Protein Family Models

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises thre ACT-like (ACT1-3) and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. This entry represents the ACT2 domain. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises ACT-like and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. It also has three helical motifs (HM1-3); this entry represents HM2. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises three ACT-like (ACT1-3) and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. This entry represents ACT3 domain. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises ACT-like and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. This entry represents the helical C-terminal domain. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises ACT-like and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. This is the first ACT-like domain (ACT1) found at the N-terminal of GDH. The ACT domains of these proteins differ from the archetypal ACT fold in that strand strand beta1 is located in the position usually occupied by strand beta4 creating an ACT-like topology with a beta1-4 antiparallel sheet [2]. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises ACT-like and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. It also includes three helical motifs (HM1-3), HM3 is represented in this entry. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has a long N- and C-terminal segments flanking the catalytic core, comprising several domains. The flexible N-terminal domain comprises ACT-like and PAS-type domains which could act as metabolic sensors for allosteric regulation [2]. It also has three helical motifs (HM1-3), this entry represents the first one (HM1). [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-16

This entry represents the catalytic domain of several proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia [1]. The structure of GDH from Mycobacterium smegmatis revealed that it has long N- and C-terminal segments flanking the catalytic core which provide dimer-like interactions between pairs of monomers [2]. The N-terminal segment is flexible and contains ACT-like and PAS-type domains that may play a role as metabolic sensors for allosteric regulation [2]. [1]. 10924516. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. Minambres B, Olivera ER, Jensen RA, Luengo JM;. J Biol Chem 2000;275:39529-39542. [2]. 34083757. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Lazaro M, Melero R, Huet C, Lopez-Alonso JP, Delgado S, Dodu A, Bruch EM, Abriata LA, Alzari PM, Valle M, Lisa MN;. Commun Biol. 2021;4:684. (from Pfam)

Date:

2024-10-21

NAD-specific glutamate dehydrogenase is involved in arginine catabolism by converting L-glutamate into 2-oxoglutarate, which is then channeled into the tricarboxylic acid cycle; can also utilize other amino acids of the glutamate family

Date:

2024-11-16