O52791 · HMAS_AMYOR
- Protein4-hydroxymandelate synthase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids357 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.
Catalytic activity
- 3-(4-hydroxyphenyl)pyruvate + O2 = (S)-4-hydroxymandelate + CO2
Cofactor
Note: Binds 1 Fe cation per subunit.
Pathway
Antibiotic biosynthesis; vancomycin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 161 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 161 | substrate | ||||
Sequence: H | ||||||
Binding site | 201 | substrate | ||||
Sequence: S | ||||||
Binding site | 214 | substrate | ||||
Sequence: T | ||||||
Binding site | 241 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 241 | substrate | ||||
Sequence: H | ||||||
Binding site | 305 | substrate | ||||
Sequence: Q | ||||||
Binding site | 320 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4-hydroxymandelate synthase activity | |
Molecular Function | 4-hydroxyphenylpyruvate dioxygenase activity | |
Molecular Function | iron ion binding | |
Biological Process | tyrosine catabolic process | |
Biological Process | vancomycin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxymandelate synthase
- EC number
- Short namesHMS; HmaS
- Alternative names
Organism names
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Amycolatopsis
Accessions
- Primary accessionO52791
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000418534 | 1-357 | 4-hydroxymandelate synthase | |||
Sequence: MQNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKGDVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTGQSEFGAARR |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-129 | VOC 1 | ||||
Sequence: EIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQR | ||||||
Domain | 158-309 | VOC 2 | ||||
Sequence: GIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTA |
Sequence similarities
Belongs to the 4HPPD family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length357
- Mass (Da)38,339
- Last updated1998-06-01 v1
- ChecksumF146FCE537CEF2CA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ223998 EMBL· GenBank· DDBJ | CAA11761.1 EMBL· GenBank· DDBJ | Genomic DNA |