P24226 · HISX_BRAOC
- ProteinHistidinol dehydrogenase, chloroplastic
- GeneHDH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Miscellaneous
Cabbage may contain multiple HDH isozymes encoded by different genes.
Catalytic activity
- H2O + L-histidinol + 2 NAD+ = 3 H+ + L-histidine + 2 NADH
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 | 156 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 218 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 241 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 267 | substrate | ||||
Sequence: S | ||||||
Binding site | 289 | substrate | ||||
Sequence: Q | ||||||
Binding site | 289 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 292 | substrate | ||||
Sequence: H | ||||||
Binding site | 292 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 357 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 358 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 358 | substrate | ||||
Sequence: H | ||||||
Binding site | 391 | substrate | ||||
Sequence: D | ||||||
Binding site | 391 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 445 | substrate | ||||
Sequence: E | ||||||
Binding site | 450 | substrate | ||||
Sequence: H | ||||||
Binding site | 450 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Molecular Function | histidinol dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD binding | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistidinol dehydrogenase, chloroplastic
- EC number
- Short namesHDH
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionP24226
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-31 | Chloroplast | ||||
Sequence: MSFDLSRLSLTSSPRLSFLTRTATKKGFVRC | ||||||
Chain | PRO_0000007216 | 32-469 | Histidinol dehydrogenase, chloroplastic | |||
Sequence: SMKSYRLSELSFSQVENLKARPRIDFSSIFTTVNPIIDAVRSKGDTAVKEYTERFDKVQLNKVVEDVSELDIPELDSAVKEAFDVAYDNIYAFHFAQMSTEKSVENMKGVRCKRVSRSIGSVGLYVPGGTAVLPSTALMLAIPAQIAGCKTVVLATPPTKEGSICKEVLYCAKRAGVTHILKAGGAQAIAAMAWGTDSCPKVEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADEHASPVYIAADLLSQAEHGPDSQVVLVVVGDGVNLKAIEEEIAKQCKSLPRGEFASKALSHSFTVFARDMIEAITFSNLYAPEHLIINVKDAEKWEGLIENAGSVFIGPWTPESVGDYASGTNHVLPTYGYARMYSGVSLDSFLKFMTVQSLTEEGLRNLGPYVATMAEIEGLDAHKRAVTLRLKDIEAKQTQTK |
Interaction
Chemistry
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length469
- Mass (Da)50,959
- Last updated1992-03-01 v1
- ChecksumEC63FA4B7B2E19CA
Keywords
- Technical term