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Q0VC53 (DOHH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyhypusine hydroxylase

Short name=DOHH
EC=1.14.99.29
Alternative name(s):
Deoxyhypusine dioxygenase
Deoxyhypusine monooxygenase
Gene names
Name:DOHH
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.1

Catalytic activity

[eIF5A]-deoxyhypusine + AH2 + O2 = [eIF5A]-hypusine + A + H2O. HAMAP-Rule MF_03101

Cofactor

Binds 2 Fe2+ ions per subunit By similarity. HAMAP-Rule MF_03101

Pathway

Protein modification; eIF5A hypusination. HAMAP-Rule MF_03101

Sequence similarities

Belongs to the deoxyhypusine hydroxylase family.

Contains 6 HEAT-like PBS-type repeats.

Ontologies

Keywords
   Biological processHypusine biosynthesis
   DomainRepeat
   LigandIron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-lysine modification to peptidyl-hypusine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functiondeoxyhypusine monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Deoxyhypusine hydroxylase HAMAP-Rule MF_03101
PRO_0000326490

Regions

Repeat23 – 4927HEAT-like PBS-type 1 HAMAP-Rule MF_03101
Repeat54 – 8027HEAT-like PBS-type 2 HAMAP-Rule MF_03101
Repeat87 – 11327HEAT-like PBS-type 3 HAMAP-Rule MF_03101
Repeat175 – 20127HEAT-like PBS-type 4 HAMAP-Rule MF_03101
Repeat206 – 23227HEAT-like PBS-type 5 HAMAP-Rule MF_03101
Repeat239 – 26527HEAT-like PBS-type 6 HAMAP-Rule MF_03101

Sites

Metal binding561Iron 1 By similarity
Metal binding571Iron 1 By similarity
Metal binding891Iron 1 By similarity
Metal binding901Iron 1 By similarity
Metal binding2081Iron 2 By similarity
Metal binding2091Iron 2 By similarity
Metal binding2411Iron 2 By similarity
Metal binding2421Iron 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Mutagenesis571E → G: Severe reduction in activity. Ref.1
Sequence conflict2661P → S in ABL86660. Ref.1
Sequence conflict2661P → S in ABL86661. Ref.1
Sequence conflict2661P → S in ABL86662. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q0VC53 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 4487BA5BDFC61AB9

FASTA30333,261
        10         20         30         40         50         60 
MVTEQEVEAV GQTLVDPGQP LQARFRALFT LRGLGGPVAI SWISRAFDDD SALLKHELAY 

        70         80         90        100        110        120 
CLGQMQDRRA IPVLLDVLRD TRQEPMVRHE AGEALGAIGD PEVLEILKQY STDPVVEVAE 

       130        140        150        160        170        180 
TCQLAVRRLE WLQQHGGESA VRGPYLSVDP APPAEERDLG QLREALLDEA RPLFDRYRAM 

       190        200        210        220        230        240 
FALRDAGGKE AALALAEGLR CGSALFRHEI GYVLGQMQHE AAVPQLAAAL AQPTENPMVR 

       250        260        270        280        290        300 
HECAEALGAI ARPACLAALR AHVADPERVV RESCEVALDM YEYETGSTFQ YADGLERLRS 


PLS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of bovine deoxyhypusine hydroxylase cDNA and homologs."
Huang J.-K., Cui Y., Chen C.-H., Clampitt D., Lin C.-T., Wen L.
Protein Expr. Purif. 54:126-133(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLU-57.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ990881 mRNA. Translation: ABL86660.1.
DQ990882 mRNA. Translation: ABL86661.1.
DQ990883 mRNA. Translation: ABL86662.1.
BC120351 mRNA. Translation: AAI20352.1.
RefSeqNP_001069354.1. NM_001075886.1.
XP_005209005.1. XM_005208948.1.
UniGeneBt.10480.

3D structure databases

ProteinModelPortalQ0VC53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000006935.

Proteomic databases

PRIDEQ0VC53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006935; ENSBTAP00000006935; ENSBTAG00000005272.
GeneID526521.
KEGGbta:526521.

Organism-specific databases

CTD83475.

Phylogenomic databases

eggNOGCOG1413.
GeneTreeENSGT00500000044957.
HOGENOMHOG000248665.
HOVERGENHBG081460.
InParanoidQ0VC53.
KOK06072.
OMARESCQVA.
OrthoDBEOG75TMCH.
TreeFamTF105626.

Enzyme and pathway databases

UniPathwayUPA00354.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
HAMAPMF_03101. Deoxyhypusine_hydroxylase.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027517. Deoxyhypusine_hydroxylase.
IPR021133. HEAT_type_2.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
SMARTSM00567. EZ_HEAT. 6 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20874385.

Entry information

Entry nameDOHH_BOVIN
AccessionPrimary (citable) accession number: Q0VC53
Secondary accession number(s): A5H2K6, A5H2K8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways