bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Duganella zoogloeoides]
class I SAM-dependent methyltransferase( domain architecture ID 11454890)
class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor
List of domain hits
Name | Accession | Description | Interval | E-value | |||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
62-172 | 8.13e-24 | |||
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis : Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 93.54 E-value: 8.13e-24
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Name | Accession | Description | Interval | E-value | ||||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
62-172 | 8.13e-24 | ||||
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 93.54 E-value: 8.13e-24
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Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
57-223 | 4.41e-23 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 92.88 E-value: 4.41e-23
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UbiG | TIGR01983 | ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
78-168 | 8.17e-07 | ||||
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone] Pssm-ID: 273910 Cd Length: 224 Bit Score: 48.83 E-value: 8.17e-07
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
78-168 | 1.35e-06 | ||||
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 46.27 E-value: 1.35e-06
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PRK08317 | PRK08317 | hypothetical protein; Provisional |
54-226 | 1.43e-03 | ||||
hypothetical protein; Provisional Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 39.15 E-value: 1.43e-03
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Name | Accession | Description | Interval | E-value | ||||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
62-172 | 8.13e-24 | ||||
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 93.54 E-value: 8.13e-24
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Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
57-223 | 4.41e-23 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 92.88 E-value: 4.41e-23
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UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
72-190 | 6.51e-12 | ||||
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 61.93 E-value: 6.51e-12
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COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
67-179 | 1.60e-11 | ||||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 61.94 E-value: 1.60e-11
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Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
75-168 | 1.64e-11 | ||||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 59.84 E-value: 1.64e-11
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Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
72-168 | 2.11e-10 | ||||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 58.02 E-value: 2.11e-10
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Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
80-166 | 9.82e-10 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 54.68 E-value: 9.82e-10
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Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
80-168 | 3.72e-09 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 53.05 E-value: 3.72e-09
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SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
74-168 | 2.54e-08 | ||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 53.00 E-value: 2.54e-08
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
80-164 | 1.14e-07 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 48.71 E-value: 1.14e-07
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UbiG | TIGR01983 | ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
78-168 | 8.17e-07 | ||||
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone] Pssm-ID: 273910 Cd Length: 224 Bit Score: 48.83 E-value: 8.17e-07
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
78-168 | 1.35e-06 | ||||
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 46.27 E-value: 1.35e-06
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Methyltransf_31 | pfam13847 | Methyltransferase domain; This family appears to have methyltransferase activity. |
78-202 | 2.16e-04 | ||||
Methyltransferase domain; This family appears to have methyltransferase activity. Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.86 E-value: 2.16e-04
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MetW | pfam07021 | Methionine biosynthesis protein MetW; This family consists of several bacterial and one ... |
62-146 | 2.42e-04 | ||||
Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells. Pssm-ID: 399779 Cd Length: 193 Bit Score: 41.29 E-value: 2.42e-04
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COG4627 | COG4627 | Predicted SAM-depedendent methyltransferase [General function prediction only]; |
78-226 | 5.50e-04 | ||||
Predicted SAM-depedendent methyltransferase [General function prediction only]; Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 39.85 E-value: 5.50e-04
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PRK08317 | PRK08317 | hypothetical protein; Provisional |
54-226 | 1.43e-03 | ||||
hypothetical protein; Provisional Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 39.15 E-value: 1.43e-03
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Blast search parameters | ||||
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