UniProt functional annotation for Q70LM7



	UniProt functional annotation for Q70LM7

UniProt code: Q70LM7.

Organism: Brevibacillus parabrevis.

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.

Function: Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N- formylation of the first amino acid residue in the synthesized dipeptide.

Cofactor: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000305}; Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};

Biophysicochemical properties: Kinetic parameters: KM=0.84 mM for valine; KM=2.40 mM for isoleucine;

Subunit: Large multienzyme complex composed of 4 subunits; LgrA, LgrB, LgrC and LgrD.

Domain: Two module-bearing peptide synthase with a C-terminal epimerization domain, which is probably inactive. 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). At the N-terminus, contains a N- formyltransferase domain that is probably responsible for the formylation of the first incorporated amino acid.

Miscellaneous: Linear gramicidin is a pentadecapeptide antibiotic produced during sporulation.

Similarity: Belongs to the ATP-dependent AMP-binding enzyme family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Brevibacillus parabrevis.
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.



Function:		Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N- formylation of the first amino acid residue in the synthesized dipeptide.


Cofactor:		Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000305}; Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
Biophysicochemical properties:		Kinetic parameters: KM=0.84 mM for valine; KM=2.40 mM for isoleucine;
Subunit:		Large multienzyme complex composed of 4 subunits; LgrA, LgrB, LgrC and LgrD.
Domain:		Two module-bearing peptide synthase with a C-terminal epimerization domain, which is probably inactive. 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). At the N-terminus, contains a N- formyltransferase domain that is probably responsible for the formylation of the first incorporated amino acid.
Miscellaneous:		Linear gramicidin is a pentadecapeptide antibiotic produced during sporulation.
Similarity:		Belongs to the ATP-dependent AMP-binding enzyme family. {ECO:0000305}.