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UniProt functional annotation for Q5SM19 | ||
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| UniProt code: Q5SM19. |
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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: | |
Acts on leucine, isoleucine and valine. {ECO:0000256|RuleBase:RU364094}. |
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| Catalytic activity: | |
Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000256|ARBA:ARBA00000627, ECO:0000256|RuleBase:RU364094}; |
| Catalytic activity: | |
Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L- glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000256|ARBA:ARBA00000995, ECO:0000256|RuleBase:RU364094}; |
| Catalytic activity: | |
Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L- glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000256|ARBA:ARBA00001745, ECO:0000256|RuleBase:RU364094}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|RuleBase:RU364094}; |
| Pathway: | |
Amino-acid biosynthesis; L-isoleucine biosynthesis; L- isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00004824, ECO:0000256|RuleBase:RU364094}. |
| Pathway: | |
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00005072, ECO:0000256|RuleBase:RU364094}. |
| Pathway: | |
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931, ECO:0000256|RuleBase:RU364094}. |
| Similarity: | |
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000256|ARBA:ARBA00009320, ECO:0000256|RuleBase:RU364094}. |
Annotations taken from UniProtKB at the EBI.