P0C062 · GRSA_BREBE
- ProteinGramicidin S synthase 1
- GenegrsA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1098 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.
Miscellaneous
The racemization reaction takes place in the thioester-bound stage of phenylalanine that is formed via the thiol group of the serine-bound phosphopantetheine.
Catalytic activity
- ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H+
Cofactor
Note: Binds 1 phosphopantetheine covalently.
Pathway
Antibiotic biosynthesis; gramicidin S biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ligase activity | |
Molecular Function | phenylalanine racemase (ATP-hydrolyzing) activity | |
Biological Process | antibiotic biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGramicidin S synthase 1
- Alternative names
Including 2 domains:
- Recommended nameATP-dependent D-phenylalanine adenylase
- Short namesD-PheA
- Alternative names
- Recommended namePhenylalanine racemase [ATP-hydrolyzing]
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Brevibacillus
Accessions
- Primary accessionP0C062
- Secondary accessions
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193086 | 1-1098 | Gramicidin S synthase 1 | |||
Sequence: MLNSSKSILIHAQNKNGTHEEEQYLFAVNNTKAEYPRDKTIHQLFEEQVSKRPNNVAIVCENEQLTYHELNVKANQLARIFIEKGIGKDTLVGIMMEKSIDLFIGILAVLKAGGAYVPIDIEYPKERIQYILDDSQARMLLTQKHLVHLIHNIQFNGQVEIFEEDTIKIREGTNLHVPSKSTDLAYVIYTSGTTGNPKGTMLEHKGISNLKVFFENSLNVTEKDRIGQFASISFDASVWEMFMALLTGASLYIILKDTINDFVKFEQYINQKEITVITLPPTYVVHLDPERILSIQTLITAGSATSPSLVNKWKEKVTYINAYGPTETTICATTWVATKETTGHSVPIGAPIQNTQIYIVDENLQLKSVGEAGELCIGGEGLARGYWKRPELTSQKFVDNPFVPGEKLYKTGDQARWLPDGNIEYLGRIDNQVKIRGHRVELEEVESILLKHMYISETAVSVHKDHQEQPYLCAIFVSEKHIPLEQLRQFSSEELPTYMIPSYFIQLDKMPLTSNGKIDRKQLPEPDLTFGMRVDYEAPRNEIEETLVTIWQDVLGIEKIGIKDNFYALGGDSIKAIQVAARLHSYQLKLETKDLLKYPTIDQLVHYIKDSKRRSEQGIVEGEIGLTPIQHWFFEQQFTNMHHWNQSYMLYRPNGFDKEILLRVFNKIVEHHDALRMIYKHHNGKIVQINRGLEGTLFDFYTFDLTANDNEQQVICEESARLQNSINLEVGPLVKIALFHTQNGDHLFMAIHHLVVDGISWRILFEDLATAYEQAMHQQTIALPEKTDSFKDWSIELEKYANSELFLEEAEYWHHLNYYTDNVQIKKDYVTMNNKQKNIRYVGMELTIEETEKLLKNVNKAYRTEINDILLTALGFALKEWADIDKIVINLEGHGREEILEQMNIARTVGWFTSQYPVVLDMQKSDDLSYQIKLMKENLRRIPNKGIGYEIFKYLTTEYLRPVLPFTLKPEINFNYLGQFDTDVKTELFTRSPYSMGNSLGPDGKNNLSPEGESYFVLNINGFIEEGKLHITFSYNEQQYKEDTIQQLSRSYKQHLLAIIEHCVQKEDTELTPSDFSFKELELEEMDDIFDLLADSLT | ||||||
Modified residue | 573 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Large multienzyme complex of GrsA and GrsB.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 538-612 | Carrier | ||||
Sequence: APRNEIEETLVTIWQDVLGIEKIGIKDNFYALGGDSIKAIQVAARLHSYQLKLETKDLLKYPTIDQLVHYIKDSK |
Domain
One-module-bearing peptide synthase with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional) (By similarity).
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,098
- Mass (Da)126,566
- Last updated2005-07-05 v1
- ChecksumB8E0B55C33BBA1E8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D00519 EMBL· GenBank· DDBJ | BAA00406.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D00938 EMBL· GenBank· DDBJ | BAA00777.1 EMBL· GenBank· DDBJ | Genomic DNA |