Reviewed,
UniProtKB/Swiss-Prot Q9C5U8 (HISX_ARATH)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histidinol dehydrogenase, chloroplastic Short name=HDH EC=1.1.1.23 | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. |
| Catalytic activity | L-histidinol + 2 NAD+ = L-histidine + 2 NADH. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the histidinol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Chloroplast Plastid |
| Coding sequence diversity | Alternative splicing |
| Domain | Transit peptide |
| 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: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW pollen developmentInferred from mutant phenotype. Source: TAIR response to UVInferred from expression pattern. Source: TAIR |
| Cellular component | chloroplast stroma Inferred from direct assay. Source: TAIR |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activityTraceable author statement. Source: TAIR zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9C5U8-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q9C5U8-2) The sequence of this isoform differs from the canonical sequence as follows: 1-31: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 30 | 30 | Chloroplast By similarity | ||||||
| Chain | 31 – 466 | 436 | Histidinol dehydrogenase, chloroplastic | PRO_0000007215 | |||||
Sites | |||||||||
| Active site | 356 | 1 | Proton acceptor By similarity | ||||||
| Active site | 357 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 288 | 1 | Zinc By similarity | ||||||
| Metal binding | 291 | 1 | Zinc By similarity | ||||||
| Metal binding | 390 | 1 | Zinc By similarity | ||||||
| Metal binding | 449 | 1 | Zinc By similarity | ||||||
| Binding site | 155 | 1 | NAD By similarity | ||||||
| Binding site | 217 | 1 | NAD By similarity | ||||||
| Binding site | 240 | 1 | NAD By similarity | ||||||
| Binding site | 266 | 1 | Substrate By similarity | ||||||
| Binding site | 288 | 1 | Substrate By similarity | ||||||
| Binding site | 291 | 1 | Substrate By similarity | ||||||
| Binding site | 357 | 1 | Substrate By similarity | ||||||
| Binding site | 390 | 1 | Substrate By similarity | ||||||
| Binding site | 444 | 1 | Substrate By similarity | ||||||
| Binding site | 449 | 1 | Substrate By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 31 | 31 | Missing in isoform 2. | VSP_008912 | |||||
Experimental info | |||||||||
| Sequence conflict | 25 | 1 | K → KA in BAB11037. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of Arabidopsis cDNA for histidinol dehydrogenase." Fujimori K. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones." Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia. |
| [4] | "Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). |
Cross-references
Sequence databases | |
|---|---|
| AB027709 mRNA. Translation: BAB40445.1. AB007646 Genomic DNA. Translation: BAB11037.1. AY039881 mRNA. Translation: AAK63985.1. AY143900 mRNA. Translation: AAN28839.1. AY087987 mRNA. Translation: AAM65533.1. | |
| IPI | IPI00536632. IPI00549107. |
| RefSeq | NP_568981.2. |
| UniGene | At.20645 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K75 based on UniProtKB P06988. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9C5U8. |
Genome annotation databases | |
| GeneID | 836509. |
| GenomeReviews | Gene locus AT5G63890 in contig BA000015_GR. |
| KEGG | ath:AT5G63890. |
| NMPDR | fig|3702.1.peg.28443. |
Organism-specific databases | |
| TAIR | At5g63890. |
Phylogenomic databases | |
| OMA | Q9C5U8. LDAHKNA. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.23. 302. |
Gene expression databases | |
| ArrayExpress | Q9C5U8. |
| GermOnline | AT5G63890. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | 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. |
| ProDom | PD002680. Histidinol_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00069. hisD. 1 hit. |
| PROSITE | PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HISX_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9C5U8 Secondary accession number(s): Q8LA77, Q9FN00 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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