3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomerase [Bacillus subtilis]
cupin domain-containing protein( domain architecture ID 14449041)
cupin domain-containing protein such as Bacillus subtilis BacB that is involved in the synthesis of bacilysin, a non-ribosomally synthesized dipeptide antibiotic that is active against a wide range of bacteria and fungi
List of domain hits
Name | Accession | Description | Interval | E-value | |||
cupin_BacB_N | cd20307 | Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ... |
11-110 | 6.63e-54 | |||
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. : Pssm-ID: 380441 [Multi-domain] Cd Length: 100 Bit Score: 168.59 E-value: 6.63e-54
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cupin_BacB_C | cd10547 | Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ... |
127-219 | 3.29e-49 | |||
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. : Pssm-ID: 380415 [Multi-domain] Cd Length: 92 Bit Score: 156.27 E-value: 3.29e-49
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Name | Accession | Description | Interval | E-value | |||
cupin_BacB_N | cd20307 | Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ... |
11-110 | 6.63e-54 | |||
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380441 [Multi-domain] Cd Length: 100 Bit Score: 168.59 E-value: 6.63e-54
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cupin_BacB_C | cd10547 | Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ... |
127-219 | 3.29e-49 | |||
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380415 [Multi-domain] Cd Length: 92 Bit Score: 156.27 E-value: 3.29e-49
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
22-106 | 4.63e-12 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 60.63 E-value: 4.63e-12
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
41-106 | 7.59e-11 | |||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 56.50 E-value: 7.59e-11
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
156-222 | 9.09e-08 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 48.69 E-value: 9.09e-08
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
156-218 | 2.15e-07 | |||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 46.87 E-value: 2.15e-07
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Name | Accession | Description | Interval | E-value | |||
cupin_BacB_N | cd20307 | Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ... |
11-110 | 6.63e-54 | |||
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380441 [Multi-domain] Cd Length: 100 Bit Score: 168.59 E-value: 6.63e-54
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cupin_BacB_C | cd10547 | Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ... |
127-219 | 3.29e-49 | |||
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380415 [Multi-domain] Cd Length: 92 Bit Score: 156.27 E-value: 3.29e-49
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cupin_BacB | cd06975 | Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ... |
16-108 | 3.28e-45 | |||
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Pssm-ID: 380380 [Multi-domain] Cd Length: 93 Bit Score: 146.19 E-value: 3.28e-45
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cupin_BacB | cd06975 | Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ... |
127-219 | 7.10e-41 | |||
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Pssm-ID: 380380 [Multi-domain] Cd Length: 93 Bit Score: 135.01 E-value: 7.10e-41
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cupin_BacB_C | cd10547 | Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ... |
35-106 | 4.03e-17 | |||
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380415 [Multi-domain] Cd Length: 92 Bit Score: 73.84 E-value: 4.03e-17
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cupin_KdgF | cd02238 | pectin degradation protein KdgF and related proteins, cupin domain; This family includes ... |
18-106 | 1.20e-14 | |||
pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380366 [Multi-domain] Cd Length: 104 Bit Score: 67.49 E-value: 1.20e-14
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
22-106 | 4.63e-12 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 60.63 E-value: 4.63e-12
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
41-106 | 7.59e-11 | |||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 56.50 E-value: 7.59e-11
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cupin_KdgF | cd02238 | pectin degradation protein KdgF and related proteins, cupin domain; This family includes ... |
129-222 | 5.78e-10 | |||
pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380366 [Multi-domain] Cd Length: 104 Bit Score: 54.78 E-value: 5.78e-10
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ManC | COG0662 | Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; |
7-106 | 4.13e-09 | |||
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440426 [Multi-domain] Cd Length: 114 Bit Score: 52.84 E-value: 4.13e-09
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cupin_DddK | cd06988 | Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
41-106 | 1.34e-08 | |||
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380393 [Multi-domain] Cd Length: 76 Bit Score: 50.31 E-value: 1.34e-08
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QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
156-222 | 9.09e-08 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 48.69 E-value: 9.09e-08
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
156-218 | 2.15e-07 | |||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 46.87 E-value: 2.15e-07
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cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
40-106 | 4.86e-07 | |||
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation. Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 45.94 E-value: 4.86e-07
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cupin_XRE_C | cd02209 | XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ... |
35-104 | 5.58e-07 | |||
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380339 [Multi-domain] Cd Length: 90 Bit Score: 46.35 E-value: 5.58e-07
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cupin_MJ1618 | cd02214 | Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ... |
41-104 | 1.64e-05 | |||
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. Pssm-ID: 380344 [Multi-domain] Cd Length: 100 Bit Score: 42.50 E-value: 1.64e-05
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cupin_TM1459-like | cd02222 | Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ... |
40-100 | 2.10e-04 | |||
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer. Pssm-ID: 380351 [Multi-domain] Cd Length: 91 Bit Score: 38.97 E-value: 2.10e-04
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cupin_TTHA0104 | cd06122 | Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ... |
49-102 | 3.81e-04 | |||
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel). Pssm-ID: 380377 [Multi-domain] Cd Length: 102 Bit Score: 38.69 E-value: 3.81e-04
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cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
156-218 | 1.35e-03 | |||
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation. Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 36.31 E-value: 1.35e-03
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cupin_DRT102 | cd06989 | Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ... |
41-102 | 1.71e-03 | |||
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380394 Cd Length: 97 Bit Score: 36.74 E-value: 1.71e-03
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cupin_TM1459-like | cd02222 | Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ... |
156-211 | 2.32e-03 | |||
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer. Pssm-ID: 380351 [Multi-domain] Cd Length: 91 Bit Score: 36.27 E-value: 2.32e-03
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cupin_PMI_typeII_C | cd02213 | Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ... |
60-109 | 3.49e-03 | |||
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif. Pssm-ID: 380343 [Multi-domain] Cd Length: 126 Bit Score: 36.38 E-value: 3.49e-03
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cupin_BLL4011-like | cd02235 | Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ... |
41-101 | 5.29e-03 | |||
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380363 [Multi-domain] Cd Length: 100 Bit Score: 35.25 E-value: 5.29e-03
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RmlC | COG4101 | Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only]; |
41-104 | 9.97e-03 | |||
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only]; Pssm-ID: 443277 Cd Length: 146 Bit Score: 35.33 E-value: 9.97e-03
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