A0A8H3EFZ3 · A0A8H3EFZ3_9LECA
- Protein5-aminolevulinate synthase
- GeneHEM1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids614 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Catalytic activity
- glycine + H+ + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Cofactor
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | 5-aminolevulinate synthase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5-aminolevulinate synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Lecanoromycetes > OSLEUM clade > Lecanoromycetidae > Lecanorales > Lecanorineae > Parmeliaceae > Imshaugia
Accessions
- Primary accessionA0A8H3EFZ3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 110-130 | Disordered | ||||
Sequence: HTQKRKTQAQQAAATSGPKPA | ||||||
Domain | 181-533 | Aminotransferase class I/classII | ||||
Sequence: VTVWCSNDYLGMGRNPQVLKAMHETLDTYGSGAGGTRNISGHNQHAVALESTIARLHAQEAALVFSSCYVANDATLATLGSKLPNCVILSDSMNHASMIQGIRHSGAKKLVFKHNNLADLEAKLASLPPDVPKIIAFESVYSMCGSIGPIEEICDLADKYGAITFLDEVHAVGMYGPHGAGVAEHLDYEAHVAGRPKGTIMDRIDIITGTLGKAYGCVGGYIAGSAKMVDTIRSLAPGFIFTTSLPPATMAGAKTAIEYQMEFQGDRRLQQLHTRSTKQALVEKGLPVMPNPSHIIPVLVGNAELAKQASDLLLKDWGIYVQAINYPTVPVGEERLRFTPTPGHVEKYQKELV |
Sequence similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length614
- Mass (Da)66,425
- Last updated2022-01-19 v1
- Checksum2C63E9E5D25B2552
Keywords
- Technical term