Reviewed,
UniProtKB/Swiss-Prot Q97KI2 (HISX_CLOAB)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 |
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| Organism | Clostridium acetobutylicum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1488 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 431 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 – 431 | 431 | Histidinol dehydrogenase HAMAP MF_01024 | PRO_0000135756 | |||||
Sites | |||||||||
| Active site | 329 | 1 | Proton acceptor By similarity | ||||||
| Active site | 330 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 261 | 1 | Zinc By similarity | ||||||
| Metal binding | 264 | 1 | Zinc By similarity | ||||||
| Metal binding | 363 | 1 | Zinc By similarity | ||||||
| Metal binding | 422 | 1 | Zinc By similarity | ||||||
| Binding site | 131 | 1 | NAD By similarity | ||||||
| Binding site | 193 | 1 | NAD By similarity | ||||||
| Binding site | 216 | 1 | NAD By similarity | ||||||
| Binding site | 239 | 1 | Substrate By similarity | ||||||
| Binding site | 261 | 1 | Substrate By similarity | ||||||
| Binding site | 264 | 1 | Substrate By similarity | ||||||
| Binding site | 330 | 1 | Substrate By similarity | ||||||
| Binding site | 363 | 1 | Substrate By similarity | ||||||
| Binding site | 417 | 1 | Substrate By similarity | ||||||
| Binding site | 422 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787. |
Cross-references
Sequence databases | |
|---|---|
| AE001437 Genomic DNA. Translation: AAK78913.1. | |
| PIR | F97015. |
| RefSeq | NP_347573.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K75 based on UniProtKB P06988. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1117120. |
| GenomeReviews | Gene locus CA_C0937 in contig AE001437_GR. |
| KEGG | cac:CAC0937. |
| NMPDR | fig|272562.1.peg.1102. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q97KI2. |
| OMA | Q97KI2. LDAHKNA. |
Enzyme and pathway databases | |
| BioCyc | CACE272562:CAC0937-MON. |
| BRENDA | 1.1.1.23. 2866. |
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_CLOAB | ||||||||
| Accession | Primary (citable) accession number: Q97KI2 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


