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Conserved domains on  [gi|1655140282|ref|WP_137624810|]
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2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Lactiplantibacillus pingfangensis]

Protein Classification

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase( domain architecture ID 11497020)

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 6-237 3.05e-136

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


:

Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 382.18  E-value: 3.05e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282   6 AQSIINYIGNSKKKTPVKVFVKGQLDQItDVPASIKTFFSGNAGVLFGDWADVEPFLTANAAKIEDSEIENNARNSAVPM 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQV-DFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:TIGR03532  80 LDLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTKSKTELMSELRNL 237
Cdd:TIGR03532 160 PVVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 6-237 3.05e-136

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 382.18  E-value: 3.05e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282   6 AQSIINYIGNSKKKTPVKVFVKGQLDQItDVPASIKTFFSGNAGVLFGDWADVEPFLTANAAKIEDSEIENNARNSAVPM 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQV-DFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:TIGR03532  80 LDLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTKSKTELMSELRNL 237
Cdd:TIGR03532 160 PVVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-215 1.20e-47

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: 154.08  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDD 171
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140282 172 DVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTVVGG-VPAR 215
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLtqstpIYDRETGEIYYGrVPPG 130
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-87 7.07e-41

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 134.60  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282   5 DAQSIINYIGNSKKKTPVKVFVKGQLDQITDVPASIKTFFSGNAGVLFGDWADVEPFLTANAAKIEDSEIENNARNSAVP 84
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEFEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 1655140282  85 MAD 87
Cdd:pfam08503  81 LLD 83
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 86-235 1.66e-36

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 129.54  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNaVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:PRK11830   97 ARFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQAN 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTV-VGGVPARK---------------------LK 218
Cdd:PRK11830  176 PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLgqstkIYDRETGEVhYGRVPAGSvvvpgslpskdggyslycaviVK 255

                         170
                  ....*....|....*..
gi 1655140282 219 DIDDKTKSKTELMSELR 235
Cdd:PRK11830  256 KVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 86-236 2.75e-34

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 123.69  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNaVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:COG2171    91 DYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQAA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTV-VGGVPARK---------------------LK 218
Cdd:COG2171   170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLtastkIYDRVTGEVyYGRVPAGSvvvpgslpgkdgdyglycaviVK 249

                         170
                  ....*....|....*...
gi 1655140282 219 DIDDKTKSKTELMSELRN 236
Cdd:COG2171   250 RRDEKTRSKTSLNELLRD 267
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 6-237 3.05e-136

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 382.18  E-value: 3.05e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282   6 AQSIINYIGNSKKKTPVKVFVKGQLDQItDVPASIKTFFSGNAGVLFGDWADVEPFLTANAAKIEDSEIENNARNSAVPM 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQV-DFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:TIGR03532  80 LDLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTKSKTELMSELRNL 237
Cdd:TIGR03532 160 PVVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-215 1.20e-47

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: 154.08  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDD 171
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140282 172 DVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTVVGG-VPAR 215
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLtqstpIYDRETGEIYYGrVPPG 130
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-87 7.07e-41

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 134.60  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282   5 DAQSIINYIGNSKKKTPVKVFVKGQLDQITDVPASIKTFFSGNAGVLFGDWADVEPFLTANAAKIEDSEIENNARNSAVP 84
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEFEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 1655140282  85 MAD 87
Cdd:pfam08503  81 LLD 83
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 86-235 1.66e-36

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 129.54  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNaVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:PRK11830   97 ARFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQAN 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTV-VGGVPARK---------------------LK 218
Cdd:PRK11830  176 PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLgqstkIYDRETGEVhYGRVPAGSvvvpgslpskdggyslycaviVK 255

                         170
                  ....*....|....*..
gi 1655140282 219 DIDDKTKSKTELMSELR 235
Cdd:PRK11830  256 KVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 86-236 2.75e-34

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 123.69  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  86 ADLKQYNARIEPGVAIRDQVLIGDNaVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAK 165
Cdd:COG2171    91 DYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQAA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV-----INDVEPNTV-VGGVPARK---------------------LK 218
Cdd:COG2171   170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLtastkIYDRVTGEVyYGRVPAGSvvvpgslpgkdgdyglycaviVK 249

                         170
                  ....*....|....*...
gi 1655140282 219 DIDDKTKSKTELMSELRN 236
Cdd:COG2171   250 RRDEKTRSKTSLNELLRD 267
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
107-225 3.73e-31

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 111.89  E-value: 3.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 107 IGDNAVIMMGAVINIG-AEIGEGSMIDMGAIL--GGRAIVGKNCHIGAGTVLAGV--------VEPPSAKPVQIDDDVLI 175
Cdd:COG0110    11 IGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVTIGDDVWI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1655140282 176 GANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTK 225
Cdd:COG0110    91 GAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 95-213 1.12e-28

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: 107.19  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  95 IEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGvveppsakPVQIDDDVL 174
Cdd:cd03360    87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1655140282 175 IGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVP 213
Cdd:cd03360   159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-214 1.99e-28

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: 106.42  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  95 IEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEppsakpvqIDDDVL 174
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVV--------IGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1655140282 175 IGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPA 214
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 119-223 1.70e-23

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: 92.84  E-value: 1.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 119 INIGAEIGEGSMID--MGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:COG1045    68 IHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGAN 147

                          90       100
                  ....*....|....*....|....*..
gi 1655140282 197 AIVINDVEPNTVVGGVPARKLKDIDDK 223
Cdd:COG1045   148 SVVLKDVPPGSTVVGVPARIVKRKGSK 174
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 124-217 6.19e-23

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: 89.44  E-value: 6.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 124 EIGEGSMIDMGAILGGRA--IVGKNCHIGAGTVLAGV-----------VEPPSAKPVQIDDDVLIGANAVVLEGVHVGKG 190
Cdd:cd04647     3 SIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVTIYDHnhdiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                          90       100
                  ....*....|....*....|....*..
gi 1655140282 191 AVVAAGAIVINDVEPNTVVGGVPARKL 217
Cdd:cd04647    83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 107-218 3.21e-22

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: 87.94  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 107 IGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSA-------KPVQIDDDVLIGANA 179
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKiyrkwelKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1655140282 180 VVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLK 218
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 92-223 3.86e-22

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: 88.62  E-value: 3.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVI-----NIgaEIGEGSMIDMGAIL----GGRAIVGKNCHIGAGTVLAGVVepp 162
Cdd:cd04645     5 SAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCT--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655140282 163 sakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVIND--VEPNTVVGGVPARKLKDIDDK 223
Cdd:cd04645    80 ------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDE 136
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 88-215 2.24e-21

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: 87.09  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  88 LKQYNARIEPGVAIRDQVL------IGDNAVIM------MGAviNIgaEIGEGSMIDMGAIL--GGRAIVGKNCHIGAGT 153
Cdd:cd03357    20 LHEYNQTPPSDAEERRELLkelfgsVGENVYIEppfhcdYGY--NI--HIGDNFYANFNCTIldVAPVTIGDNVLIGPNV 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140282 154 VLAGV---VEPPS-------AKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPAR 215
Cdd:cd03357    96 QIYTAghpLDPEErnrgleyAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPAR 167
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 124-218 3.20e-21

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: 86.06  E-value: 3.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 124 EIGEGSMID--MGAILGGRAIVGKNCHIGAGTVL--------------------------AGVVEPPSAKPVQIDDDVLI 175
Cdd:cd03349     3 SVGDYSYGSgpDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypfyifggeweddAKFDDWPSKGDVIIGNDVWI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1655140282 176 GANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLK 218
Cdd:cd03349    83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 92-223 5.79e-21

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 85.85  E-value: 5.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVIN-----IgaEIGEGSMIDMGAIL----GGRAIVGKNCHIGAGTVLAGVVepp 162
Cdd:COG0663    16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGCT--- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655140282 163 sakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVIND--VEPNTVVGGVPARKLKDIDDK 223
Cdd:COG0663    91 ------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEE 147
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 116-213 2.31e-20

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: 82.49  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 116 GAVINIGAEIGEGSMID--MGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVV 193
Cdd:cd03354     2 GIDIHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                          90       100
                  ....*....|....*....|
gi 1655140282 194 AAGAIVINDVEPNTVVGGVP 213
Cdd:cd03354    82 GANAVVTKDVPANSTVVGVP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 92-219 1.46e-17

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: 77.83  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVI------------------NIGA-------EIGEGSMIDMGAIlgGRAIVGK- 145
Cdd:cd03352    43 DCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgggwvkipQLGGviigddvEIGANTTIDRGAL--GDTVIGDg 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 146 -----------NCHIGAGTVLAGVVEppSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPA 214
Cdd:cd03352   121 tkidnlvqiahNVRIGENCLIAAQVG--IAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPA 198


                  ....*
gi 1655140282 215 RKLKD 219
Cdd:cd03352   199 QPHRE 203
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 92-219 1.06e-16

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: 77.75  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVIniGA----------------------------EIGEGSMIDMGAIlgGRAIV 143
Cdd:COG1044   150 DCVLHPNVTIYERCVIGDRVIIHSGAVI--GAdgfgfapdedggwvkipqlgrvvigddvEIGANTTIDRGAL--GDTVI 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 144 GK------------NCHIGAGTVLA---GVveppsAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTV 208
Cdd:COG1044   226 GDgtkidnlvqiahNVRIGEHTAIAaqvGI-----AGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGV 300

                         170
                  ....*....|.
gi 1655140282 209 VGGVPARKLKD 219
Cdd:COG1044   301 YSGSPAQPHRE 311
PLN02739 PLN02739
serine acetyltransferase
 114-228 7.54e-15

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 72.76  E-value: 7.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 114 MMGAVINIGAEIGEGSMID--MGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGA 191
Cdd:PLN02739  203 VFGIDIHPAARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGA 282

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1655140282 192 VVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTKSKT 228
Cdd:PLN02739  283 MVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLT 319
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 125-217 8.32e-15

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: 68.02  E-value: 8.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 125 IGEGSMID-MGAI-LGGRAIVGKNCHIGAGT-----VLAGVVeppsAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGA 197
Cdd:cd05825    12 IGEGVWIYnLAPVtIGSDACISQGAYLCTGShdyrsPAFPLI----TAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARS 87

                          90       100
                  ....*....|....*....|
gi 1655140282 198 IVINDVEPNTVVGGVPARKL 217
Cdd:cd05825    88 VVVRDLPAWTVYAGNPAVPV 107
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 143-218 9.92e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 69.84  E-value: 9.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 143 VGKNCHIGAGTVLAGVVEPPSA----------KPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGV 212
Cdd:PRK10092   96 IGDNCMLAPGVHIYTATHPLDPvarnsgaelgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGN 175


                  ....*.
gi 1655140282 213 PARKLK 218
Cdd:PRK10092  176 PARIIK 181
PLN02694 PLN02694
serine O-acetyltransferase
 119-233 2.62e-14

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 70.44  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 119 INIGAEIGEGSMID--MGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:PLN02694  163 IHPAAKIGKGILFDhaTGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAG 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1655140282 197 AIVINDVEPNTVVGGVPAR---------KLKDIDDKTKSKTELMSE 233
Cdd:PLN02694  243 SVVLIDVPPRTTAVGNPARlvggkekpaKHEECPGESMDHTSFISE 288
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 123-199 5.42e-14

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: 64.96  E-value: 5.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140282 123 AEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV 199
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
PRK10502 PRK10502
putative acyl transferase; Provisional
 88-219 3.64e-13

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 65.36  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  88 LKQYNARIEPGVAIRDQV--------LIGDNAVIMMGAVINIGAEIgegsmidmgailggraIVGKNCHIGAGTVLAGVV 159
Cdd:PRK10502   47 LRLFGAKIGKGVVIRPSVritypwklTIGDYAWIGDDVWLYNLGEI----------------TIGAHCVISQKSYLCTGS 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140282 160 EPPS-------AKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKD 219
Cdd:PRK10502  111 HDYSdphfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 92-215 2.31e-12

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: 64.65  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGG------------RAIVGKN------------- 146
Cdd:COG1043    19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptRLEIGDNntirefvtihrgt 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 147 ------------------------CHIGAGTV------LAGVVEppsakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:COG1043    99 vqgggvtrigddnllmayvhvahdCVVGNNVIlannatLAGHVE--------VGDHAIIGGLSAVHQFVRIGAHAMVGGG 170

                         170
                  ....*....|....*....
gi 1655140282 197 AIVINDVEPNTVVGGVPAR 215
Cdd:COG1043   171 SGVVKDVPPYVLAAGNPAR 189
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 166-225 1.09e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 61.94  E-value: 1.09e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVVGGVPARKLKDIDDKTK 225
Cdd:PRK09527  131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDK 190
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-188 1.55e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.85  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  88 LKQYNARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVlagvveppsakpv 167
Cdd:PRK00892   96 TPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVT------------- 162

                          90       100
                  ....*....|....*....|.
gi 1655140282 168 qIDDDVLIGANAVVLEGVHVG 188
Cdd:PRK00892  163 -IYHAVRIGNRVIIHSGAVIG 182
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 92-215 1.62e-11

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: 62.06  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGG-----------------------------RA- 141
Cdd:cd03351    17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptrleigdnntirefvtihRGt 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 142 -------------------------IVGKNCHIGAGTVLAGVVEppsakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:cd03351    97 aqgggvtrignnnllmayvhvahdcVIGNNVILANNATLAGHVE--------IGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                         170
                  ....*....|....*....
gi 1655140282 197 AIVINDVEPNTVVGGVPAR 215
Cdd:cd03351   169 SGVVQDVPPYVIAAGNRAR 187
cysE PRK11132
serine acetyltransferase; Provisional
 119-215 1.70e-11

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 62.41  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 119 INIGAEIGEGSMID--MGAILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:PRK11132  144 IHPAAKIGRGIMLDhaTGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223

                          90
                  ....*....|....*....
gi 1655140282 197 AIVINDVEPNTVVGGVPAR 215
Cdd:PRK11132  224 SVVLQPVPPHTTAAGVPAR 242
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
92-215 2.42e-11

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 61.65  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGG------------RAIVGKN------------- 146
Cdd:PRK05289   20 NVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEdpqdlkykgeptRLVIGDNntirefvtinrgt 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 147 ------------------------CHIGAGTV------LAGVVEppsakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAG 196
Cdd:PRK05289  100 vqgggvtrigdnnllmayvhvahdCVVGNHVIlannatLAGHVE--------VGDYAIIGGLTAVHQFVRIGAHAMVGGM 171

                         170
                  ....*....|....*....
gi 1655140282 197 AIVINDVEPNTVVGGVPAR 215
Cdd:PRK05289  172 SGVSQDVPPYVLAEGNPAR 190
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 92-209 8.44e-11

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: 59.36  E-value: 8.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVlIGDNAVIMMGAVINiGAEIGEGSMID------MGAILG--------------------------- 138
Cdd:cd03353    39 DCVIGPNCVIKDST-IGDGVVIKASSVIE-GAVIGNGATVGpfahlrPGTVLGegvhignfveikkstigegskanhlsy 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140282 139 -GRAIVGKNCHIGAGTVLA---GVveppsAK-PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVV 209
Cdd:cd03353   117 lGDAEIGEGVNIGAGTITCnydGV-----NKhRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
PLN02296 PLN02296
carbonate dehydratase
 92-226 9.03e-11

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 60.14  E-value: 9.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAV-------INIGAE--IGEGSMIDMG-AILGGR---AIVGKNCHIGAGTVLAGV 158
Cdd:PLN02296   58 DAFVAPSASVIGDVQVGRGSSIWYGCVlrgdvnsISVGSGtnIQDNSLVHVAkTNLSGKvlpTIIGDNVTIGHSAVLHGC 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655140282 159 VeppsakpvqIDDDVLIGANAVVLEGVHVGKGAVVAAGAIvindVEPNTVV------GGVPARKLKDIDDKTKS 226
Cdd:PLN02296  138 T---------VEDEAFVGMGATLLDGVVVEKHAMVAAGAL----VRQNTRIpsgevwAGNPAKFLRKLTEEEIA 198
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 99-223 9.56e-11

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 58.15  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  99 VAIRDQVLIGDNAVIM--MGAVInigaeIGEGSMIDMGAILGGR----AIVGKNCHIGAGTVLAGVveppsakpvQIDDD 172
Cdd:cd04745    19 VIIGKNCYIGPHASLRgdFGRIV-----IRDGANVQDNCVIHGFpgqdTVLEENGHIGHGAILHGC---------TIGRN 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1655140282 173 VLIGANAVVLEGVHVGKGAVVAAGAIVIN--DVEPNTVVGGVPARKLKDIDDK 223
Cdd:cd04745    85 ALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSDE 137
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 92-206 2.68e-10

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: 59.65  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDqVLIGDNAVIMM----GAVI----NIG--------AEIGEGSMIdmG-------AILG---------- 138
Cdd:COG1207   290 GVVIGPNCTLKD-STIGDGVVIKYsvieDAVVgagaTVGpfarlrpgTVLGEGVKI--GnfvevknSTIGegskvnhlsy 366

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655140282 139 -GRAIVGKNCHIGAGTVLA---GVveppsAK-PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPN 206
Cdd:COG1207   367 iGDAEIGEGVNIGAGTITCnydGV-----NKhRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAG 434
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 93-199 7.17e-10

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: 56.06  E-value: 7.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  93 ARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEG-----------SMIDMGAILG-----GRAIVGKNCHIGAGTVLA 156
Cdd:cd05636    24 AIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGcvvgnsvevknSIIMDGTKVPhlnyvGDSVLGENVNLGAGTITA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140282 157 GVVEPPSAKPVQID----------------DDVLIGANAVVLEGVHVGKGAVVAAGAIV 199
Cdd:cd05636   104 NLRFDDKPVKVRLKgervdtgrrklgaiigDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-208 1.90e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 57.04  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  93 ARIEPGVAIRDQVLIGdNAVIMMGAVINIGAEIGEGSMIdmgailgGRAIVGKNCHIGAGTVLA---GVveppSAKPVQI 169
Cdd:PRK14356  334 ARLRPGAVLEEGARVG-NFVEMKKAVLGKGAKANHLTYL-------GDAEIGAGANIGAGTITCnydGV----NKHRTVI 401

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1655140282 170 DDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTV 208
Cdd:PRK14356  402 GEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 53-227 2.27e-09

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 56.96  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  53 GDWADVEPFltanaAKIEDSEIENNArnSAVPMAdlkqynaRIEPGVAIRDQVLIGdNAVIMMGAVINIGAEIGEGSMId 132
Cdd:PRK09451  304 GDDCEISPY-----SVVEDANLGAAC--TIGPFA-------RLRPGAELAEGAHVG-NFVEMKKARLGKGSKAGHLTYL- 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 133 mgailgGRAIVGKNCHIGAGTVLAGVVEPPSAKPVqIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNT-VVGG 211
Cdd:PRK09451  368 ------GDAEIGDNVNIGAGTITCNYDGANKFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENElVISR 440

                         170
                  ....*....|....*.
gi 1655140282 212 VPARKLKDIDDKTKSK 227
Cdd:PRK09451  441 VPQRHIQGWQRPVKKK 456
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-209 2.75e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 56.47  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  69 IEDSEIENN--ARNSAVPMADLkQYNARIEPGVAIRDQVLIGDNAVImmGAVINI-GAEIGEGSMIDMGAILGGrAIVGK 145
Cdd:PRK14360  295 IENSQIGENvtVLYSVVSDSQI-GDGVKIGPYAHLRPEAQIGSNCRI--GNFVEIkKSQLGEGSKVNHLSYIGD-ATLGE 370

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655140282 146 NCHIGAGTVLA---GVveppSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTVV 209
Cdd:PRK14360  371 QVNIGAGTITAnydGV----KKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLA 433
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 68-206 3.74e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 55.99  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  68 KIEDSEIENNA--RNSAVPMADLKQY-----NARIEPGVAIRDQVLIGdNAVIMMGAVINIGAEIGEGSMIdmgailgGR 140
Cdd:PRK14354  297 RIVDSTIGDGVtiTNSVIEESKVGDNvtvgpFAHLRPGSVIGEEVKIG-NFVEIKKSTIGEGTKVSHLTYI-------GD 368

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655140282 141 AIVGKNCHIGAGTVlagVVEPPSAK--PVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPN 206
Cdd:PRK14354  369 AEVGENVNIGCGTI---TVNYDGKNkfKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 68-208 3.75e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 56.31  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  68 KIEDSEIENNAR--NSAVPMADLkQYNARIEPGVAIRDQVLIGDNAVImmGAVINI-GAEIGEGSMIDMGAILGGrAIVG 144
Cdd:PRK14357  287 RIVDCEIGNNVKiiRSECEKSVI-EDDVSVGPFSRLREGTVLKKSVKI--GNFVEIkKSTIGENTKAQHLTYLGD-ATVG 362

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655140282 145 KNCHIGAGTVLAGVvEPPSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNTV 208
Cdd:PRK14357  363 KNVNIGAGTITCNY-DGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSL 425
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 84-214 5.41e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 55.03  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  84 PMADLKQyNARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILG------------GRAIVGKNCHI-- 149
Cdd:PRK12461   10 PSAKLGS-GVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGdepqdftykgeeSRLEIGDRNVIre 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 150 ----------------------------------------GAGTVLAGvveppsakPVQIDDDVLIGANAVVLEGVHVGK 189
Cdd:PRK12461   89 gvtihrgtkgggvtrigndnllmayshvahdcqignnvilVNGALLAG--------HVTVGDRAIISGNCLVHQFCRIGA 160

                         170       180
                  ....*....|....*....|....*
gi 1655140282 190 GAVVAAGAIVINDVEPNTVVGGVPA 214
Cdd:PRK12461  161 LAMMAGGSRISKDVPPYCMMAGHPT 185
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 92-219 6.74e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.15  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDM------------------GAILG--------------- 138
Cdd:PRK00892  118 GVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAnvtiyhavrignrviihsGAVIGsdgfgfandrggwvk 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 139 ----GRAIVGKNCHIGAGTV----------------------------------------LAGvveppSAKpvqIDDDVL 174
Cdd:PRK00892  198 ipqlGRVIIGDDVEIGANTTidrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAG-----STK---IGRYCM 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1655140282 175 IGANAVVLEGVHVGKGAVVAAGAIVINDV-EPNTVVGGVPARKLKD 219
Cdd:PRK00892  270 IGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQPNKE 315
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 105-223 7.65e-09

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 53.66  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 105 VLIGDnavIMMGAVINIGAE-----------IGEGSMIDMGAILGGRA----IVGKNCHIGAGTVLAGVVeppsakpvqI 169
Cdd:PRK13627   24 VLIGD---VIVGAGVYIGPLaslrgdygrliVQAGANLQDGCIMHGYCdtdtIVGENGHIGHGAILHGCV---------I 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140282 170 DDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDV--EPNTVVGGVPARKLKDIDDK 223
Cdd:PRK13627   92 GRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVSDD 147
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-207 4.04e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 50.13  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  69 IEDSEIENNArnSAVPMADLKqynariePGVAIRDQVLIGdNAVIMMGAVInigaeiGEGSMIDMGAILGGrAIVGKNCH 148
Cdd:PRK14355  318 LEDSVVGDDV--AIGPMAHLR-------PGTELSAHVKIG-NFVETKKIVM------GEGSKASHLTYLGD-ATIGRNVN 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140282 149 IGAGTVLAGVVEPPSAKPVqIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPNT 207
Cdd:PRK14355  381 IGCGTITCNYDGVKKHRTV-IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDS 438
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 92-209 2.89e-06

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: 46.08  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVIN----IGAEIGEGSMIDMGAIL----GGRAIVGKNCHIGAGTVLAGvvepps 163
Cdd:cd00710     8 SAYVHPTAVVIGDVIIGDNVFVGPGASIRadegTPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHG------ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1655140282 164 akPVQIDDDVLIGANAVVLEGVhVGKGAVVAAGAIVIN-DVEPNTVV 209
Cdd:cd00710    82 --PAYIGDNCFIGFRSVVFNAK-VGDNCVIGHNAVVDGvEIPPGRYV 125
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 92-180 3.02e-06

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 47.38  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDqvligdnaVIMMGaviniGAEIGEGSMIDmgailggRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDD 171
Cdd:COG0448   309 GVRVESGAVVEN--------SVIMP-----GVVIGEGAVIE-------NAIIDKNVVIPPGVVIGEDPEEDRKRFTVSSG 368


                  ....*....
gi 1655140282 172 DVLIGANAV 180
Cdd:COG0448   369 IVVVGKGAV 377
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 119-193 3.85e-06

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: 45.87  E-value: 3.85e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655140282 119 INIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLagvveppsaKPVQIDDDVLIGANaVVLEGVHVGKGAVV 193
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI---------KDSTIGDGVVIKAS-SVIEGAVIGNGATV 76
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-206 4.73e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 46.78  E-value: 4.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  93 ARIEPGVAIRDQVLIGdNAVIMMGAVINIGAEIGEGSMIdmgailgGRAIVGKNCHIGAGTVLA---GVveppSAKPVQI 169
Cdd:PRK14353  316 ARLRPGAELGEGAKVG-NFVEVKNAKLGEGAKVNHLTYI-------GDATIGAGANIGAGTITCnydGF----NKHRTEI 383

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1655140282 170 DDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDVEPN 206
Cdd:PRK14353  384 GAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDD 420
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 92-196 8.11e-06

Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP succinyltransferase), C-terminal left-handed parallel alpha-helix (LbH) domain: This group is composed of mostly uncharacterized proteins containing an N-terminal domain of unknown function and a C-terminal LbH domain with similarity to THP succinyltransferase LbH. THP 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 trimeric and displays the left-handed parallel alpha-helix (LbH) structural motif encoded by the hexapeptide repeat motif.


Pssm-ID: 100054  Cd Length: 147  Bit Score: 44.33  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMIDmGAILGGrAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDD 171
Cdd:cd04649     1 GVRIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVE-GRISSG-VIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                          90       100
                  ....*....|....*....|....*
gi 1655140282 172 DVLIGANAVVleGVHVGKGAVVAAG 196
Cdd:cd04649    79 RCLLGANSGI--GISLGDNCIVEAG 101
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 119-193 1.48e-05

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: 45.40  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655140282 119 INIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLagvveppsakpvqidDDVLIGANAVV----LEGVHVGKGAVV 193
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL---------------KDSTIGDGVVIkysvIEDAVVGAGATV 326
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-202 4.47e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.83  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  69 IEDSEIENnarnSAV-PMAdlkqynaRIEPGVAIRDqVLIGdNAVIMMGAVIN---------IG-AEIGEGSMIDMGAI- 136
Cdd:PRK14359  291 IEESIIEN----SDVgPLA-------HIRPKSEIKN-THIG-NFVETKNAKLNgvkaghlsyLGdCEIDEGTNIGAGTIt 357

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655140282 137 --LGGRA----IVGKNCHIGAGTVLAGvveppsakPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIVIND 202
Cdd:PRK14359  358 cnYDGKKkhktIIGKNVFIGSDTQLVA--------PVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKN 421
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 95-225 5.28e-05

Dynactin 5 (or subunit p25); 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 p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain 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: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 42.20  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  95 IEPGVAIRDQVL---IGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGAgtvlagvveppsakpVQIDD 171
Cdd:cd03359    30 IQSDVIIRGDLAtvsIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNA---------------AQIGS 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140282 172 DVLIGANAVVLEGVHVGKGAVVAAGAIVIND--VEPNTVVGGVPARKLKDIDDKTK 225
Cdd:cd03359    95 YVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQ 150
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 93-190 6.25e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.09  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  93 ARIEPGVAIRDQVLIGDNAVImmGAviniGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGvvEPPSAKPVQIDDD 172
Cdd:PRK12461    6 AVIDPSAKLGSGVEIGPFAVI--GA----NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQDFTYKGEESR 77

                          90
                  ....*....|....*...
gi 1655140282 173 VLIGANAVVLEGVHVGKG 190
Cdd:PRK12461   78 LEIGDRNVIREGVTIHRG 95
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 118-204 8.32e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 39.87  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 118 VINIGAEIGEGSMIDmgailggRAIVGKNCHIGAGTVLAGVVeppsakpvqIDDDVLIGANAVVL-----EGVHVGKGAV 192
Cdd:cd05787     1 VIGRGTSIGEGTTIK-------NSVIGRNCKIGKNVVIDNSY---------IWDDVTIEDGCTIHhsivaDGAVIGKGCT 64

                          90
                  ....*....|..
gi 1655140282 193 VAAGAIVINDVE 204
Cdd:cd05787    65 IPPGSLISFGVV 76
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 129-213 8.52e-05

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: 42.70  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 129 SMIDMGAILGGRAIVGKNCHIGAGTvlagVVEPpsakPVQIDDDVLIGANAVVLEGVHVGKGavvaagaiviNDVEPNTV 208
Cdd:COG1043     2 AMIHPTAIVDPGAKLGENVEIGPFC----VIGP----DVEIGDGTVIGSHVVIEGPTTIGKN----------NRIFPFAS 63


                  ....*
gi 1655140282 209 VGGVP 213
Cdd:COG1043    64 IGEEP 68
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
129-213 1.59e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 129 SMIDMGAILGGRAIVGKNCHIGAGTvlagVVEPpsakPVQIDDDVLIGANAVVLEGVHVGKGavvaagaiviNDVEPNTV 208
Cdd:PRK05289    3 AKIHPTAIVEPGAKIGENVEIGPFC----VIGP----NVVIGDGTVIGSHVVIDGHTTIGKN----------NRIFPFAS 64


                  ....*
gi 1655140282 209 VGGVP 213
Cdd:PRK05289   65 IGEDP 69
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 92-181 3.03e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 38.98  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  92 NARIEPGVAIRDqvligdnaVIMMGAVinigaEIGEGSMIDmgailggRAIVGKNCHIGAGTVLAGVVEPPSAKPVQIDD 171
Cdd:cd04651    34 GVRVGSGSVVED--------SVIMPNV-----GIGRNAVIR-------RAIIDKNVVIPDGVVIGGDPEEDRARFYVTED 93

                          90
                  ....*....|.
gi 1655140282 172 D-VLIGANAVV 181
Cdd:cd04651    94 GiVVVGKGMVI 104
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 93-203 6.35e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.35  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  93 ARIEPGVAIRDQVLIGdNAVIMMGAVINIGAEIGEGSMIdmgailgGRAIVGKNCHIGAGTVLA---GVVEPPSakpvQI 169
Cdd:PRK14358  335 ARLRPGTVLGEGVHIG-NFVETKNARLDAGVKAGHLAYL-------GDVTIGAETNVGAGTIVAnfdGVNKHQS----KV 402

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1655140282 170 DDDVLIGANAVVLEGVHVGKGAVVAAGAIVINDV 203
Cdd:PRK14358  403 GAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDV 436
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-204 6.89e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.40  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 131 IDMGAILGGRAIVGKNCHIGAGTVLagvveppsaKPVQIDDDVLIGANAVVlEGVHVGK------------GAVVAAGAI 198
Cdd:PRK09451  274 IDTNVIIEGNVTLGNRVKIGAGCVL---------KNCVIGDDCEISPYSVV-EDANLGAactigpfarlrpGAELAEGAH 343


                  ....*.
gi 1655140282 199 VINDVE 204
Cdd:PRK09451  344 VGNFVE 349
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 61-188 8.42e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.85  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  61 FLTANAaKIEDS------EIENNARNSAVpmadlkQYNARIEPGVAIRDqvligdnAVIMMGAvinigaEIGEGSMIDmG 134
Cdd:PRK05293  284 YIAENA-KVKNSlvvegcVVYGTVEHSVL------FQGVQVGEGSVVKD-------SVIMPGA------KIGENVVIE-R 342

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1655140282 135 AILGGRAIVGKNCHIGAGTvlagvveppsakpvqiDDDVLIGANAVVLEGVHVG 188
Cdd:PRK05293  343 AIIGENAVIGDGVIIGGGK----------------EVITVIGENEVIGVGTVIG 380
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 130-213 8.81e-04

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: 39.34  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 130 MIDMGAILGGRAIVGKNCHIGAGTvlagVVEPpsakPVQIDDDVLIGANAVVLEGVHVGKGavvaagaiviNDVEPNTVV 209
Cdd:cd03351     1 MIHPTAIVDPGAKIGENVEIGPFC----VIGP----NVEIGDGTVIGSHVVIDGPTTIGKN----------NRIFPFASI 62


                  ....
gi 1655140282 210 GGVP 213
Cdd:cd03351    63 GEAP 66
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
122-151 9.34e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 9.34e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1655140282 122 GAEIGEGSMIDMGAILGGRAIVGKNCHIGA 151
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 95-201 1.60e-03

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.19  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282  95 IEPGVAIRDQVLIGDNAVIMMGAVINiGAEIGEGSMIDMGAILGGrAIVGKNCHIG------AGTVLAGVVEPPS---AK 165
Cdd:PRK14358  279 IEPGVLLRGQTRVADGVTIGAYSVVT-DSVLHEGAVIKPHSVLEG-AEVGAGSDVGpfarlrPGTVLGEGVHIGNfveTK 356

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1655140282 166 PVQIDDDVLIGANAvVLEGVHVGKGAVVAAGAIVIN 201
Cdd:PRK14358  357 NARLDAGVKAGHLA-YLGDVTIGAETNVGAGTIVAN 391
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 94-150 2.22e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 38.71  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655140282  94 RIEPGVAIRDqvligdnaVIMMGA----------------VINIGaeIGEGSMIDmgailggRAIVGKNCHIG 150
Cdd:PRK02862  332 RIESGCTIED--------TLVMGAdfyesseereelrkegKPPLG--IGEGTTIK-------RAIIDKNARIG 387
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 123-205 2.46e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 38.38  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 123 AEIGEGSMIDMGAILGGrAIVGKNCHIGAGTVLA---GVveppSAKPVQIDDDVLIGANAVVLEGVHVGKGAVVAAGAIV 199
Cdd:PRK14352  358 ATIGRGTKVPHLTYVGD-ADIGEHSNIGASSVFVnydGV----NKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVI 432


                  ....*.
gi 1655140282 200 INDVEP 205
Cdd:PRK14352  433 REDVPP 438
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
167-199 3.43e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.34  E-value: 3.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1655140282 167 VQIDDDVLIGANAVVleGVHVGKGAVVAAGAIV 199
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 125-210 4.13e-03

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: 35.30  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 125 IGEGSMIDMGAILGgRAIVGKNCHIGAGTVLAGVVeppsakpvqIDDDVLIGANAVVLEGVhVGKGAVVAAGAivinDVE 204
Cdd:cd03356     2 IGESTVIGENAIIK-NSVIGDNVRIGDGVTITNSI---------LMDNVTIGANSVIVDSI-IGDNAVIGENV----RVV 66


                  ....*.
gi 1655140282 205 PNTVVG 210
Cdd:cd03356    67 NLCIIG 72
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 107-159 4.31e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 35.25  E-value: 4.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1655140282 107 IGDNaVIMMGAVINIGAEIGEGSMIDMgAILGGRAIVGKNCHIGAGTVLA-GVV 159
Cdd:cd05787    25 IGKN-VVIDNSYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLISfGVV 76
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
166-195 4.62e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 4.62e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1655140282 166 PVQIDDDVLIGANAVVLEGVHVGKGAVVAA 195
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 99-163 4.83e-03

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 36.39  E-value: 4.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655140282  99 VAIRDQVLIGDNAVIMmgaviniGAEIGEGSMIDMGAILGGRAIVGKNCHIGAGTVLAGVVEPPS 163
Cdd:cd04650    62 TEIGDYVTIGHNAVVH-------GAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPD 119
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 92-153 5.14e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 35.33  E-value: 5.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655140282  92 NARIEPGVAIRDQVLIGDNAVIMMGAVINIGAEIGEGSMID---MGAILG-----------GRAIVGKNCHIGAGT 153
Cdd:cd05635    17 DAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGgevEDSIIEgysnkqhdgflGHSYLGSWCNLGAGT 92
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 105-165 5.89e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 35.33  E-value: 5.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655140282 105 VLIGDNAVIMMGAVINIGAEIGEGSMIDMGAILGGRAIVGKNCHIGaGTVLAGVVEPPSAK 165
Cdd:cd05635    12 IYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIG-GEVEDSIIEGYSNK 71
PRK10191 PRK10191
putative acyl transferase; Provisional
 114-215 8.23e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 35.64  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655140282 114 MMGAVINIGAEIGEGSMIDMG--AILGGRAIVGKNCHIGAGTVLAGVVEPPSAKPVqIDDDVLIGANAVVLEGVHVGKGA 191
Cdd:PRK10191   39 FFGYEIQAAATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGNRGADNMACPH-IGNGVELGANVIILGDITIGNNV 117

                          90       100
                  ....*....|....*....|....
gi 1655140282 192 VVAAGAIVINDVEPNTVVGGVPAR 215
Cdd:PRK10191  118 TVGAGSVVLDSVPDNALVVGEKAR 141
 
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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