serine dehydratase (SDH) alpha family protein; similar to Methanocaldococcus jannaschii L-cysteine desulfidase, an [4Fe-4S] enzyme, that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide.
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
3-459
0e+00
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.
The actual alignment was detected with superfamily member TIGR00720:
Pssm-ID: 452735 [Multi-domain] Cd Length: 450 Bit Score: 722.21 E-value: 0e+00
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called ...
3-459
0e+00
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273233 [Multi-domain] Cd Length: 450 Bit Score: 722.21 E-value: 0e+00
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
186-456
2.57e-104
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.
Pssm-ID: 427238 Cd Length: 259 Bit Score: 310.88 E-value: 2.57e-104
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called ...
3-459
0e+00
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273233 [Multi-domain] Cd Length: 450 Bit Score: 722.21 E-value: 0e+00
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
186-456
2.57e-104
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.
Pssm-ID: 427238 Cd Length: 259 Bit Score: 310.88 E-value: 2.57e-104
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
13-157
3.74e-84
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.
Pssm-ID: 427239 [Multi-domain] Cd Length: 146 Bit Score: 255.02 E-value: 3.74e-84
L-serine dehydratase, iron-sulfur-dependent, alpha subunit; This enzyme is also called serine ...
173-456
3.09e-43
L-serine dehydratase, iron-sulfur-dependent, alpha subunit; This enzyme is also called serine deaminase. L-serine dehydratase converts serine into pyruvate in the gluconeogenesis pathway from serine. This model describes the alpha chain of an iron-sulfur-dependent L-serine dehydratase, found in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of alpha chains from the homologous region of single chain forms such as found in Escherichia coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129801 Cd Length: 294 Bit Score: 154.00 E-value: 3.09e-43
L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine ...
4-150
2.98e-11
L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine deaminase. This model describes the beta chain of an iron-sulfur-dependent L-serine dehydratase, as in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of beta chains from the homologous region of single chain forms such as found in E. coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129802 [Multi-domain] Cd Length: 208 Bit Score: 62.64 E-value: 2.98e-11
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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