Reviewed,
UniProtKB/Swiss-Prot Q9PM77 (HISX_CAMJE)
Last modified
February 9, 2010.
Version 57.
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 | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 428 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 MF_01024 |
| Catalytic activity | L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024 |
| 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 – 428 | 428 | Histidinol dehydrogenase HAMAP MF_01024 | PRO_0000135751 | |||||
Sites | |||||||||
| Active site | 323 | 1 | Proton acceptor By similarity | ||||||
| Active site | 324 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 256 | 1 | Zinc By similarity | ||||||
| Metal binding | 259 | 1 | Zinc By similarity | ||||||
| Metal binding | 357 | 1 | Zinc By similarity | ||||||
| Metal binding | 416 | 1 | Zinc By similarity | ||||||
| Binding site | 234 | 1 | Substrate By similarity | ||||||
| Binding site | 256 | 1 | Substrate By similarity | ||||||
| Binding site | 259 | 1 | Substrate By similarity | ||||||
| Binding site | 324 | 1 | Substrate By similarity | ||||||
| Binding site | 357 | 1 | Substrate By similarity | ||||||
| Binding site | 411 | 1 | Substrate By similarity | ||||||
| Binding site | 416 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL35695.1. |
| PIR | D81255. |
| RefSeq | YP_002344967.1. |
3D structure databases | |
| SMR | Q9PM77. Positions 3-428. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 905868. |
| GenomeReviews | Gene locus Cj1598 in contig AL111168_GR. |
| KEGG | cje:Cj1598. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG329596. |
| OMA | LDAHKNA. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1598-MONOMER. |
| BRENDA | 1.1.1.23. 255835. |
Family and domain databases | |
| HAMAP | MF_01024. HisD. [Tree] |
| InterPro | IPR016161. Ald_DH/histidinol_DH. 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. |
| TIGRFAMs | TIGR00069. hisD. 1 hit. |
| PROSITE | PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HISX_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PM77 Secondary accession number(s): Q0P830 | ||||||||
| 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


