MULTISPECIES: phosphotransferase family protein [unclassified Sphingomonas]
Protein Classification
phosphotransferase family protein( domain architecture ID 10142358)
phosphotransferase family protein may catalyze the phosphorylation of aminoglycosides and confer aminoglycoside antibiotic resistance
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ACAD10_11_N-like | cd05154 | N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
24-275 | 9.00e-104 | |||||
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: 304.92 E-value: 9.00e-104
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| Name | Accession | Description | Interval | E-value | ||||||
| ACAD10_11_N-like | cd05154 | N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
24-275 | 9.00e-104 | ||||||
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: 304.92 E-value: 9.00e-104
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| YcbJ | COG3173 | Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
3-290 | 1.48e-90 | ||||||
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only]; Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 272.37 E-value: 1.48e-90
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| PLN02876 | PLN02876 | acyl-CoA dehydrogenase |
4-335 | 3.82e-88 | ||||||
acyl-CoA dehydrogenase Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 281.68 E-value: 3.82e-88
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| APH | pfam01636 | Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
29-248 | 3.56e-49 | ||||||
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: 164.60 E-value: 3.56e-49
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| CHK | smart00587 | ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases |
197-248 | 5.03e-04 | ||||||
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases Pssm-ID: 214734 Cd Length: 196 Bit Score: 40.39 E-value: 5.03e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| ACAD10_11_N-like | cd05154 | N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
24-275 | 9.00e-104 | ||||||
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: 304.92 E-value: 9.00e-104
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| YcbJ | COG3173 | Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
3-290 | 1.48e-90 | ||||||
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only]; Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 272.37 E-value: 1.48e-90
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| PLN02876 | PLN02876 | acyl-CoA dehydrogenase |
4-335 | 3.82e-88 | ||||||
acyl-CoA dehydrogenase Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 281.68 E-value: 3.82e-88
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| APH | pfam01636 | Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
29-248 | 3.56e-49 | ||||||
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: 164.60 E-value: 3.56e-49
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| APH_ChoK_like | cd05120 | Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
24-241 | 4.93e-18 | ||||||
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, 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). The members of this family 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 family 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: 270690 [Multi-domain] Cd Length: 158 Bit Score: 80.04 E-value: 4.93e-18
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| SrkA | COG2334 | Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
22-246 | 1.24e-13 | ||||||
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 70.34 E-value: 1.24e-13
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| HomoserineK_II | cd05153 | Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
22-248 | 1.41e-12 | ||||||
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain] Cd Length: 300 Bit Score: 67.28 E-value: 1.41e-12
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| ChoK-like | cd05151 | Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ... |
24-141 | 4.23e-05 | ||||||
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270700 [Multi-domain] Cd Length: 152 Bit Score: 42.93 E-value: 4.23e-05
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| CotS | COG0510 | Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
160-238 | 8.00e-05 | ||||||
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 42.46 E-value: 8.00e-05
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| Bud32 | COG3642 | tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ... |
66-234 | 1.00e-04 | ||||||
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 442859 [Multi-domain] Cd Length: 159 Bit Score: 42.25 E-value: 1.00e-04
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| RIO2 | COG0478 | RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ... |
66-140 | 1.81e-04 | ||||||
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms]; Pssm-ID: 440246 [Multi-domain] Cd Length: 183 Bit Score: 41.81 E-value: 1.81e-04
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| RIO2_C | cd05144 | C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ... |
47-139 | 3.23e-04 | ||||||
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). Pssm-ID: 270695 [Multi-domain] Cd Length: 183 Bit Score: 40.95 E-value: 3.23e-04
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| APH_ChoK_like_1 | cd05155 | Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ... |
66-235 | 4.54e-04 | ||||||
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: 41.07 E-value: 4.54e-04
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| CHK | smart00587 | ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases |
197-248 | 5.03e-04 | ||||||
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases Pssm-ID: 214734 Cd Length: 196 Bit Score: 40.39 E-value: 5.03e-04
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| APH | cd05150 | Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ... |
37-224 | 1.07e-03 | ||||||
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH 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: 270699 [Multi-domain] Cd Length: 244 Bit Score: 39.87 E-value: 1.07e-03
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| EcKL | pfam02958 | Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ... |
197-248 | 4.09e-03 | ||||||
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes. Pssm-ID: 397213 [Multi-domain] Cd Length: 293 Bit Score: 38.40 E-value: 4.09e-03
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| MPH2' | cd05152 | Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ... |
95-277 | 5.28e-03 | ||||||
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: 37.99 E-value: 5.28e-03
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