P10370 · HISX_SALTY
- ProteinHistidinol dehydrogenase
- GenehisD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids434 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic activity
- H2O + L-histidinol + 2 NAD+ = 3 H+ + L-histidine + 2 NADH
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 zinc ion per subunit. At high pH manganese can replace zinc.
Activity regulation
Activity is lost when the metal is removed through urea denaturation or chelation, and can be regained by addition of metal.
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 130 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 188 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 211 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 237 | substrate | ||||
Sequence: S | ||||||
Binding site | 259 | substrate | ||||
Sequence: Q | ||||||
Binding site | 259 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 262 | substrate | ||||
Sequence: H | ||||||
Binding site | 262 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 326 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 327 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 327 | substrate | ||||
Sequence: H | ||||||
Binding site | 360 | substrate | ||||
Sequence: D | ||||||
Binding site | 360 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 414 | substrate | ||||
Sequence: E | ||||||
Binding site | 419 | substrate | ||||
Sequence: H | ||||||
Binding site | 419 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | histidinol dehydrogenase activity | |
Molecular Function | NAD binding | |
Molecular Function | zinc ion binding | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistidinol dehydrogenase
- EC number
- Short namesHDH
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP10370
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 99 | Slight decrease in activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 117 | Almost no change in activity. | ||||
Sequence: C → A or S | ||||||
Mutagenesis | 154 | Almost no change in activity. | ||||
Sequence: C → A or S | ||||||
Mutagenesis | 262 | 7000-fold decrease in activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 327 | 500-fold decrease in activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 367 | Slight decrease in activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 419 | 20-fold decrease in activity. | ||||
Sequence: H → Q |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000135840 | 2-434 | Histidinol dehydrogenase | |||
Sequence: SFNTLIDWNSCSPEQQRALLTRPAISASDSITRTVSDILDNVKTRGDDALREYSAKFDKTEVTALRVTPEEIAAAGARLSDELKQAMTAAVKNIETFHSAQTLPPVDVETQPGVRCQQVTRPVSSVGLYIPGGSAPLFSTVLMLATPARIAGCQKVVLCSPPPIADEILYAAQLCGVQEIFNVGGAQAIAALAFGSESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPDFVASDLLSQAEHGPDSQVILLTPDADIARKVAEAVERQLAELPRADTARQALSASRLIVTKDLAQCVAISNQYGPEHLIIQTRNARDLVDAITSAGSVFLGDWSPESAGDYASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKAGFSALASTIETLAAAERLTAHKNAVTLRVNALKEQA |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length434
- Mass (Da)45,889
- Last updated2007-01-23 v3
- Checksum744EDDCDAB5DF6CE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X13464 EMBL· GenBank· DDBJ | CAA31823.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J01804 EMBL· GenBank· DDBJ | AAA88615.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL20976.1 EMBL· GenBank· DDBJ | Genomic DNA |