P08680 · HEM0_MOUSE
- Protein5-aminolevulinate synthase, erythroid-specific, mitochondrial
- GeneAlas2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids587 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:3557128, PubMed:8268805).
Contributes significantly to heme formation during erythropoiesis (By similarity).
Contributes significantly to heme formation during erythropoiesis (By similarity).
Catalytic activity
- succinyl-CoA + glycine + H+ = 5-aminolevulinate + CO2 + CoAThis reaction proceeds in the forward direction.
Cofactor
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 163 | substrate | |||
Binding site | 258 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 259 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 280 | substrate | |||
Binding site | 299 | substrate | |||
Binding site | 332 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 360 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 388 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Active site | 391 | ||||
Binding site | 420 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 421 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 508 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | 5-aminolevulinate synthase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | erythrocyte differentiation | |
Biological Process | heme biosynthetic process | |
Biological Process | hemoglobin biosynthetic process | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | protoporphyrinogen IX biosynthetic process | |
Biological Process | response to hypoxia |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5-aminolevulinate synthase, erythroid-specific, mitochondrial
- EC number
- Short namesALAS-E
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP08680
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Note: Localizes to the matrix side of the mitochondrion inner membrane.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 391 | Abolishes enzyme activity. | |||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 45 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-49 | Mitochondrion | |||
Chain | PRO_0000001224 | 50-587 | 5-aminolevulinate synthase, erythroid-specific, mitochondrial | ||
Modified residue | 391 | N6-(pyridoxal phosphate)lysine | |||
Proteomic databases
PTM databases
Expression
Tissue specificity
Predomnantly expressed in erythroid cells.
Gene expression databases
Structure
Family & Domains
Domain
C-terminus is a mobile self-inhibitory loop which interferes directly with active site.
Sequence similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length587
- Mass (Da)64,753
- Last updated2002-01-23 v3
- MD5 Checksum7956226253FB74EB8E006971116BCD34
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2AFM1 | A2AFM1_MOUSE | Alas2 | 572 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 61-75 | in Ref. 1; AAA37207 | |||
Sequence conflict | 66 | in Ref. 3; BAB22254 | |||
Sequence conflict | 171 | in Ref. 2; AAA91866 | |||
Sequence conflict | 338 | in Ref. 2; AAA91866 | |||
Sequence conflict | 368-372 | in Ref. 2; AAA91866 | |||
Sequence conflict | 427 | in Ref. 1; AAA37207 | |||
Sequence conflict | 479 | in Ref. 2; AAA91866 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15268 EMBL· GenBank· DDBJ | AAA37207.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M63244 EMBL· GenBank· DDBJ | AAA91866.1 EMBL· GenBank· DDBJ | mRNA | ||
AK002642 EMBL· GenBank· DDBJ | BAB22254.1 EMBL· GenBank· DDBJ | mRNA | ||
AK077610 EMBL· GenBank· DDBJ | BAC36898.1 EMBL· GenBank· DDBJ | mRNA |