Q6FUV3 (DOHH_CANGA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Deoxyhypusine hydroxylase Short name=DOHH EC=1.14.99.29 Alternative name(s): Deoxyhypusine dioxygenase Deoxyhypusine monooxygenase | ||||
| Gene names |
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| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome] | ||||
| Taxonomic identifier | 284593 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › ![]() |
Protein attributes
| Sequence length | 322 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. HAMAP-Rule MF_03101 |
| Pathway | Protein modification; eIF5A hypusination. HAMAP-Rule MF_03101 |
| Subcellular location | Cytoplasm. Nucleus By similarity HAMAP-Rule MF_03101. |
| Sequence similarities | Belongs to the deoxyhypusine hydroxylase family. Contains 4 HEAT-like PBS-type repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hypusine biosynthesis |
| Cellular component | Cytoplasm Nucleus |
| Domain | Repeat |
| Ligand | Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | peptidyl-lysine modification to hypusine Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | deoxyhypusine monooxygenase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 322 | 322 | Deoxyhypusine hydroxylase HAMAP-Rule MF_03101 | PRO_0000283659 | |||||
Regions | |||||||||
| Repeat | 109 – 135 | 27 | HEAT-like PBS-type 1 HAMAP-Rule MF_03101 | ||||||
| Repeat | 203 – 229 | 27 | HEAT-like PBS-type 2 HAMAP-Rule MF_03101 | ||||||
| Repeat | 234 – 260 | 27 | HEAT-like PBS-type 3 HAMAP-Rule MF_03101 | ||||||
| Repeat | 267 – 293 | 27 | HEAT-like PBS-type 4 HAMAP-Rule MF_03101 | ||||||
Sites | |||||||||
| Metal binding | 78 | 1 | Iron 1 By similarity | ||||||
| Metal binding | 79 | 1 | Iron 1 By similarity | ||||||
| Metal binding | 111 | 1 | Iron 1 By similarity | ||||||
| Metal binding | 112 | 1 | Iron 1 By similarity | ||||||
| Metal binding | 236 | 1 | Iron 2 By similarity | ||||||
| Metal binding | 237 | 1 | Iron 2 By similarity | ||||||
| Metal binding | 269 | 1 | Iron 2 By similarity | ||||||
| Metal binding | 270 | 1 | Iron 2 By similarity | ||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR380952 Genomic DNA. Translation: CAG58915.1. |
| RefSeq | XP_445991.1. XM_445991.1. |
3D structure databases | |
| ProteinModelPortal | Q6FUV3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2887799. |
| KEGG | cgr:CAGL0F00407g. |
Phylogenomic databases | |
| HOGENOM | HOG000248665. |
| KO | K06072. |
| OMA | RIEWINS. |
| OrthoDB | EOG4MSH78. |
Enzyme and pathway databases | |
| UniPathway | UPA00354. |
Family and domain databases | |
| Gene3D | 1.25.10.10. 1 hit. |
| HAMAP | MF_03101. Deoxyhypusine_hydroxylase. |
| InterPro | IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR027517. Deoxyhypusine_hydroxylase. IPR004155. PBS_lyase_HEAT. [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... |
Entry information
| Entry name | DOHH_CANGA | ||||||||
| Accession | Primary (citable) accession number: Q6FUV3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
