hexaprenyldihydroxybenzoate methyltransferase [Saccharomyces cerevisiae S288C]
bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11493423)
bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
UbiG | TIGR01983 | ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
40-305 | 9.60e-113 | |||||
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: 325.40 E-value: 9.60e-113
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Name | Accession | Description | Interval | E-value | |||||
UbiG | TIGR01983 | ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
40-305 | 9.60e-113 | |||||
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: 325.40 E-value: 9.60e-113
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PLN02396 | PLN02396 | hexaprenyldihydroxybenzoate methyltransferase |
21-307 | 2.56e-36 | |||||
hexaprenyldihydroxybenzoate methyltransferase Pssm-ID: 178018 [Multi-domain] Cd Length: 322 Bit Score: 132.93 E-value: 2.56e-36
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UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
125-229 | 7.19e-28 | |||||
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: 104.71 E-value: 7.19e-28
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Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
94-272 | 3.95e-21 | |||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 87.87 E-value: 3.95e-21
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
126-226 | 4.38e-08 | |||||
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: 50.51 E-value: 4.38e-08
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Name | Accession | Description | Interval | E-value | |||||
UbiG | TIGR01983 | ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ... |
40-305 | 9.60e-113 | |||||
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: 325.40 E-value: 9.60e-113
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PLN02396 | PLN02396 | hexaprenyldihydroxybenzoate methyltransferase |
21-307 | 2.56e-36 | |||||
hexaprenyldihydroxybenzoate methyltransferase Pssm-ID: 178018 [Multi-domain] Cd Length: 322 Bit Score: 132.93 E-value: 2.56e-36
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UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
125-229 | 7.19e-28 | |||||
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: 104.71 E-value: 7.19e-28
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Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
94-272 | 3.95e-21 | |||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 87.87 E-value: 3.95e-21
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
126-218 | 1.07e-15 | |||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 71.44 E-value: 1.07e-15
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Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
107-227 | 1.26e-14 | |||||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 69.96 E-value: 1.26e-14
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UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
118-240 | 3.54e-14 | |||||
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: 68.48 E-value: 3.54e-14
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Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
127-225 | 1.57e-13 | |||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 65.38 E-value: 1.57e-13
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Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
125-227 | 6.89e-12 | |||||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 60.99 E-value: 6.89e-12
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COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
125-227 | 1.53e-10 | |||||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 59.24 E-value: 1.53e-10
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Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
127-223 | 3.36e-10 | |||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 56.22 E-value: 3.36e-10
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SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
121-226 | 3.88e-10 | |||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 58.39 E-value: 3.88e-10
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PRK07580 | PRK07580 | Mg-protoporphyrin IX methyl transferase; Validated |
122-201 | 1.22e-09 | |||||
Mg-protoporphyrin IX methyl transferase; Validated Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 57.54 E-value: 1.22e-09
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
126-226 | 4.38e-08 | |||||
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: 50.51 E-value: 4.38e-08
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PrmA | COG2264 | Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
112-226 | 1.42e-07 | |||||
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 51.71 E-value: 1.42e-07
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PRK06202 | PRK06202 | hypothetical protein; Provisional |
124-215 | 2.04e-07 | |||||
hypothetical protein; Provisional Pssm-ID: 180466 [Multi-domain] Cd Length: 232 Bit Score: 50.77 E-value: 2.04e-07
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PrmA | pfam06325 | Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
121-228 | 5.22e-07 | |||||
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences. Pssm-ID: 428888 [Multi-domain] Cd Length: 294 Bit Score: 50.34 E-value: 5.22e-07
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Methyltransf_31 | pfam13847 | Methyltransferase domain; This family appears to have methyltransferase activity. |
120-226 | 1.31e-06 | |||||
Methyltransferase domain; This family appears to have methyltransferase activity. Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 47.41 E-value: 1.31e-06
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PLN02244 | PLN02244 | tocopherol O-methyltransferase |
108-212 | 7.08e-06 | |||||
tocopherol O-methyltransferase Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 47.05 E-value: 7.08e-06
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COG4076 | COG4076 | Predicted RNA methylase [General function prediction only]; |
121-243 | 1.35e-05 | |||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 45.41 E-value: 1.35e-05
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BioC | TIGR02072 | malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
105-228 | 5.94e-05 | |||||
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin] Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 43.43 E-value: 5.94e-05
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PRK14968 | PRK14968 | putative methyltransferase; Provisional |
117-194 | 8.59e-05 | |||||
putative methyltransferase; Provisional Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 42.58 E-value: 8.59e-05
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prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
112-228 | 1.24e-04 | |||||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 42.83 E-value: 1.24e-04
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prmA | TIGR00406 | ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ... |
125-228 | 4.91e-04 | |||||
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification] Pssm-ID: 273061 Cd Length: 288 Bit Score: 40.97 E-value: 4.91e-04
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PLN02585 | PLN02585 | magnesium protoporphyrin IX methyltransferase |
124-201 | 5.69e-04 | |||||
magnesium protoporphyrin IX methyltransferase Pssm-ID: 215319 [Multi-domain] Cd Length: 315 Bit Score: 41.00 E-value: 5.69e-04
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PRK08317 | PRK08317 | hypothetical protein; Provisional |
118-210 | 5.73e-04 | |||||
hypothetical protein; Provisional Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 40.69 E-value: 5.73e-04
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PRK11705 | PRK11705 | cyclopropane fatty acyl phospholipid synthase; |
118-228 | 1.37e-03 | |||||
cyclopropane fatty acyl phospholipid synthase; Pssm-ID: 183282 Cd Length: 383 Bit Score: 39.83 E-value: 1.37e-03
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Methyltransf_32 | pfam13679 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
114-168 | 2.60e-03 | |||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 379330 [Multi-domain] Cd Length: 138 Bit Score: 37.55 E-value: 2.60e-03
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metW | TIGR02081 | methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ... |
121-210 | 3.24e-03 | |||||
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273958 Cd Length: 194 Bit Score: 38.12 E-value: 3.24e-03
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PRK11036 | PRK11036 | tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; |
112-225 | 3.99e-03 | |||||
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM; Pssm-ID: 182918 Cd Length: 255 Bit Score: 38.02 E-value: 3.99e-03
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MetW | pfam07021 | Methionine biosynthesis protein MetW; This family consists of several bacterial and one ... |
121-210 | 3.99e-03 | |||||
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: 37.82 E-value: 3.99e-03
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PRK09328 | PRK09328 | N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
112-193 | 6.72e-03 | |||||
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 37.45 E-value: 6.72e-03
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CMAS | pfam02353 | Mycolic acid cyclopropane synthetase; This family consist of ... |
94-202 | 8.21e-03 | |||||
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 37.31 E-value: 8.21e-03
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Blast search parameters | ||||
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