methylaspartate mutase, E subunit; This model represents the E (epsilon) subunit of ...
3-482
0e+00
methylaspartate mutase, E subunit; This model represents the E (epsilon) subunit of methylaspartate mutase (glutamate mutase), a cobalamin-dependent enzyme that catalyzes the first step in a pathway of glutamate fermentation. [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]
Pssm-ID: 130567 Cd Length: 480 Bit Score: 917.30 E-value: 0e+00
Methylaspartate mutase E chain (MutE); This family consists of several methylaspartate mutase ...
42-482
0e+00
Methylaspartate mutase E chain (MutE); This family consists of several methylaspartate mutase E chain proteins (EC:5.4.99.1). Glutamate mutase catalyzes the first step in the fermentation of glutamate by Clostridium tetanomorphum. This is an unusual isomerization in which L-glutamate is converted to threo-beta-methyl L-aspartate.
Pssm-ID: 428905 Cd Length: 441 Bit Score: 870.41 E-value: 0e+00
Coenzyme B12-dependent glutamate mutase epsilon subunit-like family; contains proteins similar to Clostridium cochlearium glutamate mutase (Glm) and Streptomyces tendae Tu901 NikV. Glm catalyzes a carbon-skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate. The first step in the catalysis is a homolytic cleavage of the Co-C bond of the coenzyme B12 cofactor to generate a 5'-deoxyadenosyl radical. This radical then initiates the rearrangement reaction. C. cochlearium Glm is a sigma2epsilon2 heterotetramer. Glm plays a role in glutamate fermentation in Clostridium sp. and in members of the family Enterobacteriaceae, and in the synthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. S. tendae Tu901 glutamate mutase-like proteins NikU and NIkV participate in the synthesis of the peptidyl nucleoside antibiotic nikkomycin. NikU and NikV proteins have sequence similarity to Clostridium Glm sigma and epsilon components respectively, and may catalyze the rearrangement of 2-oxoglutaric acid to 2-keto-3-methylsuccinic acid during nikkomycin synthesis.
Pssm-ID: 238149 Cd Length: 428 Bit Score: 749.59 E-value: 0e+00
methylaspartate mutase, E subunit; This model represents the E (epsilon) subunit of ...
3-482
0e+00
methylaspartate mutase, E subunit; This model represents the E (epsilon) subunit of methylaspartate mutase (glutamate mutase), a cobalamin-dependent enzyme that catalyzes the first step in a pathway of glutamate fermentation. [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]
Pssm-ID: 130567 Cd Length: 480 Bit Score: 917.30 E-value: 0e+00
Methylaspartate mutase E chain (MutE); This family consists of several methylaspartate mutase ...
42-482
0e+00
Methylaspartate mutase E chain (MutE); This family consists of several methylaspartate mutase E chain proteins (EC:5.4.99.1). Glutamate mutase catalyzes the first step in the fermentation of glutamate by Clostridium tetanomorphum. This is an unusual isomerization in which L-glutamate is converted to threo-beta-methyl L-aspartate.
Pssm-ID: 428905 Cd Length: 441 Bit Score: 870.41 E-value: 0e+00
Coenzyme B12-dependent glutamate mutase epsilon subunit-like family; contains proteins similar to Clostridium cochlearium glutamate mutase (Glm) and Streptomyces tendae Tu901 NikV. Glm catalyzes a carbon-skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate. The first step in the catalysis is a homolytic cleavage of the Co-C bond of the coenzyme B12 cofactor to generate a 5'-deoxyadenosyl radical. This radical then initiates the rearrangement reaction. C. cochlearium Glm is a sigma2epsilon2 heterotetramer. Glm plays a role in glutamate fermentation in Clostridium sp. and in members of the family Enterobacteriaceae, and in the synthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. S. tendae Tu901 glutamate mutase-like proteins NikU and NIkV participate in the synthesis of the peptidyl nucleoside antibiotic nikkomycin. NikU and NikV proteins have sequence similarity to Clostridium Glm sigma and epsilon components respectively, and may catalyze the rearrangement of 2-oxoglutaric acid to 2-keto-3-methylsuccinic acid during nikkomycin synthesis.
Pssm-ID: 238149 Cd Length: 428 Bit Score: 749.59 E-value: 0e+00
Protein of unknown function (DUF1638); This family contains sequences covering an ...
234-267
4.81e-03
Protein of unknown function (DUF1638); This family contains sequences covering an approximately 270 amino acid stretch of a group of hypothetical proteins. These proteins are expressed by archaeal species of the Methanosarcina genus.
Pssm-ID: 429662 Cd Length: 160 Bit Score: 37.58 E-value: 4.81e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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