D-arabinose 5-phosphate isomerase [Escherichia coli O157:H7 str. Sakai]
Protein Classification
KpsF/GutQ family sugar isomerase( domain architecture ID 11485066)
KpsF/GutQ family sugar isomerase similar to arabinose 5-phosphate isomerases KpsF and GutQ, which catalyze the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK10892 | PRK10892 | arabinose-5-phosphate isomerase KdsD; |
3-328 | 0e+00 | ||||||
arabinose-5-phosphate isomerase KdsD; : Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 680.68 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK10892 | PRK10892 | arabinose-5-phosphate isomerase KdsD; |
3-328 | 0e+00 | ||||||
arabinose-5-phosphate isomerase KdsD; Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 680.68 E-value: 0e+00
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| kpsF | TIGR00393 | KpsF/GutQ family protein; This model describes a number of closely related proteins with the ... |
50-318 | 9.03e-163 | ||||||
KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars] Pssm-ID: 129488 [Multi-domain] Cd Length: 268 Bit Score: 454.65 E-value: 9.03e-163
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| GutQ | COG0794 | D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
11-322 | 2.46e-145 | ||||||
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 412.06 E-value: 2.46e-145
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| SIS_Kpsf | cd05014 | KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
50-177 | 4.22e-74 | ||||||
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway. Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 224.34 E-value: 4.22e-74
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| SIS | pfam01380 | SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
45-177 | 4.59e-36 | ||||||
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway. Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 126.64 E-value: 4.59e-36
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK10892 | PRK10892 | arabinose-5-phosphate isomerase KdsD; |
3-328 | 0e+00 | ||||||
arabinose-5-phosphate isomerase KdsD; Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 680.68 E-value: 0e+00
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| kpsF | TIGR00393 | KpsF/GutQ family protein; This model describes a number of closely related proteins with the ... |
50-318 | 9.03e-163 | ||||||
KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars] Pssm-ID: 129488 [Multi-domain] Cd Length: 268 Bit Score: 454.65 E-value: 9.03e-163
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| GutQ | COG0794 | D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
11-322 | 2.46e-145 | ||||||
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 412.06 E-value: 2.46e-145
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| gutQ | PRK11543 | arabinose-5-phosphate isomerase GutQ; |
14-328 | 3.62e-117 | ||||||
arabinose-5-phosphate isomerase GutQ; Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 340.98 E-value: 3.62e-117
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| SIS_Kpsf | cd05014 | KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
50-177 | 4.22e-74 | ||||||
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway. Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 224.34 E-value: 4.22e-74
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| CBS_pair_SIS_assoc | cd04604 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
202-324 | 3.11e-56 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain] Cd Length: 124 Bit Score: 178.34 E-value: 3.11e-56
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| SIS | pfam01380 | SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
45-177 | 4.59e-36 | ||||||
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway. Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 126.64 E-value: 4.59e-36
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
206-325 | 4.18e-33 | ||||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 118.78 E-value: 4.18e-33
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
204-327 | 1.56e-27 | ||||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 104.18 E-value: 1.56e-27
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| RpiR | COG1737 | DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
5-183 | 1.34e-20 | ||||||
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription]; Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 89.60 E-value: 1.34e-20
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| SIS_RpiR | cd05013 | RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
50-177 | 3.38e-19 | ||||||
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate. Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 82.28 E-value: 3.38e-19
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
136-325 | 3.54e-19 | ||||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 84.16 E-value: 3.54e-19
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
214-324 | 9.38e-18 | ||||||
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: 77.67 E-value: 9.38e-18
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| AgaS | COG2222 | Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
50-187 | 5.61e-16 | ||||||
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 77.25 E-value: 5.61e-16
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| SIS_PHI | cd05005 | Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
50-188 | 6.97e-15 | ||||||
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI. Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 71.45 E-value: 6.97e-15
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
204-325 | 8.89e-13 | ||||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 64.50 E-value: 8.89e-13
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| CBS_pair_bac_euk | cd04623 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
213-324 | 2.60e-12 | ||||||
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: 62.43 E-value: 2.60e-12
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| CBS_pair_MUG70_1 | cd17781 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ... |
219-319 | 9.72e-12 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341417 [Multi-domain] Cd Length: 118 Bit Score: 61.06 E-value: 9.72e-12
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| SIS_GlmS_GlmD_1 | cd05008 | SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
51-178 | 2.21e-11 | ||||||
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction. Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 60.20 E-value: 2.21e-11
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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 ... |
222-325 | 3.17e-11 | ||||||
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: 59.75 E-value: 3.17e-11
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| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd17771 | CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ... |
218-323 | 4.06e-11 | ||||||
CBS domain protein; 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: 341407 [Multi-domain] Cd Length: 115 Bit Score: 59.25 E-value: 4.06e-11
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| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
201-325 | 1.13e-09 | ||||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 55.69 E-value: 1.13e-09
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| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
219-325 | 4.52e-09 | ||||||
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: 53.68 E-value: 4.52e-09
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| SIS | cd04795 | SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
52-130 | 5.18e-09 | ||||||
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 52.76 E-value: 5.18e-09
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| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
219-324 | 1.03e-08 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. 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: 341381 [Multi-domain] Cd Length: 112 Bit Score: 52.45 E-value: 1.03e-08
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| PRK11337 | PRK11337 | MurR/RpiR family transcriptional regulator; |
56-180 | 1.82e-08 | ||||||
MurR/RpiR family transcriptional regulator; Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 54.77 E-value: 1.82e-08
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| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
205-325 | 8.96e-08 | ||||||
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: 50.11 E-value: 8.96e-08
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| CBS_pair_peptidase_M50 | cd04801 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
208-325 | 4.64e-07 | ||||||
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: 47.95 E-value: 4.64e-07
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| CBS_pair_MUG70_2 | cd17782 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ... |
222-318 | 1.87e-06 | ||||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341418 [Multi-domain] Cd Length: 118 Bit Score: 46.09 E-value: 1.87e-06
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| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
219-322 | 2.59e-06 | ||||||
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: 45.49 E-value: 2.59e-06
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| CBS_pair_BON_assoc | cd04586 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
219-325 | 3.27e-06 | ||||||
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: 45.88 E-value: 3.27e-06
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| CBS_two-component_sensor_histidine_kinase_repeat1 | cd04620 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
245-317 | 4.78e-06 | ||||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; 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: 341389 [Multi-domain] Cd Length: 136 Bit Score: 45.61 E-value: 4.78e-06
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
273-325 | 1.34e-05 | ||||||
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: 42.20 E-value: 1.34e-05
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| CBS_pair_bac | cd04630 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
206-325 | 4.91e-05 | ||||||
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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 42.20 E-value: 4.91e-05
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| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
219-325 | 1.98e-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: 40.22 E-value: 1.98e-04
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| GlmS | COG0449 | Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
94-183 | 2.41e-04 | ||||||
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 42.69 E-value: 2.41e-04
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| PRK11557 | PRK11557 | MurR/RpiR family transcriptional regulator; |
51-180 | 3.65e-04 | ||||||
MurR/RpiR family transcriptional regulator; Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 41.67 E-value: 3.65e-04
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| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd04589 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
219-323 | 4.02e-04 | ||||||
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: 341365 [Multi-domain] Cd Length: 113 Bit Score: 39.48 E-value: 4.02e-04
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
273-327 | 4.48e-04 | ||||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.43 E-value: 4.48e-04
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| CBS_pair_arch | cd17776 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ... |
219-325 | 4.62e-04 | ||||||
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: 39.31 E-value: 4.62e-04
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| CBS_archAMPK_gamma-repeat2 | cd04631 | CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ... |
245-325 | 4.84e-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: 39.52 E-value: 4.84e-04
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| SIS_PGI_PMI_1 | cd05017 | The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
51-130 | 6.51e-04 | ||||||
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain. Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 38.79 E-value: 6.51e-04
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| PRK00331 | PRK00331 | isomerizing glutamine--fructose-6-phosphate transaminase; |
94-193 | 7.00e-04 | ||||||
isomerizing glutamine--fructose-6-phosphate transaminase; Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 41.18 E-value: 7.00e-04
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| SIS_GmhA | cd05006 | Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
18-147 | 9.34e-04 | ||||||
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh). Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 39.42 E-value: 9.34e-04
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
206-262 | 1.17e-03 | ||||||
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: 36.42 E-value: 1.17e-03
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| CBS_arch_repeat1 | cd17777 | CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ... |
219-324 | 1.72e-03 | ||||||
CBS pair domains found in archeal proteins, repeat 1; 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: 341413 [Multi-domain] Cd Length: 137 Bit Score: 38.09 E-value: 1.72e-03
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| TlyC | COG1253 | Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ... |
258-325 | 1.80e-03 | ||||||
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only]; Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 39.72 E-value: 1.80e-03
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| PRK07807 | PRK07807 | GuaB1 family IMP dehydrogenase-related protein; |
219-327 | 1.84e-03 | ||||||
GuaB1 family IMP dehydrogenase-related protein; Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 39.89 E-value: 1.84e-03
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| gmhA | PRK00414 | D-sedoheptulose 7-phosphate isomerase; |
98-147 | 1.94e-03 | ||||||
D-sedoheptulose 7-phosphate isomerase; Pssm-ID: 179012 [Multi-domain] Cd Length: 192 Bit Score: 38.56 E-value: 1.94e-03
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| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
267-325 | 2.29e-03 | ||||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 39.43 E-value: 2.29e-03
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
282-327 | 2.39e-03 | ||||||
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: 37.22 E-value: 2.39e-03
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| PRK12570 | PRK12570 | N-acetylmuramic acid-6-phosphate etherase; Reviewed |
13-153 | 3.80e-03 | ||||||
N-acetylmuramic acid-6-phosphate etherase; Reviewed Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 38.52 E-value: 3.80e-03
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| PRK13936 | PRK13936 | phosphoheptose isomerase; Provisional |
96-147 | 5.12e-03 | ||||||
phosphoheptose isomerase; Provisional Pssm-ID: 237567 Cd Length: 197 Bit Score: 37.33 E-value: 5.12e-03
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| PRK08674 | PRK08674 | bifunctional phosphoglucose/phosphomannose isomerase; Validated |
13-164 | 5.63e-03 | ||||||
bifunctional phosphoglucose/phosphomannose isomerase; Validated Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 38.04 E-value: 5.63e-03
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| PRK02947 | PRK02947 | sugar isomerase domain-containing protein; |
94-185 | 7.05e-03 | ||||||
sugar isomerase domain-containing protein; Pssm-ID: 179510 [Multi-domain] Cd Length: 246 Bit Score: 37.54 E-value: 7.05e-03
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