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Conserved domains on  [gi|446301146|ref|WP_000379001|]
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MULTISPECIES: aminoglycoside phosphotransferase family protein [Bacillus]

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

CATH:  3.90.1200.10|3.30.200.20
EC:  2.7.1.-
Gene Ontology:  GO:0005524|GO:0016310|GO:0016301
PubMed:  15888308|16244704|15888308

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 19-247 7.06e-38

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: 134.17  E-value: 7.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   19 SYKQNEEGWDNVAIIVND---ELLFRFPRKQEYAMRIPLEKELCTLLScSLHEIEVPKYHLFYEKNTDAIPLCSYYTLIH 95
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTgdgRYVLRLPPPGRAAEELRRELALLRHLA-AAGVPPVPRVLAGCTDAELLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   96 GEPLKTEivttLEKQERKALITQLATFLAALHSIPlKSVTALGFPIEKTLTYWKELQAKLNEYVTNSLTSFQKSTLNRLF 175
Cdd:pfam01636  80 GEVLARP----LLPEERGALLEALGRALARLHAVD-PAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446301146  176 ENFFACLATSkFQNTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDFGHEFTTSVYEQY 247
Cdd:pfam01636 155 AALLALLPAE-LPPVLVHGDLHPGNLLVDPGGR-VSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAY 224
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 19-247 7.06e-38

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: 134.17  E-value: 7.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   19 SYKQNEEGWDNVAIIVND---ELLFRFPRKQEYAMRIPLEKELCTLLScSLHEIEVPKYHLFYEKNTDAIPLCSYYTLIH 95
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTgdgRYVLRLPPPGRAAEELRRELALLRHLA-AAGVPPVPRVLAGCTDAELLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   96 GEPLKTEivttLEKQERKALITQLATFLAALHSIPlKSVTALGFPIEKTLTYWKELQAKLNEYVTNSLTSFQKSTLNRLF 175
Cdd:pfam01636  80 GEVLARP----LLPEERGALLEALGRALARLHAVD-PAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446301146  176 ENFFACLATSkFQNTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDFGHEFTTSVYEQY 247
Cdd:pfam01636 155 AALLALLPAE-LPPVLVHGDLHPGNLLVDPGGR-VSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAY 224
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 23-262 2.34e-26

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: 104.63  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  23 NEEGWD-NVAIIVNDE---LLFRFPRKQEYAMRIPLEKELCTLLSCSLhEIEVPKYHLFyekNTDAIPlcsyYTLIHGEP 98
Cdd:cd05152   19 NESGLDfQVAFARDTEgrrWVLRIPRRPDVSERLEAEKKVLDLVTPHL-PFAVPDWRIH---TPELIA----YPLLPGVP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  99 LKTEIVTTLE-------KQERKALITQLATFLAALHSIPLKSVTALGFPIEKTLTYWKELQAKLNEYVTnsltSFQKST- 170
Cdd:cd05152   91 AATIDPEIQNyvwnwdpLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKE----TFGVPPa 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 171 -LNRlFENFFACLATSKFQNTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDFGHEFTTSVYEQYST 249
Cdd:cd05152  167 lLAR-WQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGR-VTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLDAYEK 244

                        250
                 ....*....|....
gi 446301146 250 LTSH-HDPLLIHRI 262
Cdd:cd05152  245 AGGEvWPRMLEHII 258
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 1-239 1.02e-24

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 100.57  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   1 MDSYKQYIKEALPNLS-IHSYKQNEEGWDNV--AIIVNDELLFRF-PRKQEYAMRIPLEKELCTLLScSLHEIEVPKyHL 76
Cdd:COG3173    5 EAALRALLAAQLPGLAgLPEVEPLSGGWSNLtyRLDTGDRLVLRRpPRGLASAHDVRREARVLRALA-PRLGVPVPR-PL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  77 FYEKNTDAIPLCSY-YTLIHGEPLkTEIVTTLEKQERKALITQLATFLAALHSIPLKSV-TALGFP--IEKTLTYW-KEL 151
Cdd:COG3173   83 ALGEDGEVIGAPFYvMEWVEGETL-EDALPDLSPAERRALARALGEFLAALHAVDPAAAgLADGRPegLERQLARWrAQL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 152 QAKLNEyvtnsltsfqKSTLNRLFENFFACLATSK---FQNTIIHADFTHHHILFDKQNKTISGVIDFGDAQIGDPAFDF 228
Cdd:COG3173  162 RRALAR----------TDDLPALRERLAAWLAANLpewGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPAADL 231

                        250
                 ....*....|...
gi 446301146 229 AGL--YYDFGHEF 239
Cdd:COG3173  232 AYLllYWRLPDDL 244
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 19-247 7.06e-38

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: 134.17  E-value: 7.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   19 SYKQNEEGWDNVAIIVND---ELLFRFPRKQEYAMRIPLEKELCTLLScSLHEIEVPKYHLFYEKNTDAIPLCSYYTLIH 95
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTgdgRYVLRLPPPGRAAEELRRELALLRHLA-AAGVPPVPRVLAGCTDAELLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   96 GEPLKTEivttLEKQERKALITQLATFLAALHSIPlKSVTALGFPIEKTLTYWKELQAKLNEYVTNSLTSFQKSTLNRLF 175
Cdd:pfam01636  80 GEVLARP----LLPEERGALLEALGRALARLHAVD-PAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446301146  176 ENFFACLATSkFQNTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDFGHEFTTSVYEQY 247
Cdd:pfam01636 155 AALLALLPAE-LPPVLVHGDLHPGNLLVDPGGR-VSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAY 224
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 23-262 2.34e-26

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: 104.63  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  23 NEEGWD-NVAIIVNDE---LLFRFPRKQEYAMRIPLEKELCTLLSCSLhEIEVPKYHLFyekNTDAIPlcsyYTLIHGEP 98
Cdd:cd05152   19 NESGLDfQVAFARDTEgrrWVLRIPRRPDVSERLEAEKKVLDLVTPHL-PFAVPDWRIH---TPELIA----YPLLPGVP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  99 LKTEIVTTLE-------KQERKALITQLATFLAALHSIPLKSVTALGFPIEKTLTYWKELQAKLNEYVTnsltSFQKST- 170
Cdd:cd05152   91 AATIDPEIQNyvwnwdpLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKE----TFGVPPa 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 171 -LNRlFENFFACLATSKFQNTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDFGHEFTTSVYEQYST 249
Cdd:cd05152  167 lLAR-WQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGR-VTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLDAYEK 244

                        250
                 ....*....|....
gi 446301146 250 LTSH-HDPLLIHRI 262
Cdd:cd05152  245 AGGEvWPRMLEHII 258
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 1-239 1.02e-24

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 100.57  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146   1 MDSYKQYIKEALPNLS-IHSYKQNEEGWDNV--AIIVNDELLFRF-PRKQEYAMRIPLEKELCTLLScSLHEIEVPKyHL 76
Cdd:COG3173    5 EAALRALLAAQLPGLAgLPEVEPLSGGWSNLtyRLDTGDRLVLRRpPRGLASAHDVRREARVLRALA-PRLGVPVPR-PL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  77 FYEKNTDAIPLCSY-YTLIHGEPLkTEIVTTLEKQERKALITQLATFLAALHSIPLKSV-TALGFP--IEKTLTYW-KEL 151
Cdd:COG3173   83 ALGEDGEVIGAPFYvMEWVEGETL-EDALPDLSPAERRALARALGEFLAALHAVDPAAAgLADGRPegLERQLARWrAQL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 152 QAKLNEyvtnsltsfqKSTLNRLFENFFACLATSK---FQNTIIHADFTHHHILFDKQNKTISGVIDFGDAQIGDPAFDF 228
Cdd:COG3173  162 RRALAR----------TDDLPALRERLAAWLAANLpewGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPAADL 231

                        250
                 ....*....|...
gi 446301146 229 AGL--YYDFGHEF 239
Cdd:COG3173  232 AYLllYWRLPDDL 244
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 18-235 8.12e-17

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: 75.80  E-value: 8.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  18 HSYKQNEEGWDNVAIIVND--ELLFRFPRKQEYAmRIPLEKELCTLLScSLHEIEVPKyhLFYEKNTDAIPLCsYYTLIH 95
Cdd:cd05120    1 ISVKLIKEGGDNKVYLLGDprEYVLKIGPPRLKK-DLEKEAAMLQLLA-GKLSLPVPK--VYGFGESDGWEYL-LMERIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  96 GEPLKTEIVTtLEKQERKALITQLATFLAALHSIPLKSVTalgfpiektltywkelqaklneyvtnsltsfqkstlnrlf 175
Cdd:cd05120   76 GETLSEVWPR-LSEEEKEKIADQLAEILAALHRIDSSVLT---------------------------------------- 114

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 176 enffaclatskfqntiiHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGLYYDF 235
Cdd:cd05120  115 -----------------HGDLHPGNILVKPDGK-LSGIIDWEFAGYGPPAFDYAAALRDW 156
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 25-229 6.08e-13

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: 66.88  E-value: 6.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  25 EGWDNVAIIVNDELLFRFPRKQEYAMRIPLEKELCTLLS--CSLhEIEVPkyhLFYEKNTDAIPLC-SYYTLIHGEPlkt 101
Cdd:cd05155    8 SGWDNATFRLGDDLAVRLPRRAWAAELLEKEQRWLPRLAprLPL-PVPVP---LALGKPGAGYPWPwSVYRWLEGET--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 102 eiVTTLEKQERKALITQLATFLAALHSIPLKSVTALG---FPIEKTLTYWKELQAklneyVTNSLTSFQKSTLNRLFEnf 178
Cdd:cd05155   81 --AADAPLADPAAAAEDLARFLAALHAIDPAGPPNPGrgnPLRGRDLAVRDAEEA-----LAALAGLLDVAAARALWE-- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446301146 179 fACLATS--KFQNTIIHADFTHHHILFDkqNKTISGVIDFGDAQIGDPAFDFA 229
Cdd:cd05155  152 -RALAAPawAGPPVWLHGDLHPGNLLVR--DGRLSAVIDFGDLGVGDPACDLA 201
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 114-229 6.81e-07

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: 49.95  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146 114 ALITQLATFLAALHSIplksvtALGFPIEKTLTY----WKELQAKLNEYVTNSLTSFQKSTLNRLfeNFFACLATSKFQN 189
Cdd:cd05153  108 EQCRAIGAALARLHLA------LAGFPPPRPNPRglawWKPLAERLKARLDLLAADDRALLEDEL--ARLQALAPSDLPR 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446301146 190 TIIHADFTHHHILFDKQNktISGVIDFGDAQIGDPAFDFA 229
Cdd:cd05153  180 GVIHADLFRDNVLFDGDR--LSGIIDFYDACYDPLLYDLA 217
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
171-237 9.36e-07

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 47.85  E-value: 9.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446301146 171 LNRLFENFFACLATSKFQNTIIHADFTHHHILFDKQNKTIsgVIDFGDAQIGDPAFDFAGLYYDFGH 237
Cdd:COG0510   31 LLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLY--LIDWEYAGLGDPAFDLAALLVEYGL 95
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 94-237 2.38e-06

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: 48.00  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446301146  94 IHGEPLKTEIVTT-LEKQERKALITQLATFLAALHSIPLKSVTALGFP-----IEKTLTYWKELqakLNEYVTNSLTSFQ 167
Cdd:cd05154   85 VDGRVLPDPLPRPdLSPEERRALARSLVDALAALHSVDPAALGLADLGrpegyLERQVDRWRRQ---LEAAATDPPPALE 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446301146 168 KsTLNRLFENFFACLATskfqnTIIHADFTHHHILFDKQNKtISGVIDFGDAQIGDPAFDFAGL---YYDFGH 237
Cdd:cd05154  162 E-ALRWLRANLPADGRP-----VLVHGDFRLGNLLFDPDGR-VTAVLDWELATLGDPLEDLAWLlarWWRPGD 227
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 191-239 3.50e-06

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: 47.61  E-value: 3.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446301146 191 IIHADFTHHHILFDkqNKTISGVIDFGDAQIGDPAFDFA-GLYYDFGHEF 239
Cdd:COG2334  181 VIHGDLHPDNVLFD--GDGVSGLIDFDDAGYGPRLYDLAiALNGWADGPL 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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