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Conserved domains on  [gi|504696543|ref|WP_014883645|]
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MULTISPECIES: type A chloramphenicol O-acetyltransferase [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
2-oxoacid_dh super family cl02008
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
1-214 4.48e-128

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


The actual alignment was detected with superfamily member PRK13757:

Pssm-ID: 445639  Cd Length: 219  Bit Score: 360.33  E-value: 4.48e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   1 MEKIIPEYTAVNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDN 80
Cdd:PRK13757   1 MEKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFYPAFIHILARLMNAHPEFRMAMKDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543  81 ELVIWNEIHPNYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKeESRENIFFISGIPWVSFTSFSVS 160
Cdd:PRK13757  81 ELVIWDSVHPCYTVFHEQTETFSSLWSEYHDDFRQFLHIYSQDVACYGENLAYFPK-GFIENMFFVSANPWVSFTSFDLN 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504696543 161 VANMKNFFAPMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQEVCD 214
Cdd:PRK13757 160 VANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLNELQQYCD 213
 
Name Accession Description Interval E-value
PRK13757 PRK13757
type A chloramphenicol O-acetyltransferase;
1-214 4.48e-128

type A chloramphenicol O-acetyltransferase;


Pssm-ID: 172295  Cd Length: 219  Bit Score: 360.33  E-value: 4.48e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   1 MEKIIPEYTAVNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDN 80
Cdd:PRK13757   1 MEKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFYPAFIHILARLMNAHPEFRMAMKDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543  81 ELVIWNEIHPNYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKeESRENIFFISGIPWVSFTSFSVS 160
Cdd:PRK13757  81 ELVIWDSVHPCYTVFHEQTETFSSLWSEYHDDFRQFLHIYSQDVACYGENLAYFPK-GFIENMFFVSANPWVSFTSFDLN 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504696543 161 VANMKNFFAPMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQEVCD 214
Cdd:PRK13757 160 VANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLNELQQYCD 213
CatA COG4845
Chloramphenicol O-acetyltransferase [Defense mechanisms];
7-215 1.53e-102

Chloramphenicol O-acetyltransferase [Defense mechanisms];


Pssm-ID: 443873  Cd Length: 210  Bit Score: 295.21  E-value: 1.53e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   7 EYTAVNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWN 86
Cdd:COG4845    2 MYKPIDLETWPRKEHFEFFRNFDPPTFSITVELDVTALYKYAKKNGLSFFPAYLYAILKAVNEIPEFRYRIEDGEVVEYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543  87 EIHPNYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESRENIFFISGIPWVSFTSFSVSVANMKN 166
Cdd:COG4845   82 VIHPSFTIFHKEDETFSFVWIPYDEDFETFYANYLEDIERYKNSTGLFPKEGNPDNLFYISCLPWLSFTSFSHAIPGNPD 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504696543 167 FFAPMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQEVCDA 215
Cdd:COG4845  162 DSIPIITFGKYYEENGRLLMPVSIQVHHALVDGYHVGRFLEELQELLDE 210
CAT pfam00302
Chloramphenicol acetyltransferase;
11-210 1.25e-97

Chloramphenicol acetyltransferase;


Pssm-ID: 425592  Cd Length: 201  Bit Score: 282.78  E-value: 1.25e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   11 VNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWNEIHP 90
Cdd:pfam00302   2 IDLETWHRKEHFEHYRNVVQCTYSMTVELDITAFLKEIKKKKYKFYPAQIYALARVVNKHPEFRMAMKDGELGYWDSVHP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   91 NYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESRENIFFISGIPWVSFTSFSVSVANMKNFFAP 170
Cdd:pfam00302  82 SYTVFNKETETFSSIWTEYDPDFRQFYHIYSADLAEYGENTKFFPKGNFPENMFPVSSLPWVSFTSFNLNVANNDDYLAP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 504696543  171 MFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQ 210
Cdd:pfam00302 162 IFTMGKYYTEGDKILLPVAIQVHHAVCDGFHAGRFINELQ 201
CAT smart01059
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the ...
11-210 4.35e-96

Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.


Pssm-ID: 215002  Cd Length: 202  Bit Score: 278.71  E-value: 4.35e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543    11 VNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWNEIHP 90
Cdd:smart01059   2 IDIENWNRKEHFEFFRNFDNPTFSITVNIDITNLLKYIKENKYSFFPAYLYAVLKAVNEIPEFRMRIDDGKLVEWDSVHP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543    91 NYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESREN-IFFISGIPWVSFTSFSVSVANMKNFFA 169
Cdd:smart01059  82 SYTIFHKEDETFSFIWTPYDEDFKDFYQNALADIERYKNNPGLFPKENIPRNdLFYISAIPWVSFTSITHNISNGRNDSI 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 504696543   170 PMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQ 210
Cdd:smart01059 162 PIITWGKYFKQEGKLLLPVSIQVHHAVVDGYHVGRFINKLQ 202
 
Name Accession Description Interval E-value
PRK13757 PRK13757
type A chloramphenicol O-acetyltransferase;
1-214 4.48e-128

type A chloramphenicol O-acetyltransferase;


Pssm-ID: 172295  Cd Length: 219  Bit Score: 360.33  E-value: 4.48e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   1 MEKIIPEYTAVNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDN 80
Cdd:PRK13757   1 MEKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFYPAFIHILARLMNAHPEFRMAMKDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543  81 ELVIWNEIHPNYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKeESRENIFFISGIPWVSFTSFSVS 160
Cdd:PRK13757  81 ELVIWDSVHPCYTVFHEQTETFSSLWSEYHDDFRQFLHIYSQDVACYGENLAYFPK-GFIENMFFVSANPWVSFTSFDLN 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504696543 161 VANMKNFFAPMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQEVCD 214
Cdd:PRK13757 160 VANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLNELQQYCD 213
CatA COG4845
Chloramphenicol O-acetyltransferase [Defense mechanisms];
7-215 1.53e-102

Chloramphenicol O-acetyltransferase [Defense mechanisms];


Pssm-ID: 443873  Cd Length: 210  Bit Score: 295.21  E-value: 1.53e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   7 EYTAVNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWN 86
Cdd:COG4845    2 MYKPIDLETWPRKEHFEFFRNFDPPTFSITVELDVTALYKYAKKNGLSFFPAYLYAILKAVNEIPEFRYRIEDGEVVEYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543  87 EIHPNYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESRENIFFISGIPWVSFTSFSVSVANMKN 166
Cdd:COG4845   82 VIHPSFTIFHKEDETFSFVWIPYDEDFETFYANYLEDIERYKNSTGLFPKEGNPDNLFYISCLPWLSFTSFSHAIPGNPD 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504696543 167 FFAPMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQEVCDA 215
Cdd:COG4845  162 DSIPIITFGKYYEENGRLLMPVSIQVHHALVDGYHVGRFLEELQELLDE 210
CAT pfam00302
Chloramphenicol acetyltransferase;
11-210 1.25e-97

Chloramphenicol acetyltransferase;


Pssm-ID: 425592  Cd Length: 201  Bit Score: 282.78  E-value: 1.25e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   11 VNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWNEIHP 90
Cdd:pfam00302   2 IDLETWHRKEHFEHYRNVVQCTYSMTVELDITAFLKEIKKKKYKFYPAQIYALARVVNKHPEFRMAMKDGELGYWDSVHP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543   91 NYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESRENIFFISGIPWVSFTSFSVSVANMKNFFAP 170
Cdd:pfam00302  82 SYTVFNKETETFSSIWTEYDPDFRQFYHIYSADLAEYGENTKFFPKGNFPENMFPVSSLPWVSFTSFNLNVANNDDYLAP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 504696543  171 MFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQ 210
Cdd:pfam00302 162 IFTMGKYYTEGDKILLPVAIQVHHAVCDGFHAGRFINELQ 201
CAT smart01059
Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the ...
11-210 4.35e-96

Chloramphenicol acetyltransferase; Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.


Pssm-ID: 215002  Cd Length: 202  Bit Score: 278.71  E-value: 4.35e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543    11 VNLSRWARKEHFEVFQGFAQSTFNQTVLVDITVLLSHIKNVGWKFYPTIIFLVAKIVNRHPEFRMAMKDNELVIWNEIHP 90
Cdd:smart01059   2 IDIENWNRKEHFEFFRNFDNPTFSITVNIDITNLLKYIKENKYSFFPAYLYAVLKAVNEIPEFRMRIDDGKLVEWDSVHP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696543    91 NYTIFHNETETFSSLWSHYDGDIQHFQKTYSEDMARYGDKLAYWPKEESREN-IFFISGIPWVSFTSFSVSVANMKNFFA 169
Cdd:smart01059  82 SYTIFHKEDETFSFIWTPYDEDFKDFYQNALADIERYKNNPGLFPKENIPRNdLFYISAIPWVSFTSITHNISNGRNDSI 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 504696543   170 PMFTLGKYYEQEGRVLLPLAVQVHHSVCDGFHVARFFNELQ 210
Cdd:smart01059 162 PIITWGKYFKQEGKLLLPVSIQVHHAVVDGYHVGRFINKLQ 202
 
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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