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Conserved domains on  [gi|652970167|ref|WP_027223060|]
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acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase [Legionella pneumophila]

Protein Classification

UDP-N-acetylglucosamine O-acyltransferase( domain architecture ID 11437198)

UDP-N-acetylglucosamine O-acyltransferase catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc, the first step of lipid A biosynthetic pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 22-276 5.30e-140

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


:

Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 394.00  E-value: 5.30e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:COG1043    4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:COG1043   84 DNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:COG1043  164 HAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEVR 243

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:COG1043  244 ELLDFIRASKRGIIR 258
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 22-276 5.30e-140

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 394.00  E-value: 5.30e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:COG1043    4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:COG1043   84 DNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:COG1043  164 HAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEVR 243

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:COG1043  244 ELLDFIRASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
22-276 2.65e-139

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 392.54  E-value: 2.65e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLVIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:PRK05289  85 DNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:PRK05289 165 HAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSPEVK 244

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:PRK05289 245 EILDFIESSKRGIIR 259
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 22-274 1.01e-136

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 385.63  E-value: 1.01e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:cd03351   82 DNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:cd03351  162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEVE 241

                        250
                 ....*....|...
gi 652970167 262 YILKFLQTSTRSF 274
Cdd:cd03351  242 ELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 22-272 2.76e-109

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 316.12  E-value: 2.76e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167   22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|.
gi 652970167  262 YILKFLQTSTR 272
Cdd:TIGR01852 241 EILDFIRESKR 251
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 194-272 1.23e-24

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 94.06  E-value: 1.23e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652970167  194 DVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVNYILKFLQTSTR 272
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKR 79
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 22-276 5.30e-140

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 394.00  E-value: 5.30e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:COG1043    4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRLEIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:COG1043   84 DNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:COG1043  164 HAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSPEVR 243

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:COG1043  244 ELLDFIRASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
22-276 2.65e-139

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 392.54  E-value: 2.65e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTRLVIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:PRK05289  85 DNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:PRK05289 165 HAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDSPEVK 244

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:PRK05289 245 EILDFIESSKRGIIR 259
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 22-274 1.01e-136

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 385.63  E-value: 1.01e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:cd03351   82 DNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:cd03351  162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEVE 241

                        250
                 ....*....|...
gi 652970167 262 YILKFLQTSTRSF 274
Cdd:cd03351  242 ELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 22-272 2.76e-109

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 316.12  E-value: 2.76e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167   22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  102 NNNIIREYVTINRGTAGGGGETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|.
gi 652970167  262 YILKFLQTSTR 272
Cdd:TIGR01852 241 EILDFIRESKR 251
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 22-276 2.26e-99

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 291.16  E-value: 2.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEKSTVFIG 101
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 102 NNNIIREYVTINRGTAGGGgETRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGR 181
Cdd:PRK12461  82 DRNVIREGVTIHRGTKGGG-VTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 182 MSMIGAQSKITKDVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVN 261
Cdd:PRK12461 161 LAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQQFESPEVE 240

                        250
                 ....*....|....*
gi 652970167 262 YILKFLQTSTRSFYR 276
Cdd:PRK12461 241 ELIDFIKASKRGIVR 255
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 22-205 1.75e-36

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 132.06  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIE------------------TGAIIG 83
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHpnvtiyercvigdrviihSGAVIG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  84 A---------------VPQdlkfTGeksTVFIGNN-----NiireyVTINRGTAgggGETRVGNH----NLimtsVHVAH 139
Cdd:COG1044  179 AdgfgfapdedggwvkIPQ----LG---RVVIGDDveigaN-----TTIDRGAL---GDTVIGDGtkidNL----VQIAH 239

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652970167 140 DVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGI--HqfVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:COG1044  240 NVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIagH--LTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 21-205 2.16e-36

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 128.29  E-value: 2.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLKFTGEK----- 95
Cdd:cd03352    9 SIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDGGGwvkip 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  96 --STVFIGNNNIIREYVTINRGTaggGGETRVGNH----NLimtsVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGA 169
Cdd:cd03352   89 qlGGVIIGDDVEIGANTTIDRGA---LGDTVIGDGtkidNL----VQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGG 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 652970167 170 LCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:cd03352  162 QVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 22-203 3.95e-30

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 115.62  E-value: 3.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPY------------------SIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIG 83
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNavigagvvigdgvvigagAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  84 A--------------VPQdlkfTGeksTVFIGNNNIIREYVTINRGTaggGGETRVGNH----NLimtsVHVAHDVQMGN 145
Cdd:PRK00892 183 SdgfgfandrggwvkIPQ----LG---RVIIGDDVEIGANTTIDRGA---LDDTVIGEGvkidNL----VQIAHNVVIGR 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 652970167 146 NNIIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSG 203
Cdd:PRK00892 249 HTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSS 306
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 194-272 1.23e-24

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 94.06  E-value: 1.23e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652970167  194 DVLPYTLVSGNPPKRFGINVERLRRNGYNSSQRIVIQKAYRTLFQEGQTLTDTVETLKKEFQENRDVNYILKFLQTSTR 272
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKR 79
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 96-205 8.20e-18

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 79.07  E-value: 8.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  96 STVFIGNNNIIREYVTINRGTaggggetRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQ 175
Cdd:cd03360   95 PSAVIGEGCVIMAGAVINPDA-------RIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQ 167

                         90       100       110
                 ....*....|....*....|....*....|
gi 652970167 176 FVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:cd03360  168 GVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 96-205 4.90e-17

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 77.15  E-value: 4.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167   96 STVFIGNNNIIREYVTINRGTaggggetRVGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQ 175
Cdd:TIGR03570  98 PSASIGEGTVIMAGAVINPDV-------RIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQ 170

                          90       100       110
                  ....*....|....*....|....*....|
gi 652970167  176 FVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:TIGR03570 171 GVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 34-210 5.84e-12

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 61.36  E-value: 5.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  34 IGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDnqietgaiigavpqdlkftgekstVFIGNNniireYVTIN 113
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDD------------------------VFIGPN-----VVFTN 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 114 RGTAGGGGETRVgnhNLIMTsvhvahdvqmgnnnIIANAVAIGGHVVIddwvtigaLCGihqfVQLGRMSMIGAQSKITK 193
Cdd:cd03358   52 DLYPRSKIYRKW---ELKGT--------------TVKRGASIGANATI--------LPG----VTIGEYALVGAGAVVTK 102

                        170
                 ....*....|....*..
gi 652970167 194 DVLPYTLVSGNPPKRFG 210
Cdd:cd03358  103 DVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
49-205 7.38e-11

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 58.73  E-value: 7.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  49 NVSIGQGTTIGSHVSIQGWT-KIGEDnqietgaiigavpqdlkftgekstVFIGNNNIIreyvtinrgtaGGGGETRVGN 127
Cdd:COG0110    8 GARIGDGVVIGPGVRIYGGNiTIGDN------------------------VYIGPGVTI-----------DDPGGITIGD 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 128 HnlimtsVHVAHDVQMGNNN----IIANAVAIGGHVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSG 203
Cdd:COG0110   53 N------VLIGPGVTILTGNhpidDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAG 126


                 ..
gi 652970167 204 NP 205
Cdd:COG0110  127 NP 128
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 98-207 1.72e-08

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 51.30  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  98 VFIGNNNIIREYVTINrgtagGGGETRVGNHNLIMTSVHV-AHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQF 176
Cdd:cd04647    2 ISIGDNVYIGPGCVIS-----AGGGITIGDNVLIGPNVTIyDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPG 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 652970167 177 VQLGRMSMIGAQSKITKDVLPYTLVSGNPPK 207
Cdd:cd04647   77 VTIGDGAVVGAGSVVTKDVPPNSIVAGNPAK 107
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-218 4.19e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.59  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  25 TALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGwTKIGEDNQIETGAI-----------IGAVPQDLKFTG 93
Cdd:PRK14355 262 TTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAGSVledsvvgddvaIGPMAHLRPGTE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  94 EKSTVFIGNnniireYVTINRGTAGGGGEtrvGNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGH-VVIDDWVTIGALCG 172
Cdd:PRK14355 341 LSAHVKIGN------FVETKKIVMGEGSK---ASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHrTVIEDDVFVGSDVQ 411

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 652970167 173 IHQFVQLGRMSMIGAQSKITKDVLPYTLVSGNPPKrfgINVE--RLRR 218
Cdd:PRK14355 412 FVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQ---VNKEgwKLRK 456
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 21-175 8.76e-08

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 50.79  E-value: 8.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPYAKIGPNVSIGPYSIIGDNVSIgqgttigshvsiqgwtkigednQIETGAIIgavpqdlkftgekstvfI 100
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATI----------------------IAEAGPII-----------------I 41

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652970167 101 GNNNIIREYVTINRGTAGGGGETRV---GNHNLIMTSVHVaHDVQMGNNNIIANAVAIGGHVVIDDWVTIGALCGIHQ 175
Cdd:cd04646   42 GENNIIEEQVTIVNKKPKDPAEPKPmiiGSNNVFEVGCKC-EALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPS 118
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 22-200 2.12e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 51.69  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPY-----SIIGDNVSIgqgttIGSHVsiqgwtkigEDNQIETGAIIGAVPQDLKFTGEKS 96
Cdd:PRK14357 264 IYPMTFIEGKTRIGEDCEIGPMtrivdCEIGNNVKI-----IRSEC---------EKSVIEDDVSVGPFSRLREGTVLKK 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  97 TVFIGNnniireYVTINRGTAGGGGETRvgnHNLIMTSVHVAHDVQMGNNNIIANAVAIGGH-VVIDDWVTIGALCGIHQ 175
Cdd:PRK14357 330 SVKIGN------FVEIKKSTIGENTKAQ---HLTYLGDATVGKNVNIGAGTITCNYDGKKKNpTFIEDGAFIGSNSSLVA 400

                        170       180
                 ....*....|....*....|....*
gi 652970167 176 FVQLGRMSMIGAQSKITKDVLPYTL 200
Cdd:PRK14357 401 PVRIGKGALIGAGSVITEDVPPYSL 425
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 22-82 2.84e-07

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 49.80  E-value: 2.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652970167   22 IHPTALISPYA------------------KIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAII 82
Cdd:TIGR03570  90 IHPSAIVSPSAsigegtvimagavinpdvRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATI 168
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 22-82 4.84e-07

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 49.02  E-value: 4.84e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAII 82
Cdd:cd03360  105 IMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATI 165
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 28-85 1.46e-06

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 45.89  E-value: 1.46e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652970167  28 ISPYAKIGPN--------VSIGPYSIIGDNVSIGQGTTIGSHVSIQGWT--KIGEDNQIETGA-IIGAV 85
Cdd:cd03354    5 IHPGAKIGPGlfidhgtgIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRhpTIGDNVVIGAGAkILGNI 73
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 22-83 7.64e-06

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 43.30  E-value: 7.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQ-----GTTIGSHV----SIQGW-TKIGEDNQIETGAIIG 83
Cdd:cd05824    2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRcvilsNSTVRDHSwvksSIVGWnSTVGRWTRLENVTVLG 73
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 93-209 1.05e-05

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 44.46  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  93 GEKSTVFIGNNNIIREYVTINRGTAGGGGETRV--GNHNLIMTSVHVAHDVQMGNNN-------------IIANAVAIGG 157
Cdd:cd03349    5 GDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGlgGNHPTDWVSTYPFYIFGGEWEDdakfddwpskgdvIIGNDVWIGH 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 652970167 158 HVVIDDWVTIGAlcgihqfvqlGrmSMIGAQSKITKDVLPYTLVSGNPPK----RF 209
Cdd:cd03349   85 GATILPGVTIGD----------G--AVIAAGAVVTKDVPPYAIVGGNPAKviryRF 128
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 26-113 1.36e-05

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 42.24  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  26 ALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGS--HVSIQGWTKIGEDNQIETGAIIGAvpqdlkftgeksTVFIGNN 103
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatGPNEKNPTIIGDNVEIGANAVIHG------------GVKIGDN 68

                         90
                 ....*....|
gi 652970167 104 NIIREYVTIN 113
Cdd:cd00208   69 AVIGAGAVVT 78
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 97-205 1.36e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 44.99  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  97 TVFIGNNNIIREYVTINrgTAGgggetRVGNHNLIMTSVHVAHDVQMGNNniianaVAIGGHVVIDDWVTIGalcgihqf 176
Cdd:PRK09527  95 TVTIGDNVLIAPNVTLS--VTG-----HPVHHELRKNGEMYSFPITIGNN------VWIGSHVVINPGVTIG-------- 153

                         90       100
                 ....*....|....*....|....*....
gi 652970167 177 vqlgRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:PRK09527 154 ----DNSVIGAGSVVTKDIPPNVVAAGVP 178
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 25-201 1.64e-05

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 44.33  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  25 TALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGwTKIGEDNQIETGAIIgavpqdlkftgEKSTvfIGNNN 104
Cdd:cd03353    9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKASSVI-----------EGAV--IGNGA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 105 IIREYVTINRGTAGGGGeTRVGNHNLIMTS-----VHVAH-----DVQMGNN------NIIANAVAIGGH-VVIDDWVTI 167
Cdd:cd03353   75 TVGPFAHLRPGTVLGEG-VHIGNFVEIKKStigegSKANHlsylgDAEIGEGvnigagTITCNYDGVNKHrTVIGDNVFI 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 652970167 168 GALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLV 201
Cdd:cd03353  154 GSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 21-121 3.27e-05

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAV--PQDLKFTGEKSTV 98
Cdd:cd03350    3 RVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVlePLQATPVIIEDDV 82

                         90       100
                 ....*....|....*....|...
gi 652970167  99 FIGNNNIIREYVTINRGTAGGGG 121
Cdd:cd03350   83 FIGANCEVVEGVIVGKGAVLAAG 105
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 22-107 3.45e-05

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 43.38  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  22 IHPTALISPYAKIGPNVSIGPYSII-GDNvsiGQGTTIGSHVSIQ----------GWTKIGEDNQIETGAIIG--AVPQD 88
Cdd:cd00710   11 VHPTAVVIGDVIIGDNVFVGPGASIrADE---GTPIIIGANVNIQdgvvihalegYSVWIGKNVSIAHGAIVHgpAYIGD 87

                         90       100
                 ....*....|....*....|..
gi 652970167  89 LKFTGEKSTVF---IGNNNIIR 107
Cdd:cd00710   88 NCFIGFRSVVFnakVGDNCVIG 109
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 159-205 4.08e-05

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 41.82  E-value: 4.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 652970167 159 VVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:cd05825   57 IVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNP 103
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 21-83 5.03e-05

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.18  E-value: 5.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 652970167  21 TIHPTALISPYAKIGPNVSIGPYSIIGDnvsigqgTTIGSHVSIQGWTkIGEDNQIETGAIIG 83
Cdd:cd03353   23 VIDPGVILEGKTVIGEDCVIGPNCVIKD-------STIGDGVVIKASS-VIEGAVIGNGATVG 77
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 21-106 7.63e-05

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 42.01  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPYA------KIGPNVSIGPYS---------IIGDNVSIGQGTTIgsHVSIQGWTKIGEDNQIETGAII-GA 84
Cdd:cd04645    1 EIDPSAFIAPNAtvigdvTLGEGSSVWFGAvlrgdvnpiRIGERTNIQDGSVL--HVDPGYPTIIGDNVTVGHGAVLhGC 78

                         90       100
                 ....*....|....*....|....*.
gi 652970167  85 VPQDLKFTGEKSTVF----IGNNNII 106
Cdd:cd04645   79 TIGDNCLIGMGAIILdgavIGKGSIV 104
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 21-208 7.66e-05

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.32  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPYA------KIGPNVSIGPY-SIIGDNVSIgqgtTIGSHVSIQgwtkigeDNqietgAIIgavpqdlkFTG 93
Cdd:COG0663   12 QIHPSAFVAPTAvvigdvTIGEDVSVWPGaVLRGDVGPI----RIGEGSNIQ-------DG-----VVL--------HVD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  94 EKSTVFIGNNniireyVTInrGtaggggetrvgnHNLImtsVHVAHdvqmgnnniIANAVAIGGHVVIDDWVTIGALCgi 173
Cdd:COG0663   68 PGYPLTIGDD------VTI--G------------HGAI---LHGCT---------IGDNVLIGMGAIVLDGAVIGDGS-- 113

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 652970167 174 hqfvqlgrmsMIGAQSKIT--KDVLPYTLVSGNPPKR 208
Cdd:COG0663  114 ----------IVGAGALVTegKVVPPGSLVVGSPAKV 140
PLN02694 PLN02694
serine O-acetyltransferase
 133-210 8.42e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.09  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 133 TSVHVAHDVQMGNNNIIANAVAIGG--------HVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGN 204
Cdd:PLN02694 179 TGVVIGETAVIGNNVSILHHVTLGGtgkacgdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGN 258


                 ....*.
gi 652970167 205 PPKRFG 210
Cdd:PLN02694 259 PARLVG 264
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 28-84 1.33e-04

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 41.61  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 652970167  28 ISPYAKIGPN--------VSIGPYSIIGDNVSIGQGTTIGSHvsiqGWTKIGEDNQIETGAIIGA 84
Cdd:COG1045   68 IHPGATIGRGffidhgtgVVIGETAVIGDNVTIYQGVTLGGT----GKEKGKRHPTIGDNVVIGA 128
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 39-151 1.36e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.42  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  39 SIGPYSIIGDNVSIGQGTTIGSHVSIQGWTKIGEDNQIETGAII-GAVpqdlkFTGEKstVFIGNNNIIREYVTINrgta 117
Cdd:cd05636    7 TVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIrGYT-----VLGDG--CVVGNSVEVKNSIIMD---- 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 652970167 118 ggggETRVGNHNLIMTSVhVAHDVQMGNNNIIAN 151
Cdd:cd05636   76 ----GTKVPHLNYVGDSV-LGENVNLGAGTITAN 104
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
32-60 1.71e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.09  E-value: 1.71e-04
                          10        20
                  ....*....|....*....|....*....
gi 652970167   32 AKIGPNVSIGPYSIIGDNVSIGQGTTIGS 60
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PLN02739 PLN02739
serine acetyltransferase
 133-215 1.90e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 42.33  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 133 TSVHVAHDVQMGNNNIIANAVAIGG--------HVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGN 204
Cdd:PLN02739 224 TGVVIGETAVIGDRVSILHGVTLGGtgketgdrHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303

                         90
                 ....*....|.
gi 652970167 205 PPKRFGINVER 215
Cdd:PLN02739 304 PAKLIGFVDEQ 314
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 149-205 1.93e-04

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 40.87  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 652970167 149 IANAVAIGGHVVIDDWVTIGalcgihqfvqlgRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:cd03357  121 IGDNVWIGGGVIILPGVTIG------------DNSVIGAGSVVTKDIPANVVAAGNP 165
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 28-84 2.11e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 42.32  E-value: 2.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 652970167  28 ISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGwTKIGEDNQIE----TGAIIGA 84
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVIKysviEDAVVGA 322
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 21-123 2.80e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.02  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  21 TIHPTALISPY-----AKIGPNVSIGPY------------SIIGDNVSIgQGTTIGSHVSIQGWTKIGeDNQIETGAIIG 83
Cdd:PRK14356 306 VVSSGATIHSFshlegAEVGDGCSVGPYarlrpgavleegARVGNFVEM-KKAVLGKGAKANHLTYLG-DAEIGAGANIG 383

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 652970167  84 A---------VPQDLKFTGEKstVFIGNNNIIREYVTINRGTAGGGGET 123
Cdd:PRK14356 384 AgtitcnydgVNKHRTVIGEG--AFIGSNTALVAPVTIGDGALVGAGSV 430
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-200 4.44e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  25 TALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGSHVSIQGwTKIGEDNQIETGAIIGAVpqdlkfTGEKSTV------ 98
Cdd:PRK14354 259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVD-STIGDGVTITNSVIEESK------VGDNVTVgpfahl 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  99 ----FIGNNNIIREYVTINRGTAGGGgeTRVGnHNLIMTSVHVAHDVQMGNNNIIANAVAIGGH-VVIDDWVTIGALCGI 173
Cdd:PRK14354 332 rpgsVIGEEVKIGNFVEIKKSTIGEG--TKVS-HLTYIGDAEVGENVNIGCGTITVNYDGKNKFkTIIGDNAFIGCNSNL 408

                        170       180
                 ....*....|....*....|....*..
gi 652970167 174 HQFVQLGRMSMIGAQSKITKDVLPYTL 200
Cdd:PRK14354 409 VAPVTVGDNAYIAAGSTITKDVPEDAL 435
PLN02357 PLN02357
serine acetyltransferase
 133-210 4.51e-04

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 41.02  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 133 TSVHVAHDVQMGNNNIIANAVAIGG--------HVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGN 204
Cdd:PLN02357 245 TGVVIGETAVVGNNVSILHNVTLGGtgkqsgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGN 324


                 ....*.
gi 652970167 205 PPKRFG 210
Cdd:PLN02357 325 PARLIG 330
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 27-83 6.04e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.61  E-value: 6.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 652970167  27 LISPYAKIGPNVSIGPySIIGDNVSIGQGTT-----------IGSHVSIQ----GW-TKIGEDNQIETGAIIG 83
Cdd:cd03356    1 LIGESTVIGENAIIKN-SVIGDNVRIGDGVTitnsilmdnvtIGANSVIVdsiiGDnAVIGENVRVVNLCIIG 72
PRK10502 PRK10502
putative acyl transferase; Provisional
 155-205 1.09e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.16  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 652970167 155 IGGHVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGNP 205
Cdd:PRK10502 121 NTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNP 171
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 21-83 1.31e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 36.84  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 652970167  21 TIHPTALISPYAKIGPNVSIGPYSIIGDN--------VSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIG 83
Cdd:cd00208    8 KIHPKAVIRGPVVIGDNVNIGPGAVIGAAtgpneknpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 50-156 1.68e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 36.46  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  50 VSIGQGTTIGSHVSIQGWTKIGEDNQIETGAIIGAVPQDLkftgEKSTVFIGNNNIIREYVTINRGtaggggetrvgnhn 129
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN----EKNPTIIGDNVEIGANAVIHGG-------------- 62

                         90       100
                 ....*....|....*....|....*..
gi 652970167 130 limtsvhvahdVQMGNNNIIANAVAIG 156
Cdd:cd00208   63 -----------VKIGDNAVIGAGAVVT 78
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 19-195 1.80e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.53  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  19 SHTIHPTALISPYAKIGPNVSIGPYSIIGDNVSIGQGT-----TIGSHVSIQGWTKIgeDNQIETGAIIGAvpqdlkFTG 93
Cdd:PRK14360 256 SCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSliensQIGENVTVLYSVVS--DSQIGDGVKIGP------YAH 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167  94 EKSTVFIGNNNIIREYVTINRGTAGGGgeTRVgNHNLIMTSVHVAHDVQMGNNNIIANAVAIGGH-VVIDDWVTIGALCG 172
Cdd:PRK14360 328 LRPEAQIGSNCRIGNFVEIKKSQLGEG--SKV-NHLSYIGDATLGEQVNIGAGTITANYDGVKKHrTVIGDRSKTGANSV 404

                        170       180
                 ....*....|....*....|...
gi 652970167 173 IHQFVQLGRMSMIGAQSKITKDV 195
Cdd:PRK14360 405 LVAPITLGEDVTVAAGSTITKDV 427
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 133-205 1.84e-03

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 37.03  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167 133 TSVHVAHDVQMGNNNIIANAVAIGG--------HVVIDDWVTIGALCGIHQFVQLGRMSMIGAQSKITKDVLPYTLVSGN 204
Cdd:cd03354   21 TGIVIGETAVIGDNCTIYQGVTLGGkgkgggkrHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGV 100


                 .
gi 652970167 205 P 205
Cdd:cd03354  101 P 101
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 32-121 6.41e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.81  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652970167   32 AKIGPNVSIGPYSI-IGDNVSIGQGTTIGSHVSIQGWTkiGEDNQIETGaiigavpqdlkftgeksTVFIGNNNIIREYV 110
Cdd:TIGR02353 113 AKIGKGVDIGSLPPvCTDLLTIGAGTIVRKEVMLLGYR--AERGRLHTG-----------------PVTLGRDAFIGTRS 173

                          90
                  ....*....|.
gi 652970167  111 TINRGTAGGGG 121
Cdd:TIGR02353 174 TLDIDTSIGDG 184
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 34-84 6.81e-03

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 36.24  E-value: 6.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 652970167  34 IGPNVSIGPYSI-----IGDNVSIGQGTTIGSHVsiqgwtkigednQIETGAIIGA 84
Cdd:cd04645   63 IGDNVTVGHGAVlhgctIGDNCLIGMGAIILDGA------------VIGKGSIVAA 106
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 26-82 7.72e-03

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 36.41  E-value: 7.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 652970167  26 ALISPYAKIGPNVSIGPYSIIGDNVSIGQGTTIGS----------HVSIQGWTKIGEDNQIETGAII 82
Cdd:cd05636   36 VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNsiimdgtkvpHLNYVGDSVLGENVNLGAGTIT 102
 
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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