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Q6RJS2 (DHYS_BRANA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 46. 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 synthase

EC=2.5.1.46
Gene names
Name:DHS
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putrescine By similarity.

Catalytic activity

[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.

Cofactor

NAD By similarity.

Pathway

Protein modification; eIF5A hypusination.

Sequence similarities

Belongs to the deoxyhypusine synthase family.

Ontologies

Keywords
   Biological processHypusine biosynthesis
   LigandNAD
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processdeoxyhypusine biosynthetic process from spermidine

Inferred from electronic annotation. Source: UniProtKB-EC

peptidyl-lysine modification to peptidyl-hypusine

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondeoxyhypusine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Deoxyhypusine synthase
PRO_0000134474

Regions

Nucleotide binding104 – 1085NAD By similarity
Nucleotide binding130 – 1323NAD By similarity
Nucleotide binding309 – 3102NAD By similarity
Nucleotide binding343 – 3442NAD By similarity
Region135 – 1362Spermidine binding By similarity
Region315 – 3173Spermidine binding By similarity
Region324 – 3307Spermidine binding By similarity

Sites

Active site3301Nucleophile By similarity
Binding site1361NAD By similarity
Binding site2371NAD By similarity
Binding site2421Spermidine By similarity
Binding site2841NAD; via amide nitrogen By similarity
Binding site2891Spermidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6RJS2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E8B62D427FF6C51F

FASTA36841,162
        10         20         30         40         50         60 
MEEDRVLSSV HSTVFKESES LEGKCDKIEG YDFNQGVNYP KLLRSMLTTG FQASNLGDVI 

        70         80         90        100        110        120 
DVVNQMLEWR LSDETIAPED CSEEEKDPAY RESVKCKIFL GFTSNLVSSG VRETIRYLVQ 

       130        140        150        160        170        180 
HHMVDVIVTT TGGVEEDLIK CLAPTFKGDF SLPGAYLRSK GLNRIGNLLV PNDNYCKFED 

       190        200        210        220        230        240 
WIIPIFDQML KEQKEESVLW TPSKLLARLG KEINNESSYL YWAYKMNIPV FCRGLTDGSL 

       250        260        270        280        290        300 
GDMLYFHSFR TSGLVIDVVQ DIRAMNGEAV HATPRKTGMI ILGGGLPKHH ICNANMMRNG 

       310        320        330        340        350        360 
ADYAVFINTG QEFDGSDSGA RPDEAVSWGK IRGSAKTVKV YCDATIAFPL LVAETFASKR 


EQSCEHKT 

« Hide

References

[1]"Suppression of deoxyhypusine synthase expression in canola using Agrobacterium tumefaciens-mediated transformation."
Wang T.-W., Wu W., Zhang C.-G., Thompson J.E.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY496434 mRNA. Translation: AAR91928.1.

3D structure databases

ProteinModelPortalQ6RJS2.
SMRQ6RJS2. Positions 27-361.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00354.

Family and domain databases

Gene3D3.40.910.10. 1 hit.
InterProIPR002773. Deoxyhypusine_synthase.
IPR029035. DHS-like_NAD/FAD-binding_dom.
[Graphical view]
PANTHERPTHR11703. PTHR11703. 1 hit.
PfamPF01916. DS. 1 hit.
[Graphical view]
SUPFAMSSF52467. SSF52467. 1 hit.
TIGRFAMsTIGR00321. dhys. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDHYS_BRANA
AccessionPrimary (citable) accession number: Q6RJS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways