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Conserved domains on  [gi|1351832|sp|P08988|]
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RecName: Full=Aminoglycoside N(3)-acetyltransferase IV; AltName: Full=ACC(3)-IV; AltName: Full=Aminocyclitol 3-N-acetyltransferase type IV

Protein Classification

AAC(3) family N-acetyltransferase( domain architecture ID 10495001)

AAC(3) family N-acetyltransferase such as aminoglycoside N(3)-acetyltransferase, which catalyzes the conversion of acetyl-CoA and a 2-deoxystreptamine antibiotic to CoA and N(3)-acetyl-2-deoxystreptamine antibiotic

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Antibiotic_NAT pfam02522
Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside ...
26-228 7.67e-73

Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside 3-N-acetyltransferases EC:2.3.1.81, these catalyze the reaction: Acetyl-Co + a 2-deoxystreptamine antibiotic <=> CoA + N3'-acetyl-2-deoxystreptamine antibiotic. The enzyme can use a range of antibiotics with 2-deoxystreptamine rings as acceptor for its acetyltransferase activity, this inactivates and confers resistance to gentamicin, kanamycin, tobramycin, neomycin and apramycin amongst others.


:

Pssm-ID: 426815  Cd Length: 232  Bit Score: 222.49  E-value: 7.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     26 LVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMPSWSGLDD---------------------EPFDPATSPvTPDLGV 84
Cdd:pfam02522   1 LVHSSLSSLGWVEGGAETVIDALLDALGPEGTLVMPTHTGDSDpapwenppvpeewwdtireemPAFDPARTP-SRGMGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     85 VSDTFWRLPNVKRSAHP-FAFAAAGPQAEQIISDPLPLPPHSPASPVARVHELDGQVLLLGVGHDANTTLHLAELMAKVP 163
Cdd:pfam02522  80 LAETFRTWPGVVRSAHPtHSFAAWGPDAEEITAGHPLDTPLGEGSPLGRLYDLDGKVLLLGVGFDRNTSLHLAEYRADIP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351832    164 YG---VPRHCTILQDGKLVRVDYLENDHCCERFALADRWLKEKSLQKEGPVGHAFARLIRSRDIVATA 228
Cdd:pfam02522 160 GRryvRPGAPVIVPDGKRVWVHYEDVDLDSEDFEKLGAAFEREGVMREGKVGNATARLFSARELVDFA 227
 
Name Accession Description Interval E-value
Antibiotic_NAT pfam02522
Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside ...
26-228 7.67e-73

Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside 3-N-acetyltransferases EC:2.3.1.81, these catalyze the reaction: Acetyl-Co + a 2-deoxystreptamine antibiotic <=> CoA + N3'-acetyl-2-deoxystreptamine antibiotic. The enzyme can use a range of antibiotics with 2-deoxystreptamine rings as acceptor for its acetyltransferase activity, this inactivates and confers resistance to gentamicin, kanamycin, tobramycin, neomycin and apramycin amongst others.


Pssm-ID: 426815  Cd Length: 232  Bit Score: 222.49  E-value: 7.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     26 LVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMPSWSGLDD---------------------EPFDPATSPvTPDLGV 84
Cdd:pfam02522   1 LVHSSLSSLGWVEGGAETVIDALLDALGPEGTLVMPTHTGDSDpapwenppvpeewwdtireemPAFDPARTP-SRGMGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     85 VSDTFWRLPNVKRSAHP-FAFAAAGPQAEQIISDPLPLPPHSPASPVARVHELDGQVLLLGVGHDANTTLHLAELMAKVP 163
Cdd:pfam02522  80 LAETFRTWPGVVRSAHPtHSFAAWGPDAEEITAGHPLDTPLGEGSPLGRLYDLDGKVLLLGVGFDRNTSLHLAEYRADIP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351832    164 YG---VPRHCTILQDGKLVRVDYLENDHCCERFALADRWLKEKSLQKEGPVGHAFARLIRSRDIVATA 228
Cdd:pfam02522 160 GRryvRPGAPVIVPDGKRVWVHYEDVDLDSEDFEKLGAAFEREGVMREGKVGNATARLFSARELVDFA 227
YokD COG2746
Aminoglycoside N3'-acetyltransferase [Defense mechanisms];
7-228 2.16e-64

Aminoglycoside N3'-acetyltransferase [Defense mechanisms];


Pssm-ID: 442043  Cd Length: 256  Bit Score: 201.58  E-value: 2.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832    7 KAELIGQLLNLGVTPGGVLLVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMP-SWSGLDDE---------------- 69
Cdd:COG2746   4 RESLAADLRALGVRPGDTVLVHSSLSSLGWVCGGAQAVIEALLDVVGPEGTLVMPtQSGDNSDPatwenppvpeewweti 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832   70 -----PFDPATSPvTPDLGVVSDTFWRLPNVKRSAHPFA-FAAAGPQAEQIISD-PLpLPPHSPASPVARVHELDGQVLL 142
Cdd:COG2746  84 raempAFDPATTP-TRGMGAIPETFRTWPGVVRSDHPQAsFAAWGPDAEEITADhPL-DYGLGEGSPLARLYELDGKVLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832  143 LGVGHDANTTLHLAELMAKVPYG--VPRHCTILQDGKLVRVDYLENDHCCERF-ALADRWLKEKSLQKeGPVGHAFARLI 219
Cdd:COG2746 162 LGVGYDTNTSLHLAEYRADAPGKrtVRYGAPILEDGERVWVEFEDIDTDSDDFeEIGEAFEAEGIVRK-GKVGNADSRLF 240

                ....*....
gi 1351832  220 RSRDIVATA 228
Cdd:COG2746 241 DARDLVDFA 249
 
Name Accession Description Interval E-value
Antibiotic_NAT pfam02522
Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside ...
26-228 7.67e-73

Aminoglycoside 3-N-acetyltransferase; This family consists of bacterial aminoglycoside 3-N-acetyltransferases EC:2.3.1.81, these catalyze the reaction: Acetyl-Co + a 2-deoxystreptamine antibiotic <=> CoA + N3'-acetyl-2-deoxystreptamine antibiotic. The enzyme can use a range of antibiotics with 2-deoxystreptamine rings as acceptor for its acetyltransferase activity, this inactivates and confers resistance to gentamicin, kanamycin, tobramycin, neomycin and apramycin amongst others.


Pssm-ID: 426815  Cd Length: 232  Bit Score: 222.49  E-value: 7.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     26 LVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMPSWSGLDD---------------------EPFDPATSPvTPDLGV 84
Cdd:pfam02522   1 LVHSSLSSLGWVEGGAETVIDALLDALGPEGTLVMPTHTGDSDpapwenppvpeewwdtireemPAFDPARTP-SRGMGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832     85 VSDTFWRLPNVKRSAHP-FAFAAAGPQAEQIISDPLPLPPHSPASPVARVHELDGQVLLLGVGHDANTTLHLAELMAKVP 163
Cdd:pfam02522  80 LAETFRTWPGVVRSAHPtHSFAAWGPDAEEITAGHPLDTPLGEGSPLGRLYDLDGKVLLLGVGFDRNTSLHLAEYRADIP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351832    164 YG---VPRHCTILQDGKLVRVDYLENDHCCERFALADRWLKEKSLQKEGPVGHAFARLIRSRDIVATA 228
Cdd:pfam02522 160 GRryvRPGAPVIVPDGKRVWVHYEDVDLDSEDFEKLGAAFEREGVMREGKVGNATARLFSARELVDFA 227
YokD COG2746
Aminoglycoside N3'-acetyltransferase [Defense mechanisms];
7-228 2.16e-64

Aminoglycoside N3'-acetyltransferase [Defense mechanisms];


Pssm-ID: 442043  Cd Length: 256  Bit Score: 201.58  E-value: 2.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832    7 KAELIGQLLNLGVTPGGVLLVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMP-SWSGLDDE---------------- 69
Cdd:COG2746   4 RESLAADLRALGVRPGDTVLVHSSLSSLGWVCGGAQAVIEALLDVVGPEGTLVMPtQSGDNSDPatwenppvpeewweti 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832   70 -----PFDPATSPvTPDLGVVSDTFWRLPNVKRSAHPFA-FAAAGPQAEQIISD-PLpLPPHSPASPVARVHELDGQVLL 142
Cdd:COG2746  84 raempAFDPATTP-TRGMGAIPETFRTWPGVVRSDHPQAsFAAWGPDAEEITADhPL-DYGLGEGSPLARLYELDGKVLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351832  143 LGVGHDANTTLHLAELMAKVPYG--VPRHCTILQDGKLVRVDYLENDHCCERF-ALADRWLKEKSLQKeGPVGHAFARLI 219
Cdd:COG2746 162 LGVGYDTNTSLHLAEYRADAPGKrtVRYGAPILEDGERVWVEFEDIDTDSDDFeEIGEAFEAEGIVRK-GKVGNADSRLF 240

                ....*....
gi 1351832  220 RSRDIVATA 228
Cdd:COG2746 241 DARDLVDFA 249
 
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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