MULTISPECIES: cystathionine beta-synthase [Pseudomonas]
Protein Classification
CBS_like and CBS_pair_CBS domain-containing protein( domain architecture ID 12773407)
CBS_like and CBS_pair_CBS domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CysK | COG0031 | Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-311 | 1.45e-157 | |||||
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis : Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 447.96 E-value: 1.45e-157
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| CBS_pair_CBS | cd04608 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
334-452 | 2.89e-33 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). : Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 121.49 E-value: 2.89e-33
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| Name | Accession | Description | Interval | E-value | |||||||
| CysK | COG0031 | Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-311 | 1.45e-157 | |||||||
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 447.96 E-value: 1.45e-157
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| CBS_like | cd01561 | CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-310 | 4.24e-138 | |||||||
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine. Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 398.04 E-value: 4.24e-138
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| cysta_beta | TIGR01137 | cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
5-453 | 1.48e-126 | |||||||
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family] Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 374.91 E-value: 1.48e-126
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| PRK10717 | PRK10717 | cysteine synthase A; Provisional |
6-323 | 3.77e-122 | |||||||
cysteine synthase A; Provisional Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 358.79 E-value: 3.77e-122
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| PALP | pfam00291 | Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-303 | 1.34e-78 | |||||||
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4. Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 246.45 E-value: 1.34e-78
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| CBS_pair_CBS | cd04608 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
334-452 | 2.89e-33 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 121.49 E-value: 2.89e-33
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
345-414 | 8.80e-11 | |||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 59.49 E-value: 8.80e-11
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
332-388 | 4.11e-08 | |||||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 49.52 E-value: 4.11e-08
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| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
344-388 | 9.12e-07 | |||||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 45.58 E-value: 9.12e-07
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| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
332-387 | 1.81e-04 | |||||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 43.67 E-value: 1.81e-04
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| Name | Accession | Description | Interval | E-value | |||||||
| CysK | COG0031 | Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-311 | 1.45e-157 | |||||||
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 447.96 E-value: 1.45e-157
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| CBS_like | cd01561 | CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-310 | 4.24e-138 | |||||||
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine. Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 398.04 E-value: 4.24e-138
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| cysta_beta | TIGR01137 | cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
5-453 | 1.48e-126 | |||||||
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family] Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 374.91 E-value: 1.48e-126
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| PRK10717 | PRK10717 | cysteine synthase A; Provisional |
6-323 | 3.77e-122 | |||||||
cysteine synthase A; Provisional Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 358.79 E-value: 3.77e-122
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| cysK | TIGR01139 | cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
9-310 | 6.25e-104 | |||||||
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family] Pssm-ID: 273465 Cd Length: 298 Bit Score: 311.22 E-value: 6.25e-104
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| cysKM | TIGR01136 | cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
9-310 | 5.27e-103 | |||||||
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family] Pssm-ID: 273463 Cd Length: 299 Bit Score: 308.83 E-value: 5.27e-103
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| cysM | PRK11761 | cysteine synthase CysM; |
7-310 | 8.99e-80 | |||||||
cysteine synthase CysM; Pssm-ID: 236972 Cd Length: 296 Bit Score: 249.41 E-value: 8.99e-80
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| PALP | pfam00291 | Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-303 | 1.34e-78 | |||||||
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4. Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 246.45 E-value: 1.34e-78
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| Trp-synth-beta_II | cd00640 | Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-303 | 1.64e-73 | |||||||
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine. Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 231.25 E-value: 1.64e-73
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| PLN02565 | PLN02565 | cysteine synthase |
9-312 | 2.96e-70 | |||||||
cysteine synthase Pssm-ID: 166206 Cd Length: 322 Bit Score: 225.57 E-value: 2.96e-70
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| cysM | TIGR01138 | cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
9-310 | 7.47e-70 | |||||||
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family] Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 223.64 E-value: 7.47e-70
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| PLN00011 | PLN00011 | cysteine synthase |
9-310 | 1.20e-68 | |||||||
cysteine synthase Pssm-ID: 177651 Cd Length: 323 Bit Score: 221.42 E-value: 1.20e-68
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| PLN03013 | PLN03013 | cysteine synthase |
9-310 | 1.22e-62 | |||||||
cysteine synthase Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 209.25 E-value: 1.22e-62
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| PLN02356 | PLN02356 | phosphateglycerate kinase |
3-323 | 1.42e-59 | |||||||
phosphateglycerate kinase Pssm-ID: 215204 Cd Length: 423 Bit Score: 200.99 E-value: 1.42e-59
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| PLN02556 | PLN02556 | cysteine synthase/L-3-cyanoalanine synthase |
6-316 | 2.08e-54 | |||||||
cysteine synthase/L-3-cyanoalanine synthase Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 185.93 E-value: 2.08e-54
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| CBS_pair_CBS | cd04608 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
334-452 | 2.89e-33 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 121.49 E-value: 2.89e-33
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| Thr-synth_1 | cd01563 | Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
14-305 | 8.94e-25 | |||||||
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants. Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 104.21 E-value: 8.94e-25
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| ThrC | COG0498 | Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
14-302 | 1.22e-23 | |||||||
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 102.20 E-value: 1.22e-23
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| PRK06381 | PRK06381 | threonine synthase; Validated |
14-307 | 2.21e-17 | |||||||
threonine synthase; Validated Pssm-ID: 235789 Cd Length: 319 Bit Score: 82.83 E-value: 2.21e-17
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| IlvA | COG1171 | Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
16-302 | 3.97e-16 | |||||||
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 78.92 E-value: 3.97e-16
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| Thr-dehyd | cd01562 | Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
16-302 | 4.35e-15 | |||||||
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions. Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 75.60 E-value: 4.35e-15
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| thrC | TIGR00260 | threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
3-298 | 1.21e-13 | |||||||
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 71.64 E-value: 1.21e-13
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| L-Ser-dehyd | cd06448 | Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
15-206 | 1.31e-13 | |||||||
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia. Pssm-ID: 107209 Cd Length: 316 Bit Score: 71.56 E-value: 1.31e-13
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| PRK06815 | PRK06815 | threonine/serine dehydratase; |
6-302 | 7.12e-12 | |||||||
threonine/serine dehydratase; Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 66.25 E-value: 7.12e-12
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| PRK08246 | PRK08246 | serine/threonine dehydratase; |
16-190 | 1.03e-11 | |||||||
serine/threonine dehydratase; Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 65.75 E-value: 1.03e-11
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| PRK08329 | PRK08329 | threonine synthase; Validated |
16-301 | 1.28e-11 | |||||||
threonine synthase; Validated Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 65.62 E-value: 1.28e-11
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
345-414 | 8.80e-11 | |||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 59.49 E-value: 8.80e-11
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
333-457 | 8.88e-11 | |||||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 59.49 E-value: 8.88e-11
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| PRK06450 | PRK06450 | threonine synthase; Validated |
14-283 | 2.08e-10 | |||||||
threonine synthase; Validated Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 62.06 E-value: 2.08e-10
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
345-451 | 2.22e-10 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 57.64 E-value: 2.22e-10
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
333-453 | 2.31e-10 | |||||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 59.90 E-value: 2.31e-10
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| PRK05638 | PRK05638 | threonine synthase; Validated |
7-286 | 5.04e-10 | |||||||
threonine synthase; Validated Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 61.37 E-value: 5.04e-10
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| PRK06110 | PRK06110 | threonine dehydratase; |
29-114 | 1.39e-09 | |||||||
threonine dehydratase; Pssm-ID: 235699 Cd Length: 322 Bit Score: 59.24 E-value: 1.39e-09
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| PRK12483 | PRK12483 | threonine dehydratase; Reviewed |
29-299 | 1.92e-09 | |||||||
threonine dehydratase; Reviewed Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 59.81 E-value: 1.92e-09
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| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-414 | 3.03e-09 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 55.12 E-value: 3.03e-09
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| CBS_pair_bac_euk | cd04623 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
342-412 | 2.05e-08 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 52.03 E-value: 2.05e-08
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
332-388 | 4.11e-08 | |||||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 49.52 E-value: 4.11e-08
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| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
344-412 | 8.68e-08 | |||||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 50.50 E-value: 8.68e-08
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
332-414 | 1.48e-07 | |||||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 49.83 E-value: 1.48e-07
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| PLN02970 | PLN02970 | serine racemase |
16-211 | 1.84e-07 | |||||||
serine racemase Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 52.76 E-value: 1.84e-07
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| PLN02550 | PLN02550 | threonine dehydratase |
31-289 | 2.33e-07 | |||||||
threonine dehydratase Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 53.00 E-value: 2.33e-07
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
345-388 | 2.46e-07 | |||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 49.48 E-value: 2.46e-07
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| AF2118 | COG3620 | Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
332-451 | 2.51e-07 | |||||||
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription]; Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 48.48 E-value: 2.51e-07
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| PRK06608 | PRK06608 | serine/threonine dehydratase; |
31-209 | 6.91e-07 | |||||||
serine/threonine dehydratase; Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 50.92 E-value: 6.91e-07
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| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
344-388 | 9.12e-07 | |||||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 45.58 E-value: 9.12e-07
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| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-388 | 1.11e-06 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 47.42 E-value: 1.11e-06
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
332-388 | 1.95e-06 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 46.47 E-value: 1.95e-06
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| eutB | PRK07476 | threonine dehydratase; Provisional |
16-189 | 3.93e-06 | |||||||
threonine dehydratase; Provisional Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 48.42 E-value: 3.93e-06
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| CBS_pair_arch1_repeat2 | cd04632 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
345-414 | 9.59e-06 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 45.01 E-value: 9.59e-06
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| CBS_pair_BON_assoc | cd04586 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-388 | 1.70e-05 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 44.34 E-value: 1.70e-05
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| CBS_pair_Euryarchaeota | cd17784 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
345-388 | 2.52e-05 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 43.56 E-value: 2.52e-05
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| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
345-388 | 2.92e-05 | |||||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.75 E-value: 2.92e-05
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| PRK08638 | PRK08638 | bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
4-190 | 3.10e-05 | |||||||
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 45.88 E-value: 3.10e-05
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| Trp-synth_B | cd06446 | Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
16-298 | 3.22e-05 | |||||||
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions. Pssm-ID: 107207 Cd Length: 365 Bit Score: 45.99 E-value: 3.22e-05
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| CBS_pair_peptidase_M50 | cd04801 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
345-388 | 3.87e-05 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 42.94 E-value: 3.87e-05
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| CBS_archAMPK_gamma-repeat2 | cd04631 | CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ... |
330-388 | 1.05e-04 | |||||||
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 41.83 E-value: 1.05e-04
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| PRK08813 | PRK08813 | threonine dehydratase; Provisional |
16-190 | 1.14e-04 | |||||||
threonine dehydratase; Provisional Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 44.23 E-value: 1.14e-04
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| CBS_pair_voltage-gated_CLC_bac | cd04613 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
332-388 | 1.50e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 41.41 E-value: 1.50e-04
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| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
332-387 | 1.81e-04 | |||||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 43.67 E-value: 1.81e-04
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| CBS_pair_Euryarchaeota | cd17784 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
345-407 | 1.85e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 40.87 E-value: 1.85e-04
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| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
339-452 | 2.08e-04 | |||||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 43.53 E-value: 2.08e-04
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| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
345-388 | 2.47e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 40.60 E-value: 2.47e-04
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| CBS_pair_inorgPPase | cd04597 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ... |
344-391 | 3.59e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 40.02 E-value: 3.59e-04
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| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
343-387 | 4.44e-04 | |||||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 39.71 E-value: 4.44e-04
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| CBS_pair_bac | cd04629 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
344-414 | 4.65e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 39.73 E-value: 4.65e-04
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| CBS_pair_HPP_assoc | cd04600 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-388 | 7.32e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 39.47 E-value: 7.32e-04
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| CBS_pair_DHH_polyA_Pol_assoc | cd04595 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
323-388 | 9.04e-04 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 38.63 E-value: 9.04e-04
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| CBS_pair_arch2_repeat1 | cd04638 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
345-387 | 1.35e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 38.09 E-value: 1.35e-03
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| PRK09224 | PRK09224 | threonine ammonia-lyase IlvA; |
29-200 | 1.38e-03 | |||||||
threonine ammonia-lyase IlvA; Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 40.89 E-value: 1.38e-03
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| CBS_pair_GGDEF_PAS_repeat1 | cd09833 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ... |
343-414 | 1.81e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341403 [Multi-domain] Cd Length: 116 Bit Score: 37.97 E-value: 1.81e-03
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| CBS_pair_arch_MET2_assoc | cd04605 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-387 | 2.20e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 37.99 E-value: 2.20e-03
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| CBS_pair_arch | cd17776 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ... |
345-388 | 2.45e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341412 [Multi-domain] Cd Length: 115 Bit Score: 37.77 E-value: 2.45e-03
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| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
345-412 | 2.50e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 37.50 E-value: 2.50e-03
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| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
345-388 | 2.62e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 37.50 E-value: 2.62e-03
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| CBS_pair_GGDEF_assoc | cd04599 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-389 | 2.64e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 37.32 E-value: 2.64e-03
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| CBS_pair_GGDEF_assoc | cd04599 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-412 | 2.80e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 37.32 E-value: 2.80e-03
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| CBS_euAMPK_gamma-like_repeat2 | cd04641 | CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ... |
337-388 | 2.88e-03 | |||||||
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341399 [Multi-domain] Cd Length: 124 Bit Score: 37.49 E-value: 2.88e-03
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| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd04587 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
335-414 | 3.41e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 37.02 E-value: 3.41e-03
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| PRK07334 | PRK07334 | threonine dehydratase; Provisional |
15-189 | 3.64e-03 | |||||||
threonine dehydratase; Provisional Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 39.49 E-value: 3.64e-03
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| CBS_two-component_sensor_histidine_kinase_repeat2 | cd17774 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
345-388 | 3.71e-03 | |||||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 37.52 E-value: 3.71e-03
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| CBS_pair_arch2_repeat2 | cd04614 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
351-388 | 4.06e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341386 [Multi-domain] Cd Length: 150 Bit Score: 37.64 E-value: 4.06e-03
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| CBS_pair_voltage-gated_CLC_euk_bac | cd04592 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
333-387 | 6.25e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341368 [Multi-domain] Cd Length: 128 Bit Score: 36.96 E-value: 6.25e-03
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| CBS_pair_bac | cd17783 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
350-388 | 7.03e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341419 [Multi-domain] Cd Length: 108 Bit Score: 36.01 E-value: 7.03e-03
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| CBS_pair_DHH_polyA_Pol_assoc | cd17772 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
345-452 | 7.47e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 36.39 E-value: 7.47e-03
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| Qor | COG0604 | NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ... |
55-138 | 7.56e-03 | |||||||
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only]; Pssm-ID: 440369 [Multi-domain] Cd Length: 322 Bit Score: 38.21 E-value: 7.56e-03
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| CBS_arch_repeat2 | cd17778 | CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ... |
344-397 | 7.99e-03 | |||||||
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 36.54 E-value: 7.99e-03
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| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
345-414 | 9.52e-03 | |||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 35.98 E-value: 9.52e-03
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| PRK08206 | PRK08206 | diaminopropionate ammonia-lyase; Provisional |
67-139 | 9.55e-03 | |||||||
diaminopropionate ammonia-lyase; Provisional Pssm-ID: 236186 Cd Length: 399 Bit Score: 38.32 E-value: 9.55e-03
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