Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ...
54-295
4.14e-23
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
The actual alignment was detected with superfamily member pfam09459:
Pssm-ID: 472705 Cd Length: 192 Bit Score: 95.17 E-value: 4.14e-23
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits ...
54-295
4.14e-23
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits that catalyzes the anaerobic degradation of hydrocarbons. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
Pssm-ID: 430627 Cd Length: 192 Bit Score: 95.17 E-value: 4.14e-23
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits ...
55-295
2.92e-19
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits that catalyses the anaerobic degradation of hydrocarbons. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
Pssm-ID: 214885 Cd Length: 209 Bit Score: 84.87 E-value: 2.92e-19
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ...
65-292
9.63e-05
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
Pssm-ID: 187675 Cd Length: 158 Bit Score: 42.17 E-value: 9.63e-05
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits ...
54-295
4.14e-23
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits that catalyzes the anaerobic degradation of hydrocarbons. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
Pssm-ID: 430627 Cd Length: 192 Bit Score: 95.17 E-value: 4.14e-23
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits ...
55-295
2.92e-19
Ethylbenzene dehydrogenase; Eythylbenzene dehydrogenase is a heterotrimer of three subunits that catalyses the anaerobic degradation of hydrocarbons. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria.
Pssm-ID: 214885 Cd Length: 209 Bit Score: 84.87 E-value: 2.92e-19
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ...
65-292
9.63e-05
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
Pssm-ID: 187675 Cd Length: 158 Bit Score: 42.17 E-value: 9.63e-05
Heme-binding domain of bacterial ethylbenzene dehydrogenase; Ethylbenzene dehydrogenase (EBDH) ...
45-134
1.31e-03
Heme-binding domain of bacterial ethylbenzene dehydrogenase; Ethylbenzene dehydrogenase (EBDH) is a bacterial molybdopterin enzyme. It catalyzes anaerobic hydroxylation of alkylaromatic compounds to secondary alcohols. The DOMON domain in EBDH and related proteins, typically called the gamma subunit, binds a heme; its function in the catalytic mechanism is unclear. It co-occurs with a molybdopterin-binding subunit and an iron-sulfur protein. This family also contains heme-binding domains of dimethylsulfide dehydrogenase, selenate reductases, and chlorate reductase.
Pssm-ID: 187681 Cd Length: 224 Bit Score: 39.68 E-value: 1.31e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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