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UniProt functional annotation for Q5SH23 | ||
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| UniProt code: Q5SH23. |
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| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
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| Function: | |
Catalyzes the ATP-dependent formation of a covalent bond between the amino group of alpha-aminoadipate (AAA) and the gamma- carboxyl group of the C-terminal glutamate residue in LysW. {ECO:0000269|PubMed:19620981}. |
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| Catalytic activity: | |
Reaction=[amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-2-aminoadipate = [amino-group carrier protein]-C-terminal-N-(1,4- dicarboxybutan-1-yl)-L-glutamine + ADP + H(+) + phosphate; Xref=Rhea:RHEA:41940, Rhea:RHEA-COMP:9693, Rhea:RHEA-COMP:9694, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58672, ChEBI:CHEBI:78503, ChEBI:CHEBI:78525, ChEBI:CHEBI:456216; EC=6.3.2.43; Evidence={ECO:0000269|PubMed:19620981}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=2.1 mM for alpha-aminoadipate {ECO:0000269|PubMed:19620981}; KM=2.6 mM for ATP {ECO:0000269|PubMed:19620981}; |
| Pathway: | |
Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 1/5. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:12963379, ECO:0000269|PubMed:23434852}. |
| Similarity: | |
Belongs to the RimK family. LysX subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.