G7IKX3 · G7IKX3_MEDTR
- ProteinHistidinol dehydrogenase, chloroplastic
- Gene11412251
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids478 (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.
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 | 96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 97 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 166 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 169 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 170 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 171 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 228 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 251 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 275 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 277 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 277 | substrate | ||||
Sequence: S | ||||||
Binding site | 299 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 299 | substrate | ||||
Sequence: Q | ||||||
Binding site | 302 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 302 | substrate | ||||
Sequence: H | ||||||
Active site | 367 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 368 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 368 | substrate | ||||
Sequence: H | ||||||
Binding site | 401 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 401 | substrate | ||||
Sequence: D | ||||||
Binding site | 410 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 455 | substrate | ||||
Sequence: E | ||||||
Binding site | 460 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 460 | substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | cytoplasm | |
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
- Short namesHDH
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Trifolieae > Medicago
Accessions
- Primary accessionG7IKX3
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length478
- Mass (Da)52,045
- Last updated2012-01-25 v1
- ChecksumFC10BF07FB86D8FE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM001218 EMBL· GenBank· DDBJ | AES64804.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PSQE01000002 EMBL· GenBank· DDBJ | RHN72894.1 EMBL· GenBank· DDBJ | Genomic DNA |