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Conserved domains on  [gi|2564886272|ref|WP_306088860|]
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2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase [Qipengyuania flava]

Protein Classification

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase( domain architecture ID 11485562)

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase catalyzes the formation of CoA and N-succinyl-2-amino-6-keto-L-pimelate from succinyl-CoA and tetrahydrodipicolinate

EC:  2.3.1.117
Gene Ontology:  GO:0016779|GO:0009089|GO:0008666
SCOP:  4002837

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 3-273 7.14e-179

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


:

Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 492.78  E-value: 7.14e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   3 ADLESRITAAWEDRANVTPQSAD--VREAVEAALGMLDSGEGRVAVPDGKGGWTVNQWLKKAVLLSFRLNDNRVMDGGSA 80
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADteVREAVEEVIDLLDSGELRVAEKIDDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  81 GHpaFDKVPSKFAGWDDARFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHI 160
Cdd:PRK11830   82 RF--YDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 161 SAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTM 240
Cdd:PRK11830  160 SGGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSL 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2564886272 241 PGKDGGPGLACAVIVKTVDAQTREKTGINELLR 273
Cdd:PRK11830  240 PSKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 3-273 7.14e-179

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 492.78  E-value: 7.14e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   3 ADLESRITAAWEDRANVTPQSAD--VREAVEAALGMLDSGEGRVAVPDGKGGWTVNQWLKKAVLLSFRLNDNRVMDGGSA 80
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADteVREAVEEVIDLLDSGELRVAEKIDDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  81 GHpaFDKVPSKFAGWDDARFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHI 160
Cdd:PRK11830   82 RF--YDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 161 SAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTM 240
Cdd:PRK11830  160 SGGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSL 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2564886272 241 PGKDGGPGLACAVIVKTVDAQTREKTGINELLR 273
Cdd:PRK11830  240 PSKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 3-274 1.53e-165

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: 459.20  E-value: 1.53e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   3 ADLESRITAAWEDRANVTPQ-SADVREAVEAALGMLDSGEGRVAVPDGKGGWTVNQWLKKAVLLSFRLNDNRVMDGGSAg 81
Cdd:COG2171     2 ADLGTVIDAAWENRAELTPLaDREVREAVEEVIAALDAGPLRVAEPNLDGEWVVNEWVKKAILLSFRLEDNRVLEGGGV- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  82 hPAFDKVPSKFAgwddaRFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHIS 161
Cdd:COG2171    81 -TYHDKVPLKFD-----YFKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 162 AGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMP 241
Cdd:COG2171   155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2564886272 242 GKDGGPGLACAVIVKTVDAQTREKTGINELLRD 274
Cdd:COG2171   235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRD 267
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 5-273 2.03e-136

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-succinyltransferase. The closely related TabB protein of Pseudomonas syringae (pv. tabaci), SP|P31852|TABB_PSESZ, appears to act in the biosynthesis of tabtoxin rather than lysine. The trusted cutoff is set high enough to exclude this gene. Sequences below trusted also include a version of this enzyme which apparently utilize acetate rather than succinate (EC: 2.3.1.89). [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130038 [Multi-domain]  Cd Length: 269  Bit Score: 385.40  E-value: 2.03e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   5 LESRITAAWEDRANVTPQSAD--VREAVEAALGMLDSGEGRVAVPDGkGGWTVNQWLKKAVLLSFRLNDNRVMDGGSAGH 82
Cdd:TIGR00965   2 LQNIIETAFERRAEITPANADtvTKEAVNEVIALLDSGALRVAEKID-GQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  83 paFDKVPSKFAGWDDARFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISA 162
Cdd:TIGR00965  81 --FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 163 GAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMPG 242
Cdd:TIGR00965 159 GVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPS 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2564886272 243 KDGGPGLACAVIVKTVDAQTREKTGINELLR 273
Cdd:TIGR00965 239 KDGKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 104-241 6.26e-68

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: 206.85  E-value: 6.26e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 104 GFRVVPGAVAREGAYIAPGCVLM-PSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGD 182
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2564886272 183 NCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMP 241
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 4-69 2.83e-30

Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.


Pssm-ID: 464325 [Multi-domain]  Cd Length: 67  Bit Score: 107.94  E-value: 2.83e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2564886272   4 DLESRITAAWEDRANVTPQSA--DVREAVEAALGMLDSGEGRVAVPDGkGGWTVNQWLKKAVLLSFRL 69
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATAdaEVRDAVEEVIDLLDAGELRVAEKID-GGWVVNEWVKKAVLLYFRL 67
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 3-273 7.14e-179

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 492.78  E-value: 7.14e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   3 ADLESRITAAWEDRANVTPQSAD--VREAVEAALGMLDSGEGRVAVPDGKGGWTVNQWLKKAVLLSFRLNDNRVMDGGSA 80
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADteVREAVEEVIDLLDSGELRVAEKIDDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  81 GHpaFDKVPSKFAGWDDARFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHI 160
Cdd:PRK11830   82 RF--YDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 161 SAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTM 240
Cdd:PRK11830  160 SGGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSL 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2564886272 241 PGKDGGPGLACAVIVKTVDAQTREKTGINELLR 273
Cdd:PRK11830  240 PSKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 3-274 1.53e-165

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: 459.20  E-value: 1.53e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   3 ADLESRITAAWEDRANVTPQ-SADVREAVEAALGMLDSGEGRVAVPDGKGGWTVNQWLKKAVLLSFRLNDNRVMDGGSAg 81
Cdd:COG2171     2 ADLGTVIDAAWENRAELTPLaDREVREAVEEVIAALDAGPLRVAEPNLDGEWVVNEWVKKAILLSFRLEDNRVLEGGGV- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  82 hPAFDKVPSKFAgwddaRFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHIS 161
Cdd:COG2171    81 -TYHDKVPLKFD-----YFKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 162 AGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMP 241
Cdd:COG2171   155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2564886272 242 GKDGGPGLACAVIVKTVDAQTREKTGINELLRD 274
Cdd:COG2171   235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRD 267
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 5-273 2.03e-136

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-succinyltransferase. The closely related TabB protein of Pseudomonas syringae (pv. tabaci), SP|P31852|TABB_PSESZ, appears to act in the biosynthesis of tabtoxin rather than lysine. The trusted cutoff is set high enough to exclude this gene. Sequences below trusted also include a version of this enzyme which apparently utilize acetate rather than succinate (EC: 2.3.1.89). [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130038 [Multi-domain]  Cd Length: 269  Bit Score: 385.40  E-value: 2.03e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272   5 LESRITAAWEDRANVTPQSAD--VREAVEAALGMLDSGEGRVAVPDGkGGWTVNQWLKKAVLLSFRLNDNRVMDGGSAGH 82
Cdd:TIGR00965   2 LQNIIETAFERRAEITPANADtvTKEAVNEVIALLDSGALRVAEKID-GQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  83 paFDKVPSKFAGWDDARFRDAGFRVVPGAVAREGAYIAPGCVLMPSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISA 162
Cdd:TIGR00965  81 --FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 163 GAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMPG 242
Cdd:TIGR00965 159 GVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPS 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2564886272 243 KDGGPGLACAVIVKTVDAQTREKTGINELLR 273
Cdd:TIGR00965 239 KDGKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 104-241 6.26e-68

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: 206.85  E-value: 6.26e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 104 GFRVVPGAVAREGAYIAPGCVLM-PSFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGD 182
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2564886272 183 NCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKIVYRDTGEVIGGHIPPYSVVVPGTMP 241
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 4-69 2.83e-30

Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.


Pssm-ID: 464325 [Multi-domain]  Cd Length: 67  Bit Score: 107.94  E-value: 2.83e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2564886272   4 DLESRITAAWEDRANVTPQSA--DVREAVEAALGMLDSGEGRVAVPDGkGGWTVNQWLKKAVLLSFRL 69
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATAdaEVRDAVEEVIDLLDAGELRVAEKID-GGWVVNEWVKKAVLLYFRL 67
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 134-211 3.20e-19

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: 79.60  E-value: 3.20e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2564886272 134 AYVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFIT 211
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 98-236 1.34e-16

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: 75.98  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272  98 ARFRDAGFRVV----PGAVAREGAYIAPGCVLMP-SFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISAGAGI-GGVle 171
Cdd:cd03360    74 EKLLAAGYRFAtlihPSAVVSPSAVIGEGCVIMAgAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLsGGV-- 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2564886272 172 pmqanptIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQStkivyrdtgevigghIPPYSVVV 236
Cdd:cd03360   152 -------TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKD---------------VPDGSVVV 194
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
115-236 2.08e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 73.75  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVLMPSFVNIGAYV--GKGTMVDTWASIgscaQIGENCHISAGAGIGGV--------LEPMQANPTIIGDNC 184
Cdd:COG0110    13 DGVVIGPGVRIYGGNITIGDNVyiGPGVTIDDPGGI----TIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVTIGDDV 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2564886272 185 FIGARSEIVEGVIVGEGSVVAMGVFITQStkivyrdtgevigghIPPYSVVV 236
Cdd:COG0110    89 WIGAGATILPGVTIGDGAVVGAGSVVTKD---------------VPPYAIVA 125
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 104-220 6.71e-13

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: 64.74  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 104 GFRVVPGAVAREGAYIAPGCVLMP-SFVNIGAYVGKGTMVDtwASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGD 182
Cdd:cd04649     1 GVRIADADRVRLGAYLAEGTTVMHeGFVNFNAGTLGNCMVE--GRISSGVIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2564886272 183 NCFIGARSEIveGVIVGEGSVVAMGVFITQSTKIVYRD 220
Cdd:cd04649    79 RCLLGANSGI--GISLGDNCIVEAGLYVTAGTKVTLPD 114
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 130-236 8.20e-12

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: 60.55  E-value: 8.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 130 VNIG--AYVGKGTMVDTWASIgscaQIGENCHISAGAGI-----------GGVLEPMQANPTIIGDNCFIGARSEIVEGV 196
Cdd:cd04647     2 ISIGdnVYIGPGCVISAGGGI----TIGDNVLIGPNVTIydhnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2564886272 197 IVGEGSVVAMGVFITQStkivyrdtgevigghIPPYSVVV 236
Cdd:cd04647    78 TIGDGAVVGAGSVVTKD---------------VPPNSIVA 102
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 117-211 1.97e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.53  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPS-----FVNI-GAYVGKGTMVDTWASIGScAQIGENCHISAGA------GIggvlepmQANPTIIGDNC 184
Cdd:PRK14354  329 AHLRPGSVIGEEvkignFVEIkKSTIGEGTKVSHLTYIGD-AEVGENVNIGCGTitvnydGK-------NKFKTIIGDNA 400

                          90       100
                  ....*....|....*....|....*..
gi 2564886272 185 FIGARSEIVEGVIVGEGSVVAMGVFIT 211
Cdd:PRK14354  401 FIGCNSNLVAPVTVGDNAYIAAGSTIT 427
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 117-211 3.28e-09

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: 55.12  E-value: 3.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPSfVNIGAYV-------GKGTMVDTWASIGScAQIGENCHISAG---AGIGGVlepmQANPTIIGDNCFI 186
Cdd:cd03353    80 AHLRPGTVLGEG-VHIGNFVeikkstiGEGSKANHLSYLGD-AEIGEGVNIGAGtitCNYDGV----NKHRTVIGDNVFI 153

                          90       100
                  ....*....|....*....|....*
gi 2564886272 187 GARSEIVEGVIVGEGSVVAMGVFIT 211
Cdd:cd03353   154 GSNSQLVAPVTIGDGATIAAGSTIT 178
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 148-236 4.26e-09

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: 52.83  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 148 IGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQStkivyrdtgevigg 227
Cdd:cd03354    25 IGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD-------------- 90


                  ....*....
gi 2564886272 228 hIPPYSVVV 236
Cdd:cd03354    91 -VPANSTVV 98
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-211 6.86e-09

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 56.19  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 106 RVVPGAVAREGAYIApgcvlmpSFVNI-GAYVGKGTMVDTWASIGScAQIGENCHISAGAgIGGVLEPMQANPTIIGDNC 184
Cdd:PRK09451  331 RLRPGAELAEGAHVG-------NFVEMkKARLGKGSKAGHLTYLGD-AEIGDNVNIGAGT-ITCNYDGANKFKTIIGDDV 401

                          90       100
                  ....*....|....*....|....*..
gi 2564886272 185 FIGARSEIVEGVIVGEGSVVAMGVFIT 211
Cdd:PRK09451  402 FVGSDTQLVAPVTVGKGATIGAGTTVT 428
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 133-236 2.51e-08

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: 52.39  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 133 GAYVGKGTMVD--TWASIGSCAQIGENCHISAGAGIGGV-LEPMQANPTIiGDNCFIGARSEIVEGVIVGEGSVVAMGVF 209
Cdd:COG1045    71 GATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPTI-GDNVVIGAGAKILGPITIGDNAKIGANSV 149

                          90       100
                  ....*....|....*....|....*..
gi 2564886272 210 ITQStkivyrdtgevigghIPPYSVVV 236
Cdd:COG1045   150 VLKD---------------VPPGSTVV 161
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
178-212 3.49e-08

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 48.20  E-value: 3.49e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2564886272 178 TIIGDNCFIGARSEIveGVIVGEGSVVAMGVFITQ 212
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 115-236 3.95e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 51.57  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVL---MPSFVnIGAY--VGKGTMVDTWAsiGSCAQIGENCHISAGAGIGGVlepmqanptIIGDNCFIGAR 189
Cdd:COG0663    33 EDVSVWPGAVLrgdVGPIR-IGEGsnIQDGVVLHVDP--GYPLTIGDDVTIGHGAILHGC---------TIGDNVLIGMG 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2564886272 190 SEIVEGVIVGEGSVVAMGVFITQstkivyrdtgeviGGHIPPYSVVV 236
Cdd:COG0663   101 AIVLDGAVIGDGSIVGAGALVTE-------------GKVVPPGSLVV 134
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 109-210 2.13e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.29  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVLMPsfvniGAYVGKGtmvdtwasigscAQIGENCHISAGAGIG-GVlepmqanptIIGDNCFIG 187
Cdd:PRK00892  105 PSAVIDPSAKIGEGVSIGP-----NAVIGAG------------VVIGDGVVIGAGAVIGdGV---------KIGADCRLH 158

                          90       100
                  ....*....|....*....|...
gi 2564886272 188 ARSEIVEGVIVGEGSVVAMGVFI 210
Cdd:PRK00892  159 ANVTIYHAVRIGNRVIIHSGAVI 181
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 107-212 2.44e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 51.30  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 107 VVPGAVAREGAYIAPGcVLMPSFVNI-GAYVGKGTMVDTWASIGScAQIGENCHISAGAgIGGVLEPMQANPTIIGDNCF 185
Cdd:PRK14357  315 VGPFSRLREGTVLKKS-VKIGNFVEIkKSTIGENTKAQHLTYLGD-ATVGKNVNIGAGT-ITCNYDGKKKNPTFIEDGAF 391

                          90       100
                  ....*....|....*....|....*..
gi 2564886272 186 IGARSEIVEGVIVGEGSVVAMGVFITQ 212
Cdd:PRK14357  392 IGSNSSLVAPVRIGKGALIGAGSVITE 418
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 117-200 2.80e-07

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: 50.79  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPSfVNIGAYvgkgtmvdtwASIGSCAQIGENCHISAGAGIG-GVlepmqanptIIGDNCFIGARSEIVEG 195
Cdd:COG1044   103 AVIDPSAKIGEG-VSIGPF----------AVIGAGVVIGDGVVIGPGVVIGdGV---------VIGDDCVLHPNVTIYER 162


                  ....*
gi 2564886272 196 VIVGE 200
Cdd:COG1044   163 CVIGD 167
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 146-236 3.14e-07

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: 48.69  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 146 ASIGSCAQIGENCHISAGA------------GIGGVLEPMQAN--------PTIIGDNCFIGARSEIVEGVIVGEGSVVA 205
Cdd:cd03349    22 LSIGKFCSIAPGVKIGLGGnhptdwvstypfYIFGGEWEDDAKfddwpskgDVIIGNDVWIGHGATILPGVTIGDGAVIA 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2564886272 206 MGvfitqstKIVYRDtgevigghIPPYSVVV 236
Cdd:cd03349   102 AG-------AVVTKD--------VPPYAIVG 117
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 117-236 4.52e-07

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: 48.57  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPSF-----VNIgaYVGKG-------TMVDTWA-SIGSCAQIGENCHISAGagiGGVLEPMQ-------AN 176
Cdd:cd03357    43 GSVGENVYIEPPFhcdygYNI--HIGDNfyanfncTILDVAPvTIGDNVLIGPNVQIYTA---GHPLDPEErnrgleyAK 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 177 PTIIGDNCFIGARSEIVEGVIVGEGSVVAMGvfitqstKIVYRDtgevigghIPPYSVVV 236
Cdd:cd03357   118 PITIGDNVWIGGGVIILPGVTIGDNSVIGAG-------SVVTKD--------IPANVVAA 162
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 117-212 6.27e-07

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: 50.03  E-value: 6.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPSfVNIGAYV-------GKGTMVDTWASIGScAQIGENCHISAGAgiggvlepMQAN-------PTIIGD 182
Cdd:COG1207   330 ARLRPGTVLGEG-VKIGNFVevknstiGEGSKVNHLSYIGD-AEIGEGVNIGAGT--------ITCNydgvnkhRTVIGD 399

                          90       100       110
                  ....*....|....*....|....*....|
gi 2564886272 183 NCFIGARSEIVEGVIVGEGSVVAMGVFITQ 212
Cdd:COG1207   400 GAFIGSNTNLVAPVTIGDGATIGAGSTITK 429
PLN02296 PLN02296
carbonate dehydratase
 115-227 8.30e-07

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 48.97  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVLMPSFVNIgayvgkgtmvdtwaSIGSCAQIGENCHIS-AGAGIGGVLEPmqanpTIIGDN---------- 183
Cdd:PLN02296   75 RGSSIWYGCVLRGDVNSI--------------SVGSGTNIQDNSLVHvAKTNLSGKVLP-----TIIGDNvtighsavlh 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2564886272 184 -C------FIGARSEIVEGVIVGEGSVVAMGVFITQSTKIvyrDTGEVIGG 227
Cdd:PLN02296  136 gCtvedeaFVGMGATLLDGVVVEKHAMVAAGALVRQNTRI---PSGEVWAG 183
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 102-228 9.29e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 102 DAGFRVVPGAVAREGAYIAPGCVLMPsfvniGAYVGKGTMV--DTW----ASIGSCAQIGENCHISAGAGIG-------- 167
Cdd:PRK00892  116 GEGVSIGPNAVIGAGVVIGDGVVIGA-----GAVIGDGVKIgaDCRlhanVTIYHAVRIGNRVIIHSGAVIGsdgfgfan 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 168 --GVLEPM-QANPTIIGDNCFIGARS----------EIVEGVI------------VGEGSVVAMGVFITQSTKIvyrdtG 222
Cdd:PRK00892  191 drGGWVKIpQLGRVIIGDDVEIGANTtidrgalddtVIGEGVKidnlvqiahnvvIGRHTAIAAQVGIAGSTKI-----G 265


                  ....*...
gi 2564886272 223 E--VIGGH 228
Cdd:PRK00892  266 RycMIGGQ 273
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 109-216 1.06e-06

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: 48.17  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVLMPSfVNIGAYV--GKGTMVDTWASIGSCAQIGENCHISAGAGIGG------------------ 168
Cdd:cd03352    12 PNAVIGEGVVIGDGVVIGPG-VVIGDGVviGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgfapdgggwvkipql 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2564886272 169 ---VLEP---MQAN---------PTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKI 216
Cdd:cd03352    91 ggvIIGDdveIGANttidrgalgDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTI 153
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 115-216 1.23e-06

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: 47.02  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVLmpsfvnIGA-YVGKGTMVdtWA-----------SIGSCAQIGENC--HISAGAG--IGgvlepmqANPT 178
Cdd:cd04645     4 PSAFIAPNATV------IGDvTLGEGSSV--WFgavlrgdvnpiRIGERTNIQDGSvlHVDPGYPtiIG-------DNVT 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2564886272 179 I----------IGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKI 216
Cdd:cd04645    69 VghgavlhgctIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVI 116
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 109-216 1.36e-06

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: 48.86  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVLMPsfvniGAYVGKGTMV--DTW----ASIGSCAQIGENCHISAGAGIG-----------GVLE 171
Cdd:COG1044   119 PFAVIGAGVVIGDGVVIGP-----GVVIGDGVVIgdDCVlhpnVTIYERCVIGDRVIIHSGAVIGadgfgfapdedGGWV 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2564886272 172 PM-QANPTIIGDNCFIGA---------RSEIVE-------------GVIVGEGSVVAMGVFITQSTKI 216
Cdd:COG1044   194 KIpQLGRVVIGDDVEIGAnttidrgalGDTVIGdgtkidnlvqiahNVRIGEHTAIAAQVGIAGSTKI 261
PRK10502 PRK10502
putative acyl transferase; Provisional
 116-236 3.27e-06

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 46.48  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 116 GAYIAPGCVLMPS-------FVNIGAY--VGKGTMVDTWASIgscaQIGENCHISAGAGI-GGVLEPMQAN------PTI 179
Cdd:PRK10502   51 GAKIGKGVVIRPSvritypwKLTIGDYawIGDDVWLYNLGEI----TIGAHCVISQKSYLcTGSHDYSDPHfdlntaPIV 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2564886272 180 IGDNCFIGARSEIVEGVIVGEGSVVAmgvfitqstkivyrdTGEVIGGHIPPYSVVV 236
Cdd:PRK10502  127 IGEGCWLAADVFVAPGVTIGSGAVVG---------------ARSSVFKSLPANTICR 168
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 118-247 3.80e-06

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: 46.05  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 118 YIAPGCVLMPSFVNIGAYVGKGTMVdtwasIGSCAQIGENCHISAgAGIGgvlepmqaNPTIIGDNCFIGARSEIVEGVI 197
Cdd:cd03359    50 ILSEGCVIRPPFKKFSKGVAFFPLH-----IGDYVFIGENCVVNA-AQIG--------SYVHIGKNCVIGRRCIIKDCVK 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2564886272 198 VGEGSVVAMGVFitqstkivyrdtgevigghIPPYSVVvpGTMPGKDGGP 247
Cdd:cd03359   116 ILDGTVVPPDTV-------------------IPPYSVV--SGRPARFIGE 144
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 115-213 3.85e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 46.34  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPgcvlmpSF-----VNIgaYVGKG-------TMVDTwasigsCA-QIGENCHISAGAGIGGVLEPMQA------ 175
Cdd:PRK10092   58 TEAYIEP------TFrcdygYNI--FLGNNfyanfdcVMLDV------CPiRIGDNCMLAPGVHIYTATHPLDPvarnsg 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2564886272 176 ----NPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQS 213
Cdd:PRK10092  124 aelgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKD 165
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 128-236 4.65e-06

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: 44.80  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 128 SFVNIGAYVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGVLEPMQAN-------PTIIGDNCFIGARSEIVEGVIVGE 200
Cdd:cd03358    11 VFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIyrkwelkGTTVKRGASIGANATILPGVTIGE 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2564886272 201 GSVVAMGVFITqstkivyRDtgevigghIPPYSVVV 236
Cdd:cd03358    91 YALVGAGAVVT-------KD--------VPPYALVV 111
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 134-210 9.83e-06

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: 45.48  E-value: 9.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564886272 134 AYVGKGTMVDTWASIGSCAQIGENCHISAGAGIGgvlepmqaNPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFI 210
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 152-227 1.34e-05

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: 44.71  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2564886272 152 AQIGENCHISAGAGIGgvlepmqaNPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKI---VYRDTGEVIGG 227
Cdd:cd03352     2 AKIGENVSIGPNAVIG--------EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIgdrVIIHSGAVIGS 72
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-211 1.57e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 45.69  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 103 AGFRVVPGAVAREGAYIAPGCVLmPSFVNI-GAYVGKGTMVDTWASIGScAQIGENCHISAG---AGIGGVlepmQANPT 178
Cdd:PRK14360  318 DGVKIGPYAHLRPEAQIGSNCRI-GNFVEIkKSQLGEGSKVNHLSYIGD-ATLGEQVNIGAGtitANYDGV----KKHRT 391

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2564886272 179 IIGDNCFIGARSEIVEGVIVGEGSVVAMGVFIT 211
Cdd:PRK14360  392 VIGDRSKTGANSVLVAPITLGEDVTVAAGSTIT 424
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-212 2.53e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.10  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 106 RVVPGAVAREGAYIApgcvlmpSFVNIG-AYVGKGTMVDTWASIGScAQIGENCHISAGAgIGGVLEPMQANPTIIGDNC 184
Cdd:PRK14356  335 RLRPGAVLEEGARVG-------NFVEMKkAVLGKGAKANHLTYLGD-AEIGAGANIGAGT-ITCNYDGVNKHRTVIGEGA 405

                          90       100
                  ....*....|....*....|....*...
gi 2564886272 185 FIGARSEIVEGVIVGEGSVVAMGVFITQ 212
Cdd:PRK14356  406 FIGSNTALVAPVTIGDGALVGAGSVITK 433
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 109-186 3.22e-05

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: 44.35  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVLMPsFVNIGAYV--GKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlEP----MQANPT--II 180
Cdd:cd03351     4 PTAIVDPGAKIGENVEIGP-FCVIGPNVeiGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGE--APqdlkYKGEPTrlEI 80


                  ....*.
gi 2564886272 181 GDNCFI 186
Cdd:cd03351    81 GDNNTI 86
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 136-228 4.28e-05

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: 43.55  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 136 VGKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlepmqanPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTK 215
Cdd:cd03352   117 IGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAG--------STTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVP 188

                          90
                  ....*....|...
gi 2564886272 216 ivyrdTGEVIGGH 228
Cdd:cd03352   189 -----PGEYVSGT 196
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-212 4.83e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.08  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 104 GFRVVPGAVAR-----EGAYIAPGCVLMP-----------------SFVNI-GAYVGKGTMVDTWASIGScAQIGENCHI 160
Cdd:PRK14353  286 GVTVASGAVIHafshlEGAHVGEGAEVGPyarlrpgaelgegakvgNFVEVkNAKLGEGAKVNHLTYIGD-ATIGAGANI 364

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2564886272 161 SAGA---GIGGVLEpmqaNPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQ 212
Cdd:PRK14353  365 GAGTitcNYDGFNK----HRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITE 415
PLN02694 PLN02694
serine O-acetyltransferase
 134-207 7.57e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.48  E-value: 7.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564886272 134 AYVGKGTMVD--TWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMG 207
Cdd:PLN02694  167 AKIGKGILFDhaTGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAG 242
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
109-186 1.13e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.39  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVlmpsfvnIGAYV--GKGTMVDTWASIGSCAQIGENCHISAGAGIGGV---L----EPMQanpTI 179
Cdd:PRK05289   13 PGAKIGENVEIGPFCV-------IGPNVviGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDpqdLkykgEPTR---LV 82


                  ....*..
gi 2564886272 180 IGDNCFI 186
Cdd:PRK05289   83 IGDNNTI 89
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 122-204 1.58e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 122 GCVLMPSFVNIGA------------YVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlepmqanPTIIGDNCFIGAR 189
Cdd:PRK00892  202 GRVIIGDDVEIGAnttidrgalddtVIGEGVKIDNLVQIAHNVVIGRHTAIAAQVGIAG--------STKIGRYCMIGGQ 273

                          90       100
                  ....*....|....*....|.
gi 2564886272 190 S------EIVEGVIVGEGSVV 204
Cdd:PRK00892  274 VgiaghlEIGDGVTITAMSGV 294
PLN02739 PLN02739
serine acetyltransferase
 133-226 1.81e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 42.33  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 133 GAYVGKGTMVD--TWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFI 210
Cdd:PLN02739  211 AARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLV 290

                          90
                  ....*....|....*....
gi 2564886272 211 TQ---STKIVYRDTGEVIG 226
Cdd:PLN02739  291 LKdvpSHSMVAGNPAKLIG 309
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
177-205 2.10e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.70  E-value: 2.10e-04
                          10        20
                  ....*....|....*....|....*....
gi 2564886272 177 PTIIGDNCFIGARSEIVEGVIVGEGSVVA 205
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 117-186 3.40e-04

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: 41.16  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPSfVNIGAY--------VGKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlEPM----QANPT--IIGD 182
Cdd:COG1043     8 AIVDPGAKLGEN-VEIGPFcvigpdveIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGE--EPQdlkyKGEPTrlEIGD 84


                  ....
gi 2564886272 183 NCFI 186
Cdd:COG1043    85 NNTI 88
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 130-205 5.42e-04

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: 40.77  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 130 VNIGA------------YVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlepmqanPTIIGDNCFIGARS------E 191
Cdd:COG1044   207 VEIGAnttidrgalgdtVIGDGTKIDNLVQIAHNVRIGEHTAIAAQVGIAG--------STKIGDNVVIGGQVgiaghlT 278

                          90
                  ....*....|....
gi 2564886272 192 IVEGVIVGEGSVVA 205
Cdd:COG1044   279 IGDGVIIGAQSGVT 292
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 121-216 5.65e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 41.27  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 121 PGCVLMPSFVN-IGAYVGKGTMVDT-WASIGSCAQIGENCHISAGAGIGGVL---EPMQANPTIIGDNCFIGARSEIVEG 195
Cdd:TIGR02353 584 RGTPFLPAILRlLGVKIGRGVYIDGtDLTERDLVTIGDDSTLNEGSVIQTHLfedRVMKSDTVTIGDGATLGPGAIVLYG 663

                          90       100
                  ....*....|....*....|.
gi 2564886272 196 VIVGEGSVVAMGVFITQSTKI 216
Cdd:TIGR02353 664 VVMGEGSVLGPDSLVMKGEEV 684
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 115-210 6.62e-04

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: 39.53  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVL-----MPSFVNIGAYVGKGTMVDTWAsiGSCAQIGENCHISAGAGIGGvlepmqanPTIIGDNCFIGAR 189
Cdd:cd00710    25 DNVFVGPGASIradegTPIIIGANVNIQDGVVIHALE--GYSVWIGKNVSIAHGAIVHG--------PAYIGDNCFIGFR 94

                          90       100
                  ....*....|....*....|.
gi 2564886272 190 SeIVEGVIVGEGSVVAMGVFI 210
Cdd:cd00710    95 S-VVFNAKVGDNCVIGHNAVV 114
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 102-210 9.36e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.62  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 102 DAGFRVVPGAVAREGAYIAPGCVLMPsFVNIGAY--VGKGTMVDTWASIG------------SCAQIGENCHISAGAGI- 166
Cdd:PRK12461   15 GSGVEIGPFAVIGANVEIGDGTWIGP-HAVILGPtrIGKNNKIHQGAVVGdepqdftykgeeSRLEIGDRNVIREGVTIh 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2564886272 167 -----GGVlepmqanpTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFI 210
Cdd:PRK12461   94 rgtkgGGV--------TRIGNDNLLMAYSHVAHDCQIGNNVILVNGALL 134
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 172-213 1.16e-03

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 39.09  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2564886272 172 PMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQS 213
Cdd:PRK09677  125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKS 166
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 135-205 1.25e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 38.72  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2564886272 135 YVGKGTMVDTWASIGSCAQIGENCHISAGAGIGGVlepmqanpTIIGDNCFIGARSEIVEgVIVGEGSVVA 205
Cdd:cd05636    19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGY--------TVLGDGCVVGNSVEVKN-SIIMDGTKVP 80
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 109-186 1.48e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.24  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 109 PGAVAREGAYIAPGCVLMPsFVNIGAYV--GKGTMVDTWASIGSCAQIGENCHISAGAGIGGvlEPM------QANPTII 180
Cdd:PRK12461    4 PTAVIDPSAKLGSGVEIGP-FAVIGANVeiGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQdftykgEESRLEI 80


                  ....*.
gi 2564886272 181 GDNCFI 186
Cdd:PRK12461   81 GDRNVI 86
PLN02357 PLN02357
serine acetyltransferase
 133-207 1.55e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 39.48  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564886272 133 GAYVGKGTMVD--TWASIGSCAQIGENCHISAGAGIGGVLEPMQANPTIIGDNCFIGARSEIVEGVIVGEGSVVAMG 207
Cdd:PLN02357  232 GAKIGQGILLDhaTGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAG 308
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 127-207 1.91e-03

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: 37.20  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 127 PSFVNIGAY--VGKGTMVDTWASIgscaQIGENCHISAGAGIGG-------VLEPMQANPTIIGDNCFIGARSEIVEGVI 197
Cdd:cd05825     1 PWNLTIGDNswIGEGVWIYNLAPV----TIGSDACISQGAYLCTgshdyrsPAFPLITAPIVIGDGAWVAAEAFVGPGVT 76

                          90
                  ....*....|
gi 2564886272 198 VGEGSVVAMG 207
Cdd:cd05825    77 IGEGAVVGAR 86
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 106-205 1.95e-03

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: 38.24  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 106 RVVPGAVAREGAYIAPGCVLMPS-------FVNIGAYVGKGTMVDTWASIGS------CAQIGENCHISAGAGI-GGVle 171
Cdd:TIGR03570  95 IVSPSASIGEGTVIMAGAVINPDvrigdnvIINTGAIVEHDCVIGDFVHIAPgvtlsgGVVIGEGVFIGAGATIiQGV-- 172

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2564886272 172 pmqanptIIGDNCFIGARSEIVEGviVGEGSVVA 205
Cdd:TIGR03570 173 -------TIGAGAIVGAGAVVTKD--IPDGGVVV 197
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 115-204 2.08e-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: 36.07  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 115 EGAYIAPGCVLMPSFVNIGAYVGKGTMVDTwaSIgscaqIGENCHISAGAGIggvlepmqaNPTIIGDNCFIGARSEIVE 194
Cdd:cd03356     4 ESTVIGENAIIKNSVIGDNVRIGDGVTITN--SI-----LMDNVTIGANSVI---------VDSIIGDNAVIGENVRVVN 67

                          90
                  ....*....|
gi 2564886272 195 GVIVGEGSVV 204
Cdd:cd03356    68 LCIIGDDVVV 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 179-216 3.69e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2564886272 179 IIGDNCFIGARSEIVEGVIVGEGSVVAMGVFITQSTKI 216
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKI 151
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-244 4.58e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.27  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 156 ENCHISAGAGIGG--VLEP---MQANpTIIGDNCFIGARSEIVEgvivgegSVVAMGVFITQSTkIVYRDTGEviGGHIP 230
Cdd:PRK14354  258 ESTYIDADVEIGSdtVIEPgvvIKGN-TVIGEDCVIGPGSRIVD-------STIGDGVTITNSV-IEESKVGD--NVTVG 326

                          90
                  ....*....|....
gi 2564886272 231 PYSVVVPGTMPGKD 244
Cdd:PRK14354  327 PFAHLRPGSVIGEE 340
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 117-212 5.52e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMpSFVNIGAYV-------GKGTMVDTWASIGScAQIGENCHISAGAgIGGVLEPMQANPTIIGDNCFIGAR 189
Cdd:PRK14355  333 AHLRPGTELS-AHVKIGNFVetkkivmGEGSKASHLTYLGD-ATIGRNVNIGCGT-ITCNYDGVKKHRTVIEDDVFVGSD 409

                          90       100
                  ....*....|....*....|...
gi 2564886272 190 SEIVEGVIVGEGSVVAMGVFITQ 212
Cdd:PRK14355  410 VQFVAPVTVGRNSLIAAGTTVTK 432
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
152-188 6.25e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 6.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2564886272 152 AQIGENCHISAGAGIGGvlepmqanPTIIGDNCFIGA 188
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGG--------GVIIGDNVIIGA 30
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 140-204 6.61e-03

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: 36.63  E-value: 6.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2564886272 140 TMVDTWASIGSCAQIGENCHISAGAGIGG--VLEPM-QANPTIIGDNCFIGARSeIVEGVIVGEGSVV 204
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVILEGKTVIGEdcVIGPNcVIKDSTIGDGVVIKASS-VIEGAVIGNGATV 76
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 117-215 7.42e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.28  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564886272 117 AYIAPGCVLMPS----FVNIGAYVGKGTMVDTWASIGSCaQIGENCHISAGAgIGGVLEPMQANPTIIGDNCFIGARSEI 192
Cdd:PRK14359  305 AHIRPKSEIKNThignFVETKNAKLNGVKAGHLSYLGDC-EIDEGTNIGAGT-ITCNYDGKKKHKTIIGKNVFIGSDTQL 382

                          90       100
                  ....*....|....*....|...
gi 2564886272 193 VEGVIVGEGSVVAMGVFITQSTK 215
Cdd:PRK14359  383 VAPVNIEDNVLIAAGSTVTKDVP 405
 
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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