Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
4-313
6.12e-144
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyzes the deamination of ornithine to proline. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina.
:
Pssm-ID: 426766 [Multi-domain] Cd Length: 313 Bit Score: 408.01 E-value: 6.12e-144
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
4-313
6.12e-144
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyzes the deamination of ornithine to proline. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina.
Pssm-ID: 426766 [Multi-domain] Cd Length: 313 Bit Score: 408.01 E-value: 6.12e-144
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
7-310
3.17e-116
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 441972 [Multi-domain] Cd Length: 322 Bit Score: 337.89 E-value: 3.17e-116
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ...
40-308
1.50e-52
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric, NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other Archaea. For a number of close homologs, scoring between trusted and noise cutoffs, it is not clear at present what is the enzymatic activity.
Pssm-ID: 131424 Cd Length: 325 Bit Score: 175.49 E-value: 1.50e-52
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
158-205
6.71e-04
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 39.56 E-value: 6.71e-04
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
4-313
6.12e-144
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyzes the deamination of ornithine to proline. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina.
Pssm-ID: 426766 [Multi-domain] Cd Length: 313 Bit Score: 408.01 E-value: 6.12e-144
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
7-310
3.17e-116
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 441972 [Multi-domain] Cd Length: 322 Bit Score: 337.89 E-value: 3.17e-116
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ...
40-308
1.50e-52
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric, NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other Archaea. For a number of close homologs, scoring between trusted and noise cutoffs, it is not clear at present what is the enzymatic activity.
Pssm-ID: 131424 Cd Length: 325 Bit Score: 175.49 E-value: 1.50e-52
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
162-220
1.19e-05
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.
Pssm-ID: 460229 [Multi-domain] Cd Length: 136 Bit Score: 44.10 E-value: 1.19e-05
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
123-202
2.91e-04
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 41.66 E-value: 2.91e-04
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
158-205
6.71e-04
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 39.56 E-value: 6.71e-04
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
162-211
7.00e-04
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 40.71 E-value: 7.00e-04
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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