Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial ...
152-314
2.13e-131
Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial oxidoreductases. This domain is related to pfam02894, and it is likely to be an alpha/beta-domain involved in substrate binding and oligomerization.
:
Pssm-ID: 437690 Cd Length: 163 Bit Score: 370.49 E-value: 2.13e-131
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
2-229
1.33e-34
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]
The actual alignment was detected with superfamily member TIGR04380:
Pssm-ID: 275173 [Multi-domain] Cd Length: 330 Bit Score: 128.49 E-value: 1.33e-34
Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial ...
152-314
2.13e-131
Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial oxidoreductases. This domain is related to pfam02894, and it is likely to be an alpha/beta-domain involved in substrate binding and oligomerization.
Pssm-ID: 437690 Cd Length: 163 Bit Score: 370.49 E-value: 2.13e-131
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
2-229
1.33e-34
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]
Pssm-ID: 275173 [Multi-domain] Cd Length: 330 Bit Score: 128.49 E-value: 1.33e-34
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
3-122
1.10e-27
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 104.21 E-value: 1.10e-27
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
3-91
5.00e-04
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 39.83 E-value: 5.00e-04
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
4-87
5.35e-04
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 40.88 E-value: 5.35e-04
Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial ...
152-314
2.13e-131
Bacterial oxidoreductases, C-terminal; This is the C-terminal domain of predicted bacterial oxidoreductases. This domain is related to pfam02894, and it is likely to be an alpha/beta-domain involved in substrate binding and oligomerization.
Pssm-ID: 437690 Cd Length: 163 Bit Score: 370.49 E-value: 2.13e-131
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
2-229
1.33e-34
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]
Pssm-ID: 275173 [Multi-domain] Cd Length: 330 Bit Score: 128.49 E-value: 1.33e-34
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
3-122
1.10e-27
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 104.21 E-value: 1.10e-27
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
9-115
2.18e-04
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.
Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 39.98 E-value: 2.18e-04
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
3-91
5.00e-04
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 39.83 E-value: 5.00e-04
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
4-87
5.35e-04
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 40.88 E-value: 5.35e-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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