O34651 · HISX_BACSU
- ProteinHistidinol dehydrogenase
- GenehisD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids427 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic activity
- L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
Cofactor
Note: Binds 1 zinc ion per subunit.
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 | 123 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 185 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 208 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 231 | substrate | ||||
Sequence: S | ||||||
Binding site | 253 | substrate | ||||
Sequence: Q | ||||||
Binding site | 253 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 256 | substrate | ||||
Sequence: H | ||||||
Binding site | 256 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 321 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 322 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 322 | substrate | ||||
Sequence: H | ||||||
Binding site | 355 | substrate | ||||
Sequence: D | ||||||
Binding site | 355 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 409 | substrate | ||||
Sequence: E | ||||||
Binding site | 414 | substrate | ||||
Sequence: H | ||||||
Binding site | 414 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO34651
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135728 | 1-427 | Histidinol dehydrogenase | |||
Sequence: MKIKTISGAERLSLKRSIDAGTEEQRKTVRSIIEDVKANGDQAVRSYTAKFDCIEIDSPLVTKEEFEEAYTSLDSRLLQVIRQAIENIREYHERQLQSSWFYHRKDGTMLGQKVTALDSAGVYVPGGTAAYPSSVLMNVIPALVAGVERIVLVTPPGKDGLLSPGVLVAAAELGIKDIYKMGGAQAIAALAYGTETIEPVDKITGPGNIYVALAKREVFGDVDIDMIAGPSEIVVLADETAIPSEIAADLLSQAEHDKLSSCVFVTDSMALAETVSAEVNKQLETLPRREIAEASVRDYGCIYVAETMVEAIETVNTLAPEHLEIITQSPEALLGSIKHAGAIFLGRYSPEPVGDYFAGPNHVLPTNGTARFSSPLNVTDFQKKSSIISYSQSAFEEHAESIAAFARLEGLEAHARSIEARERRISK |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)46,256
- Last updated1998-01-01 v1
- ChecksumBDB0B2AE3C580E7F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017113 EMBL· GenBank· DDBJ | AAC67295.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB15496.1 EMBL· GenBank· DDBJ | Genomic DNA |