P0C062 · GRSA_BREBE

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

Cofactor

pantetheine 4'-phosphate (UniProtKB | Rhea| CHEBI:47942 )

Note: Binds 1 phosphopantetheine covalently.

Pathway

Antibiotic biosynthesis; gramicidin S biosynthesis.

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionligase activity
Molecular Functionphenylalanine racemase (ATP-hydrolyzing) activity
Biological Processantibiotic biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Gramicidin S synthase 1
  • Alternative names
    • Gramicidin S synthase I

Including 2 domains:

  • Recommended name
    ATP-dependent D-phenylalanine adenylase
  • Short names
    D-PheA
  • Alternative names
    • D-phenylalanine activase
  • Recommended name
    Phenylalanine racemase [ATP-hydrolyzing]
  • EC number

Gene names

    • Name
      grsA
    • Synonyms
      grs1

Organism names

Accessions

  • Primary accession
    P0C062
  • Secondary accessions
    • P14687

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001930861-1098Gramicidin S synthase 1
Modified residue573O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Subunit

Large multienzyme complex of GrsA and GrsB.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain538-612Carrier

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,098
  • Mass (Da)
    126,566
  • Last updated
    2005-07-05 v1
  • Checksum
    B8E0B55C33BBA1E8
MLNSSKSILIHAQNKNGTHEEEQYLFAVNNTKAEYPRDKTIHQLFEEQVSKRPNNVAIVCENEQLTYHELNVKANQLARIFIEKGIGKDTLVGIMMEKSIDLFIGILAVLKAGGAYVPIDIEYPKERIQYILDDSQARMLLTQKHLVHLIHNIQFNGQVEIFEEDTIKIREGTNLHVPSKSTDLAYVIYTSGTTGNPKGTMLEHKGISNLKVFFENSLNVTEKDRIGQFASISFDASVWEMFMALLTGASLYIILKDTINDFVKFEQYINQKEITVITLPPTYVVHLDPERILSIQTLITAGSATSPSLVNKWKEKVTYINAYGPTETTICATTWVATKETTGHSVPIGAPIQNTQIYIVDENLQLKSVGEAGELCIGGEGLARGYWKRPELTSQKFVDNPFVPGEKLYKTGDQARWLPDGNIEYLGRIDNQVKIRGHRVELEEVESILLKHMYISETAVSVHKDHQEQPYLCAIFVSEKHIPLEQLRQFSSEELPTYMIPSYFIQLDKMPLTSNGKIDRKQLPEPDLTFGMRVDYEAPRNEIEETLVTIWQDVLGIEKIGIKDNFYALGGDSIKAIQVAARLHSYQLKLETKDLLKYPTIDQLVHYIKDSKRRSEQGIVEGEIGLTPIQHWFFEQQFTNMHHWNQSYMLYRPNGFDKEILLRVFNKIVEHHDALRMIYKHHNGKIVQINRGLEGTLFDFYTFDLTANDNEQQVICEESARLQNSINLEVGPLVKIALFHTQNGDHLFMAIHHLVVDGISWRILFEDLATAYEQAMHQQTIALPEKTDSFKDWSIELEKYANSELFLEEAEYWHHLNYYTDNVQIKKDYVTMNNKQKNIRYVGMELTIEETEKLLKNVNKAYRTEINDILLTALGFALKEWADIDKIVINLEGHGREEILEQMNIARTVGWFTSQYPVVLDMQKSDDLSYQIKLMKENLRRIPNKGIGYEIFKYLTTEYLRPVLPFTLKPEINFNYLGQFDTDVKTELFTRSPYSMGNSLGPDGKNNLSPEGESYFVLNINGFIEEGKLHITFSYNEQQYKEDTIQQLSRSYKQHLLAIIEHCVQKEDTELTPSDFSFKELELEEMDDIFDLLADSLT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D00519
EMBL· GenBank· DDBJ
BAA00406.1
EMBL· GenBank· DDBJ
Genomic DNA
D00938
EMBL· GenBank· DDBJ
BAA00777.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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