Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aminoacyl-histidine dipeptidase; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Predicted amidohydrolase [General function prediction only]; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aspartokinase (AK) [1] catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Glutamate synthase (NADPH), homotetrameric; One pathway for the assimilation of ammonia and glutamate biosynthesis involves homotetrameric glutamate synthase which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aminoacyl-histidine dipeptidase; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydrataseP20132, threonine dehydrataseP04968 tryptophan synthase beta chainthreonine synthasecysteine synthase, cystathionine beta-synthase-aminocyclopropane-1-carboxylate deaminase; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Glutamate dehydrogenases (EC, EC, and EC) (GluDH) are enzymes that catalyse the NAD-and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction -this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion o [...]

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Chorismate mutase / prephenate dehydratase.The bifunctional P-protein, which plays a central role in phenylalanine biosynthesis, contains two catalytic domains (chorismate mutase and prephenate dehydratase) and a regulatory domain (ACT). It is part of the shikimate pathway, which is present only in bacteria, fungi, and plants; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Hypothetical protein; This entry represents prephenate dehydrogenase (PDHG), an enzyme involved in tyrosine biosynthesis [PMID: 21798280], Three enzymes catalyse the conversion of chorismate to hydroxyphenylpyruvate or pyruvate in the aromatic amino acid biosynthesis pathway. In this pathway, chorismate is a branch point intermediate that is converted to tryptophan, phenylalanine (Phe), and tyrosine (Tyr). In bacteria the enzymes, chorismate mutase (CM), prephenate dehydratase (PDT), and prephenate dehydrogenase (PDHG) are either present as distinct proteins or fusions combining two ac [...]

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Hemolysin; Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [PUBMED:1990006] into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Shikimate 5-dehydrogenase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aspartate-ammonia ligase; ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Histidinol-phosphate aminotransferase; L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; High confidence in function and specificity; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Aspartokinase; Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine; High confidence in function and specificity; Belongs to the aspartokinase family.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Pyruvate dehydrogenase (NADP(+)); Pyruvate + CoA + NADP(+) <=> acetyl-CoA + CO(2) + NADPH; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Pyruvate-flavodoxin oxidoreductase; The oxidative decarboxylation of pyruvate to acetyl-CoA, a central step in energy metabolism, can occur by two different mechanisms. In anaerobic organisms, this reaction is reversibly catalysed by a single enzyme using either ferrodoxin or flavodoxin as the electron acceptor; High confidence in function and specificity.

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into class I and class II. This entry includes proteins from both subfamilies; High confidence in function and specificity.

Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

Gamma-glutamyltransferase; Gamma-glutamyltranspeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification; High confidence in function and specificity.

Aminoacyl-histidine dipeptidase; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases; High confidence in function and specificity.

Gamma-glutamyltransferase; Gamma-glutamyltranspeptidase (GGT) catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification; High confidence in function and specificity.

Glutamate synthase (NADPH), homotetrameric; One pathway for the assimilation of ammonia and glutamate biosynthesis involves homotetrameric glutamate synthase which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+; High confidence in function and specificity.