Reviewed,
UniProtKB/Swiss-Prot Q8YF59 (HISX_BRUME)
Last modified
November 3, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histidinol dehydrogenase Short name=HDH EC=1.1.1.23 | ||||
| Gene names |
| ||||
| Organism | Brucella melitensis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 29459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | L-histidinol + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activityInferred from electronic annotation. Source: HAMAP zinc 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 – 430 | 430 | Histidinol dehydrogenase HAMAP MF_01024 | PRO_0000135740 | |||||
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
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References
| [1] | "The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. Overbeek R.Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1. |
Cross-references
Sequence databases | |
|---|---|
| AE008917 Genomic DNA. Translation: AAL52849.1. | |
| PIR | AF3460. |
| RefSeq | NP_540585.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KAE based on UniProtKB P06988. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1197379. |
| GenomeReviews | Gene locus BMEI1668 in contig AE008917_GR. |
| KEGG | bme:BMEI1668. |
| NMPDR | fig|224914.1.peg.1667. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8YF59. |
| OMA | LLPEMPR. |
Enzyme and pathway databases | |
| BioCyc | BMEL224914:BMEI1668-MON. |
| BRENDA | 1.1.1.23. 277959. |
Family and domain databases | |
| HAMAP | MF_01024. [Tree] |
| InterPro | IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH_prok-type. [Graphical view] |
| PANTHER | PTHR21256:SF2. Hstdl_DH_prok. 1 hit. |
| Pfam | PF00815. Histidinol_dh. 1 hit. [Graphical view] |
| PRINTS | PR00083. HOLDHDRGNASE. |
| ProDom | PD002680. Histidinol_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00069. hisD. 1 hit. |
| PROSITE | PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HISX_BRUME | ||||||||
| Accession | Primary (citable) accession number: Q8YF59 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Brucella melitensis Brucella melitensis (strain 16M): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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