Q9SFH9 · HEM21_ARATH
- ProteinDelta-aminolevulinic acid dehydratase 1, chloroplastic
- GeneHEMB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids430 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Catalytic activity
- 2 5-aminolevulinate = porphobilinogen + 2 H2O + H+
Cofactor
Note: Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator.
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 298 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 308 | 5-aminolevulinate 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 320 | 5-aminolevulinate 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 336 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 351 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 377 | 5-aminolevulinate 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 416 | 5-aminolevulinate 2 (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Cellular Component | mitochondrion | |
Molecular Function | metal ion binding | |
Molecular Function | porphobilinogen synthase activity | |
Biological Process | chlorophyll biosynthetic process | |
Biological Process | porphyrin-containing compound biosynthetic process | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDelta-aminolevulinic acid dehydratase 1, chloroplastic
- EC number
- Short namesALADH1
- 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 accessionQ9SFH9
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Embryo lethal when homozygous. Impaired plant growth and development.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 26 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-52 | Chloroplast | ||||
Sequence: MATTPIFNASCSFPSTRGIDCKSYIGLRSNVSKVSVASSRIATSQRRNLVVR | ||||||
Chain | PRO_0000013314 | 53-430 | Delta-aminolevulinic acid dehydratase 1, chloroplastic | |||
Sequence: ASESGNGHAKKLGMSDAECEAAVAAGNVPEAPPVPPKPAAPVGTPIIKPLNLSRRPRRNRASPVTRAAFQETDISPANFVYPLFIHEGEEDTPIGAMPGCYRLGWRHGLVQEVAKARAVGVNSIVLFPKVPEALKNSTGDEAYNDNGLVPRTIRLLKDKYPDLIIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVSQARAGADVVSPSDMMDGRVGAIRSALDAEGFQNVSIMSYTAKYASSFYGPFREALDSNPRFGDKKTYQMNPANYREALIEAREDEAEGADILLVKPGLPYLDIIRLLRDKSPLPIAAYQVSGEYSMIKAGGVLKMIDEEKVMMESLMCLRRAGADIILTYFALQAATCLCGEKR |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in cotyledons during dark-to-light transition.
Induction
Up-regulated by the transcription factors FAR1 and FHY3.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 82-101 | Disordered | ||||
Sequence: EAPPVPPKPAAPVGTPIIKP |
Sequence similarities
Belongs to the ALAD family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length430
- Mass (Da)46,690
- Last updated2000-05-01 v1
- Checksum44B0984247FC6147
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC013289 EMBL· GenBank· DDBJ | AAG52549.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE34969.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE34970.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | ANM58523.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF327428 EMBL· GenBank· DDBJ | AAG42018.1 EMBL· GenBank· DDBJ | mRNA | ||
AF361803 EMBL· GenBank· DDBJ | AAK32816.1 EMBL· GenBank· DDBJ | mRNA | ||
AY059154 EMBL· GenBank· DDBJ | AAL15379.1 EMBL· GenBank· DDBJ | mRNA | ||
AY081254 EMBL· GenBank· DDBJ | AAL91143.1 EMBL· GenBank· DDBJ | mRNA | ||
AY113941 EMBL· GenBank· DDBJ | AAM44989.1 EMBL· GenBank· DDBJ | mRNA | ||
AY120705 EMBL· GenBank· DDBJ | AAM53263.1 EMBL· GenBank· DDBJ | mRNA | ||
AY128711 EMBL· GenBank· DDBJ | AAM91111.1 EMBL· GenBank· DDBJ | mRNA |