transferase [Streptomyces canus]
Protein Classification
aminoglycoside phosphotransferase family protein( domain architecture ID 12025366)
aminoglycoside phosphotransferase family protein may catalyze the phosphorylation of small molecules such as aminoglycosides and confer aminoglycoside antibiotic resistance; similar to Streptomyces coelicolor 3-hydroxyasparagine phosphotransferase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| APH | pfam01636 | Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
34-257 | 4.23e-13 | ||||
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881. : Pssm-ID: 426359 [Multi-domain] Cd Length: 239 Bit Score: 67.53 E-value: 4.23e-13
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| Name | Accession | Description | Interval | E-value | |||||
| APH | pfam01636 | Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
34-257 | 4.23e-13 | |||||
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881. Pssm-ID: 426359 [Multi-domain] Cd Length: 239 Bit Score: 67.53 E-value: 4.23e-13
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| YcbJ | COG3173 | Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
5-257 | 4.79e-12 | |||||
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only]; Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 65.14 E-value: 4.79e-12
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| MPH2' | cd05152 | Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ... |
50-248 | 1.71e-10 | |||||
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). Pssm-ID: 270701 [Multi-domain] Cd Length: 276 Bit Score: 60.72 E-value: 1.71e-10
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| Name | Accession | Description | Interval | E-value | |||||
| APH | pfam01636 | Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
34-257 | 4.23e-13 | |||||
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881. Pssm-ID: 426359 [Multi-domain] Cd Length: 239 Bit Score: 67.53 E-value: 4.23e-13
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| YcbJ | COG3173 | Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
5-257 | 4.79e-12 | |||||
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only]; Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 65.14 E-value: 4.79e-12
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| MPH2' | cd05152 | Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ... |
50-248 | 1.71e-10 | |||||
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). Pssm-ID: 270701 [Multi-domain] Cd Length: 276 Bit Score: 60.72 E-value: 1.71e-10
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| APH_ChoK_like_1 | cd05155 | Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ... |
33-234 | 3.53e-08 | |||||
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). Pssm-ID: 270704 [Multi-domain] Cd Length: 234 Bit Score: 53.39 E-value: 3.53e-08
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| CotS | COG0510 | Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
150-264 | 1.96e-07 | |||||
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 49.78 E-value: 1.96e-07
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| ACAD10_11_N-like | cd05154 | N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
101-234 | 1.13e-04 | |||||
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). Pssm-ID: 270703 [Multi-domain] Cd Length: 254 Bit Score: 42.99 E-value: 1.13e-04
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| Blast search parameters | ||||
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