UniProt functional annotation for Q8DXM9



	UniProt functional annotation for Q8DXM9

UniProt code: Q8DXM9.

Organism: Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).

Taxonomy: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus.

Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

Catalytic activity: Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma- glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000255|HAMAP- Rule:MF_00782};

Catalytic activity: Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP + glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP- Rule:MF_00782};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};

Activity regulation: Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).

Biophysicochemical properties: Kinetic parameters: KM=22 mM for L-glutamate; KM=156 uM for L-cysteine; KM=8.2 mM for alpha-L-aminobutyrate; KM=64 uM for ATP (in the reaction with gamma-GCS); KM=5.9 mM for gamma-L-glutamyl-L-cysteine; KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate; KM=6.3 mM for glycine; KM=420 uM for ATP (in the reaction with GS);

Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP- Rule:MF_00782}.

Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP- Rule:MF_00782}.

Subunit: Monomer. {ECO:0000305}.

Similarity: In the N-terminal section; belongs to the glutamate-- cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000255|HAMAP- Rule:MF_00782}.

Annotations taken from UniProtKB at the EBI.


Organism:		Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus.



Function:		Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.


Catalytic activity:		Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma- glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000255\|HAMAP- Rule:MF_00782};
Catalytic activity:		Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP + glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255\|HAMAP- Rule:MF_00782};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
Activity regulation:		Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).
Biophysicochemical properties:		Kinetic parameters: KM=22 mM for L-glutamate; KM=156 uM for L-cysteine; KM=8.2 mM for alpha-L-aminobutyrate; KM=64 uM for ATP (in the reaction with gamma-GCS); KM=5.9 mM for gamma-L-glutamyl-L-cysteine; KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate; KM=6.3 mM for glycine; KM=420 uM for ATP (in the reaction with GS);
Pathway:		Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. {ECO:0000255\|HAMAP- Rule:MF_00782}.
Pathway:		Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. {ECO:0000255\|HAMAP- Rule:MF_00782}.
Subunit:		Monomer. {ECO:0000305}.
Similarity:		In the N-terminal section; belongs to the glutamate-- cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000255\|HAMAP- Rule:MF_00782}.