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Q4HZ35 (DOHH_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LIA1
ORF Names:FGSG_09773
OrganismGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum) [Reference proteome]
Taxonomic identifier229533 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella ›

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_03101

Catalytic activity

Protein N(6)-(4-aminobutyl)-L-lysine + AH2 + O2 = protein N(6)-((R)-4-amino-2-hydroxybutyl)-L-lysine + A + H2O. HAMAP-Rule MF_03101

Cofactor

Binds 2 Fe2+ ions per subunit By similarity.

Pathway

Protein modification; eIF5A hypusination. HAMAP-Rule MF_03101

Subcellular location

Cytoplasm. Nucleus By similarity.

Sequence similarities

Belongs to the deoxyhypusine hydroxylase family.

Contains 5 HEAT-like PBS-type repeats.

Ontologies

Keywords
   Biological processHypusine biosynthesis
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandIron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule cytoskeleton organization

Inferred from electronic annotation. Source: EnsemblFungi

peptidyl-lysine modification to hypusine

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondeoxyhypusine monooxygenase activity

Inferred from electronic annotation. Source: EC

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 – 337337Deoxyhypusine hydroxylase HAMAP-Rule MF_03101
PRO_0000283666

Regions

Repeat73 – 9927HEAT-like PBS-type 1 HAMAP-Rule MF_03101
Repeat106 – 13227HEAT-like PBS-type 2 HAMAP-Rule MF_03101
Repeat202 – 23534HEAT-like PBS-type 3 HAMAP-Rule MF_03101
Repeat240 – 26627HEAT-like PBS-type 4 HAMAP-Rule MF_03101
Repeat273 – 30028HEAT-like PBS-type 5 HAMAP-Rule MF_03101

Sites

Metal binding751Iron 1 By similarity
Metal binding761Iron 1 By similarity
Metal binding1081Iron 1 By similarity
Metal binding1091Iron 1 By similarity
Metal binding2421Iron 2 By similarity
Metal binding2431Iron 2 By similarity
Metal binding2751Iron 2 By similarity
Metal binding2761Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4HZ35 [UniParc].

Last modified August 16, 2005. Version 1.
Checksum: 4806FBD8DB5E74F9

FASTA33736,535
        10         20         30         40         50         60 
MSPSADTPEI SNSADSTVLS LKKSLCSEDS PLPIRFRALF SLKHVATTAD DDATRVAAIE 

        70         80         90        100        110        120 
AIAAGFASPS ALLKHELAYC LGQTGNTAAV KPLRQVLSDL KEDPMCRHEA AEALGALGWA 

       130        140        150        160        170        180 
DNLDILREYR DRKEEDISIV ETCEIAIERI EWENSAERQK EKLRPSDFAS IDPAPPMPES 

       190        200        210        220        230        240 
DKEAEVEDLG RKLMDTNADL FSRYRAMFAL RDLASPPDLP TATPAVLALA KGLSDSSALF 

       250        260        270        280        290        300 
RHEIAFVFGQ LSHPASIPAL TEALSNTNEA SMVRHEAAEA LGSLGEKDGV EDTLRKFLHD 

       310        320        330 
KEKVVRESCI VALDIAEYEK GEDAEYALIP ESAGAAA

« Hide

References

« Hide 'large scale' references
[1]"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization."
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. expand/collapse author list , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.
Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[2]"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. expand/collapse author list , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.

Cross-references

Sequence databases

RefSeqXP_389949.1. XM_389949.1.

3D structure databases

ProteinModelPortalQ4HZ35.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFGSG_09773T0; FGSG_09773P0; FGSG_09773.
GeneID2791492.
KEGGfgr:FG09773.1.

Phylogenomic databases

KOK06072.

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.
IPR021133. HEAT_type_2.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
SMARTSM00567. EZ_HEAT. 6 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDOHH_GIBZE
AccessionPrimary (citable) accession number: Q4HZ35
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: August 16, 2005
Last modified: March 6, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents