSLDDL NKAAKEDPHV AVRETCELAI NRINWTHGGA KDKENLQQSL YSSIDPAPPL 

       190        200        210        220        230        240 
PLEKDATIPE LQALLNDPKQ PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA 

       250        260        270        280        290        300 
YVFGQIGSPA AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR 

       310        320 
ESCIVALDMY DYENSNELEY APTAN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, MASS SPECTROMETRY.
[11]	"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-169 AND SER-281, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49570 Genomic DNA. Translation: CAA89598.1. L47993 Genomic DNA. Translation: AAB39296.1. BK006943 Genomic DNA. Translation: DAA08857.1.
PIR	S57089.
RefSeq	NP_012604.1. NM_001181728.1.
3D structure databases
ProteinModelPortal	P47120.
SMR	P47120. Positions 186-216, 252-310.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2829N.
IntAct	P47120. 9 interactions.
MINT	MINT-539495.
STRING	4932.YJR070C.
Proteomic databases
PaxDb	P47120.
PeptideAtlas	P47120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJR070C; YJR070C; YJR070C.
GeneID	853534.
KEGG	sce:YJR070C.
Organism-specific databases
CYGD	YJR070c.
SGD	S000003831. LIA1.
Phylogenomic databases
eggNOG	COG1413.
GeneTree	ENSGT00500000044957.
HOGENOM	HOG000248665.
KO	K06072.
OMA	FRHEVAF.
OrthoDB	EOG4MSH78.
Enzyme and pathway databases
UniPathway	UPA00354.
Gene expression databases
Genevestigator	P47120.
GermOnline	YJR070C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.25.10.10. 1 hit.
HAMAP	MF_03101. Deoxyhypusine_hydroxylase.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR004155. PBS_lyase_HEAT. [Graphical view]
Pfam	PF03130. HEAT_PBS. 3 hits. [Graphical view]
SMART	SM00567. EZ_HEAT. 5 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	974236.

Entry information

Entry name

DOHH_YEAST

Accession

Primary (citable) accession number: P47120
Secondary accession number(s): D6VWP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents