P34047 · HIS5A_ARATH
- ProteinImidazoleglycerol-phosphate dehydratase 1, chloroplastic
- GeneHISN5A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids270 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Catalytic activity
- D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Cofactor
Note: Binds 2 manganese ions per subunit.
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 84 | substrate | |||
Binding site | 110 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 110-118 | substrate | |||
Binding site | 136 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 136-140 | substrate | |||
Binding site | 137 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 140 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 162 | substrate | |||
Binding site | 184 | substrate | |||
Binding site | 208 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 232 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 232-240 | substrate | |||
Binding site | 233 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 236 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 262-264 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | imidazoleglycerol-phosphate dehydratase activity | |
Molecular Function | metal ion binding | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameImidazoleglycerol-phosphate dehydratase 1, chloroplastic
- EC number
- Short namesIGPD 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP34047
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-62 | Chloroplast | |||
Modified residue | 63 | N-acetylserine | |||
Chain | PRO_0000158253 | 63-270 | Imidazoleglycerol-phosphate dehydratase 1, chloroplastic | ||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 250-270 | Disordered | |||
Sequence similarities
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.
P34047-1
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.
- Name1
- Length270
- Mass (Da)29,225
- Last updated1994-02-01 v1
- MD5 Checksum138E051B3423C8329BBFF0F95A72DA96
P34047-2
- Name2
- NoteMay be due to an intron retention.
- Differences from canonical
- 205-270: LVEHFFQSLVNTSGMTLHIRQLAGENSHHIIEATFKAFARALRQATETDPRRGGTIPSSKGVLSRS → VLSLLLELSSFGFICVIRCLVIIESVAKNCLTFRFVVGGALFPVVGEYFWYDSSHPAARW
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 201 | in Ref. 6; BAD44082 | |||
Alternative sequence | VSP_008895 | 205-270 | in isoform 2 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U02689 EMBL· GenBank· DDBJ | AAA93196.1 EMBL· GenBank· DDBJ | mRNA | ||
AB022215 EMBL· GenBank· DDBJ | BAB01781.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE76636.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE76637.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK118815 EMBL· GenBank· DDBJ | BAC43405.1 EMBL· GenBank· DDBJ | mRNA | ||
AY070442 EMBL· GenBank· DDBJ | AAL49845.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176319 EMBL· GenBank· DDBJ | BAD44082.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176429 EMBL· GenBank· DDBJ | BAD44192.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087948 EMBL· GenBank· DDBJ | AAM65496.1 EMBL· GenBank· DDBJ | mRNA |