Q2YPB8 (HISX_BRUA2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 54.
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: Histidinol dehydrogenase Short name=HDH EC=1.1.1.23 | ||||
| Gene names |
| ||||
| Organism | Brucella abortus (strain 2308) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 359391 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024 |
| Catalytic activity | L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024 |
| Sequence similarities | Belongs to the histidinol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 430 | 430 | Histidinol dehydrogenase HAMAP-Rule MF_01024 | PRO_0000229851 | |||||
Sites | |||||||||
| Active site | 327 | 1 | Proton acceptor By similarity | ||||||
| Active site | 328 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 259 | 1 | Zinc By similarity | ||||||
| Metal binding | 262 | 1 | Zinc By similarity | ||||||
| Metal binding | 361 | 1 | Zinc By similarity | ||||||
| Metal binding | 420 | 1 | Zinc By similarity | ||||||
| Binding site | 130 | 1 | NAD By similarity | ||||||
| Binding site | 191 | 1 | NAD By similarity | ||||||
| Binding site | 214 | 1 | NAD By similarity | ||||||
| Binding site | 237 | 1 | Substrate By similarity | ||||||
| Binding site | 259 | 1 | Substrate By similarity | ||||||
| Binding site | 262 | 1 | Substrate By similarity | ||||||
| Binding site | 328 | 1 | Substrate By similarity | ||||||
| Binding site | 361 | 1 | Substrate By similarity | ||||||
| Binding site | 415 | 1 | Substrate By similarity | ||||||
| Binding site | 420 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM040264 Genomic DNA. Translation: CAJ10241.1. |
| RefSeq | YP_413759.1. NC_007618.1. |
3D structure databases | |
| ProteinModelPortal | Q2YPB8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 359391.BAB1_0285. |
Proteomic databases | |
| PRIDE | Q2YPB8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAJ10241; CAJ10241; BAB1_0285. |
| GeneID | 3788752. |
| KEGG | bmf:BAB1_0285. |
| PATRIC | 17843419. VBIBruMel86222_0297. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0141. |
| HOGENOM | HOG000243914. |
| KO | K00013. |
| OMA | ARDRIEF. |
| ProtClustDB | PRK00877. |
Enzyme and pathway databases | |
| BioCyc | BMEL359391:GJOQ-290-MONOMER. |
| UniPathway | UPA00031; UER00014. |
Family and domain databases | |
| HAMAP | MF_01024. HisD. |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR022695. Histidinol_DH_monofunct. IPR012131. Hstdl_DH. [Graphical view] |
| Pfam | PF00815. Histidinol_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000099. Histidinol_dh. 1 hit. |
| PRINTS | PR00083. HOLDHDRGNASE. |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR00069. hisD. 1 hit. |
| PROSITE | PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HISX_BRUA2 | ||||||||
| Accession | Primary (citable) accession number: Q2YPB8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella abortus strain 2308 Brucella abortus (strain 2308): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
