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Conserved domains on  [gi|1624566576|ref|WP_136409619|]
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MULTISPECIES: gamma carbonic anhydrase family protein [Muribaculaceae]

Protein Classification

gamma carbonic anhydrase family protein( domain architecture ID 11429531)

gamma carbonic anhydrase family protein is a hexapeptide repeat protein similar to carnitine operon protein CaiE and phenylacetic acid degradation protein PaaY, which are involved in amine/polyamine and aromatic compound metabolism, respectively

CATH:  2.160.10.10
EC:  4.2.1.-
Gene Ontology:  GO:0046872
PubMed:  15500694|11747907|11696553|10611359
SCOP:  4002848

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-173 3.78e-81

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 238.00  E-value: 3.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   4 IKSVRGYTPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIG 83
Cdd:COG0663     3 IYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLT-IGDDVTIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  84 HNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEINRkIAKNYL 163
Cdd:COG0663    82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE-SAENYV 160

                         170
                  ....*....|
gi 1624566576 164 MYSTWYDAEL 173
Cdd:COG0663   161 ELARRYLAEL 170
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-173 3.78e-81

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 238.00  E-value: 3.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   4 IKSVRGYTPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIG 83
Cdd:COG0663     3 IYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLT-IGDDVTIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  84 HNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEINRkIAKNYL 163
Cdd:COG0663    82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE-SAENYV 160

                         170
                  ....*....|
gi 1624566576 164 MYSTWYDAEL 173
Cdd:COG0663   161 ELARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 13-166 2.77e-75

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: 222.67  E-value: 2.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIGHNVTIHGAK 92
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTI-IGDNVTVGHGAVLHGCT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  93 IHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEInRKIAKNYLMYS 166
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAEL-RESAEHYVELA 152
PLN02296 PLN02296
carbonate dehydratase
 11-162 4.59e-48

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 157.59  E-value: 4.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  11 TPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTlyQKSTIE-------IGDDVSIG 83
Cdd:PLN02296   52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHV--AKTNLSgkvlptiIGDNVTIG 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  84 HNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEINrKIAKNY 162
Cdd:PLN02296  130 HSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFIS-QSATNY 207
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 52-141 2.38e-08

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: 52.83  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  52 KIGNRVniqdgsVLHTLYQKST--IEIGDDVSIGHNVTIHGAK------------IHDFALIGMGAVVMDDAEVGEGALV 117
Cdd:TIGR02353 114 KIGKGV------DIGSLPPVCTdlLTIGAGTIVRKEVMLLGYRaergrlhtgpvtLGRDAFIGTRSTLDIDTSIGDGAQL 187

                          90       100
                  ....*....|....*....|....
gi 1624566576 118 AAGSVVLSRTKIGPNELWGGAPAK 141
Cdd:TIGR02353 188 GHGSALQGGQSIPDGERWHGSPAQ 211
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
12-39 5.52e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1624566576  12 PEIGKNCFLADNCTIIGDVVMGDDCSIW 39
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-173 3.78e-81

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 238.00  E-value: 3.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   4 IKSVRGYTPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIG 83
Cdd:COG0663     3 IYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLT-IGDDVTIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  84 HNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEINRkIAKNYL 163
Cdd:COG0663    82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE-SAENYV 160

                         170
                  ....*....|
gi 1624566576 164 MYSTWYDAEL 173
Cdd:COG0663   161 ELARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 13-166 2.77e-75

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: 222.67  E-value: 2.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIGHNVTIHGAK 92
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTI-IGDNVTVGHGAVLHGCT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  93 IHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEInRKIAKNYLMYS 166
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAEL-RESAEHYVELA 152
PLN02296 PLN02296
carbonate dehydratase
 11-162 4.59e-48

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 157.59  E-value: 4.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  11 TPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTlyQKSTIE-------IGDDVSIG 83
Cdd:PLN02296   52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHV--AKTNLSgkvlptiIGDNVTIG 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  84 HNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEINrKIAKNY 162
Cdd:PLN02296  130 HSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFIS-QSATNY 207
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 12-163 9.70e-38

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: 127.30  E-value: 9.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  12 PEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYqKSTIEIGDDVSIGHNVTIHGA 91
Cdd:cd04650     1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDH-GYPTEIGDYVTIGHNAVVHGA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624566576  92 KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDpEQSKEINRKIAKNYL 163
Cdd:cd04650    80 KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLT-EEEIEWIKKNAEEYV 150
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 12-159 1.77e-36

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: 124.40  E-value: 1.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  12 PEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIGHNVTIHGA 91
Cdd:cd04745     1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTV-LEENGHIGHGAILHGC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566576  92 KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEqskEINRKIA 159
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDE---EVAWKTR 144
PLN02472 PLN02472
uncharacterized protein
 4-174 1.34e-27

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 103.89  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   4 IKSVRGYTPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKST-----IEIGD 78
Cdd:PLN02472   52 IIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTglpaeTLIDR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  79 DVSIGHNVTIHGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMVDPEQSKEIN--- 155
Cdd:PLN02472  132 YVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEIPkla 211

                         170       180
                  ....*....|....*....|....*.
gi 1624566576 156 ---RKIAKNY----LMYSTWYdAELE 174
Cdd:PLN02472  212 vaiNDLSQSHfsefLPYSTAY-LEVE 236
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
26-150 5.48e-24

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 91.86  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  26 IIGDVVMGDDCSIWFNTVLRGdvNSIKIGNRVNIQDGSvlhTLYQKSTIEIGDDVSIGHNVTIHGA-------------- 91
Cdd:COG0110     5 LLFGARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGV---TIDDPGGITIGDNVLIGPGVTILTGnhpiddpatfplrt 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624566576  92 ---KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVlsrTK-IGPNELWGGAPAKFIKMVDPEQ 150
Cdd:COG0110    80 gpvTIGDDVWIGAGATILPGVTIGDGAVVGAGSVV---TKdVPPYAIVAGNPARVIRKRDEEE 139
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 9-146 3.79e-22

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 88.33  E-value: 3.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   9 GYTPEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIeIGDDVSIGHNVTI 88
Cdd:PRK13627    8 GLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTI-VGENGHIGHGAIL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566576  89 HGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKMV 146
Cdd:PRK13627   87 HGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSV 144
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 12-129 5.24e-22

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: 87.30  E-value: 5.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  12 PEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDV-NSIKIGNRVNIQDGSVLHTLYQKStIEIGDDVSIGHNVTIHG 90
Cdd:cd00710     3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEgTPIIIGANVNIQDGVVIHALEGYS-VWIGKNVSIAHGAIVHG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566576  91 ------------------AKIHDFALIGMGAVVmDDAEVGEGALVAAGSVVLSRTKI 129
Cdd:cd00710    82 payigdncfigfrsvvfnAKVGDNCVIGHNAVV-DGVEIPPGRYVPAGAVITSQTQA 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 50-143 2.91e-20

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: 80.96  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  50 SIKIGNRVNIQDGSVLHTlyqKSTIEIGDDVSIGHNVTIHGA--------------------KIHDFALIGMGAVVMDDA 109
Cdd:cd04647     1 NISIGDNVYIGPGCVISA---GGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVVILPGV 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1624566576 110 EVGEGALVAAGSVVlsrTK-IGPNELWGGAPAKFI 143
Cdd:cd04647    78 TIGDGAVVGAGSVV---TKdVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 33-144 3.78e-19

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: 78.70  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  33 GDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSvlhTLYQKSTIEigDDVSIGHNVT----------------IHGAKIHDF 96
Cdd:cd03358     2 GDNCIIGTNVFIENDV---KIGDNVKIQSNV---SIYEGVTIE--DDVFIGPNVVftndlyprskiyrkweLKGTTVKRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1624566576  97 ALIGMGAVVMDDAEVGEGALVAAGSVVlsrTK-IGPNELWGGAPAKFIK 144
Cdd:cd03358    74 ASIGANATILPGVTIGEYALVGAGAVV---TKdVPPYALVVGNPARIIG 119
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 22-162 1.27e-16

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: 73.02  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  22 DNCTIIGDVVMGDDCsiwfntVLRGDVNSIKIGNRVNIQDGSVLHTLYQKSTIE-------IGDDVSIGHNVTIHGAKIH 94
Cdd:cd03359    20 QNIVLNGKTIIQSDV------IIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGvaffplhIGDYVFIGENCVVNAAQIG 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566576  95 DFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPAKFIKmVDPEQSKEINRKIAKNY 162
Cdd:cd03359    94 SYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIG-ELPECTQELMEEETKEY 160
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 13-141 1.54e-15

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: 71.29  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVL--------------HTLYQKSTIEIGD 78
Cdd:cd03352    21 VIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC---IIGDRVIIHSGAVIgsdgfgfapdgggwVKIPQLGGVIIGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  79 DVSIGHNVTIH-----------GAKI-------H-----------------------DFALIGMGAVVMDDAEVGEGALV 117
Cdd:cd03352    98 DVEIGANTTIDrgalgdtvigdGTKIdnlvqiaHnvrigencliaaqvgiagsttigDNVIIGGQVGIAGHLTIGDGVVI 177

                         170       180
                  ....*....|....*....|....
gi 1624566576 118 AAGSVVLSRTKigPNELWGGAPAK 141
Cdd:cd03352   178 GAGSGVTSIVP--PGEYVSGTPAQ 199
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 13-141 1.79e-15

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 72.86  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVL--------------HTLYQKSTIEIGD 78
Cdd:PRK00892  132 VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV---RIGNRVIIHSGAVIgsdgfgfandrggwVKIPQLGRVIIGD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  79 DVSIG----------------------------HNVTI--H-----------GAKIHDFALIGMGAVVMDDAEVGEGALV 117
Cdd:PRK00892  209 DVEIGanttidrgalddtvigegvkidnlvqiaHNVVIgrHtaiaaqvgiagSTKIGRYCMIGGQVGIAGHLEIGDGVTI 288

                         170       180
                  ....*....|....*....|....
gi 1624566576 118 AAGSVVLSRTKiGPNELWGGAPAK 141
Cdd:PRK00892  289 TAMSGVTKSIP-EPGEYSSGIPAQ 311
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-141 2.36e-14

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: 69.66  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVL---------------HTLYQKSTIEIG 77
Cdd:COG1044   128 VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC---VIGDRVIIHSGAVIgadgfgfapdedggwVKIPQLGRVVIG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  78 DDVSIG----------------------------HNVTI--H-----------GAKIHDFALIGMGAVVMDDAEVGEGAL 116
Cdd:COG1044   205 DDVEIGanttidrgalgdtvigdgtkidnlvqiaHNVRIgeHtaiaaqvgiagSTKIGDNVVIGGQVGIAGHLTIGDGVI 284

                         170       180
                  ....*....|....*....|....*
gi 1624566576 117 VAAGSVVLSrtKIGPNELWGGAPAK 141
Cdd:COG1044   285 IGAQSGVTK--SIPEGGVYSGSPAQ 307
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 13-145 2.49e-12

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: 61.41  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIgdvvMGDDCSIWFNTVlRGDVNSIKIGNRVNIQDGsvlhtLYQKSTIEIGDDVSIGHNVTIhgak 92
Cdd:cd03349    23 SIGKFCSIAPGVKIG----LGGNHPTDWVST-YPFYIFGGEWEDDAKFDD-----WPSKGDVIIGNDVWIGHGATI---- 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  93 ihdfaligmgavvMDDAEVGEGALVAAGSVVlsrTK-IGPNELWGGAPAKFIKM 145
Cdd:cd03349    89 -------------LPGVTIGDGAVIAAGAVV---TKdVPPYAIVGGNPAKVIRY 126
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 30-106 2.75e-12

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: 59.57  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  30 VVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLHTLY---QKSTIEIGDDVSIGHNVTIHG-AKIHDFALIGMGAVV 105
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPV---VIGDNVNIGPGAVIGAATgpnEKNPTIIGDNVEIGANAVIHGgVKIGDNAVIGAGAVV 77


                  .
gi 1624566576 106 M 106
Cdd:cd00208    78 T 78
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 13-139 5.69e-12

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: 61.35  E-value: 5.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsikignrvniqdgsvlhtlyqkstiEIGDDVSIGHNVTIHG-A 91
Cdd:cd03360    98 VIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDC--------------------------VIGDFVHIAPGVVLSGgV 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1624566576  92 KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRtkIGPNELWGGAP 139
Cdd:cd03360   152 TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKD--VPDGSVVVGNP 197
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 9-143 1.29e-11

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: 60.13  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   9 GYTPEIGKNCFLADNCTIIgdvvmgddcsiwfntvlrgDVNSIKIGNRVNIQDGSVLHTLY-------QKSTIEIGDDVS 81
Cdd:cd03357    60 GYNIHIGDNFYANFNCTIL-------------------DVAPVTIGDNVLIGPNVQIYTAGhpldpeeRNRGLEYAKPIT 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624566576  82 IGHNVtihgakihdfaLIGMGAVVMDDAEVGEGALVAAGSVVlsrTK-IGPNELWGGAPAKFI 143
Cdd:cd03357   121 IGDNV-----------WIGGGVIILPGVTIGDNSVIGAGSVV---TKdIPANVVAAGNPARVI 169
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 13-132 7.22e-10

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: 55.50  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsikIGNRVNIQDGSVLHtlyqksTIEIGDDVSIG-------HN 85
Cdd:cd03353    17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDST----IGDGVVIKASSVIE------GAVIGNGATVGpfahlrpGT 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  86 VTIHGAKIHDF-----ALIGMGAVV-----MDDAEVGEGALVAAGSVVL-------SRTKIGPN 132
Cdd:cd03353    87 VLGEGVHIGNFveikkSTIGEGSKAnhlsyLGDAEIGEGVNIGAGTITCnydgvnkHRTVIGDN 150
PLN02739 PLN02739
serine acetyltransferase
 73-162 8.08e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 56.97  E-value: 8.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  73 TIEIGDDVSIGHNVTIHGA---------KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSrtKIGPNELWGGAPAKFI 143
Cdd:PLN02739  231 TAVIGDRVSILHGVTLGGTgketgdrhpKIGDGALLGACVTILGNISIGAGAMVAAGSLVLK--DVPSHSMVAGNPAKLI 308

                          90       100
                  ....*....|....*....|....*...
gi 1624566576 144 KMVDPEQ---------SKEINRKIAKNY 162
Cdd:PLN02739  309 GFVDEQDpsltmeydaTREFFQNVAVAY 336
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 75-132 1.33e-09

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: 56.18  E-value: 1.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  75 EIGDDVSIGHNVTIH-GAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:COG1044   110 KIGEGVSIGPFAVIGaGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDR 168
PLN02694 PLN02694
serine O-acetyltransferase
 73-141 1.46e-09

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 55.80  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  73 TIEIGDDVSIGHNVTIHGA---------KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVL-----SRTKIG-PNELWGG 137
Cdd:PLN02694  186 TAVIGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLidvppRTTAVGnPARLVGG 265


                  ....*.
gi 1624566576 138 --APAK 141
Cdd:PLN02694  266 keKPAK 271
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 75-132 4.16e-09

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: 53.57  E-value: 4.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  75 EIGDDVSIGHNVTIH-GAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:cd03352     3 KIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDR 61
PLN02357 PLN02357
serine acetyltransferase
 73-143 5.27e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.50  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  73 TIEIGDDVSIGHNVTIHGA---------KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSrtKIGPNELWGGAPAKFI 143
Cdd:PLN02357  252 TAVVGNNVSILHNVTLGGTgkqsgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLK--DVPPRTTAVGNPARLI 329
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 76-132 9.54e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 9.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566576  76 IGDDVSIGHNVTI-HGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:PRK00892  115 IGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNR 172
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-132 1.81e-08

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: 53.11  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRgdvNSiKIGNRVNIQ----DGSVLHtlyQKSTI----------EIGD 78
Cdd:COG1207   268 EIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK---DS-TIGDGVVIKysviEDAVVG---AGATVgpfarlrpgtVLGE 340

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566576  79 DVSIGH-----NVTIH-GAKIHDFALIGmgavvmdDAEVGEGALVAAGSVVL-------SRTKIGPN 132
Cdd:COG1207   341 GVKIGNfvevkNSTIGeGSKVNHLSYIG-------DAEIGEGVNIGAGTITCnydgvnkHRTVIGDG 400
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 52-124 2.00e-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: 51.24  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  52 KIGNRVNIQDGS--VLHtlyqkSTIEIGDDVSIGHNVTIhGA----------KIHDFALIGMGAVVMDDAEVGEGALVAA 119
Cdd:COG1045    73 TIGRGFFIDHGTgvVIG-----ETAVIGDNVTIYQGVTL-GGtgkekgkrhpTIGDNVVIGAGAKILGPITIGDNAKIGA 146


                  ....*
gi 1624566576 120 GSVVL 124
Cdd:COG1045   147 NSVVL 151
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 22-112 2.03e-08

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: 52.72  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  22 DNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLhtlyqKSTiEIGDDVSIgHNVTIHGAKIHDFALIG- 100
Cdd:COG1207   259 ATTYIDGDVEIGRDVVIDPNVILEGKT---VIGEGVVIGPNCTL-----KDS-TIGDGVVI-KYSVIEDAVVGAGATVGp 328

                          90
                  ....*....|....*..
gi 1624566576 101 -----MGAVVMDDAEVG 112
Cdd:COG1207   329 farlrPGTVLGEGVKIG 345
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 52-141 2.38e-08

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: 52.83  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  52 KIGNRVniqdgsVLHTLYQKST--IEIGDDVSIGHNVTIHGAK------------IHDFALIGMGAVVMDDAEVGEGALV 117
Cdd:TIGR02353 114 KIGKGV------DIGSLPPVCTdlLTIGAGTIVRKEVMLLGYRaergrlhtgpvtLGRDAFIGTRSTLDIDTSIGDGAQL 187

                          90       100
                  ....*....|....*....|....
gi 1624566576 118 AAGSVVLSRTKIGPNELWGGAPAK 141
Cdd:TIGR02353 188 GHGSALQGGQSIPDGERWHGSPAQ 211
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-132 2.43e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 52.53  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLrgdVNSiKIGNRVNIQDGSVLHTlyqkstiEIGDDVSIGHNVTIH--- 89
Cdd:PRK14354  267 EIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI---VDS-TIGDGVTITNSVIEES-------KVGDNVTVGPFAHLRpgs 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  90 ----GAKIHDF-----ALIGMGAVV-----MDDAEVGEGALVAAGSVVLS-------RTKIGPN 132
Cdd:PRK14354  336 vigeEVKIGNFveikkSTIGEGTKVshltyIGDAEVGENVNIGCGTITVNydgknkfKTIIGDN 399
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 21-112 4.31e-08

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: 50.88  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  21 ADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLhtlyqKSTIeIGDDVSIGHNVTIHGAKIHDFALIG 100
Cdd:cd03353     7 PETTYIDGDVEIGVDVVIDPGVILEGKT---VIGEDCVIGPNCVI-----KDST-IGDGVVIKASSVIEGAVIGNGATVG 77

                          90
                  ....*....|....*...
gi 1624566576 101 ------MGAVVMDDAEVG 112
Cdd:cd03353    78 pfahlrPGTVLGEGVHIG 95
cysE PRK11132
serine acetyltransferase; Provisional
 73-143 6.47e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 50.85  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  73 TIEIGDDVSIGHNVTIHGA---------KIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSrtKIGPNELWGGAPAKFI 143
Cdd:PRK11132  167 TAVIENDVSILQSVTLGGTgktsgdrhpKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQ--PVPPHTTAAGVPARIV 244
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 13-118 1.24e-07

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 49.41  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLhtlyqKSTIEIGDDVSIGHNVTI-HGA 91
Cdd:TIGR03570 101 SIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDC---VIGDFVHIAPGVTL-----SGGVVIGEGVFIGAGATIiQGV 172

                          90       100
                  ....*....|....*....|....*..
gi 1624566576  92 KIHDFALIGMGAVVMDDaeVGEGALVA 118
Cdd:TIGR03570 173 TIGAGAIVGAGAVVTKD--IPDGGVVV 197
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 52-125 1.73e-07

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: 47.43  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  52 KIGNRVNIQDGS--VLHtlyqkSTIEIGDDVSIGHNVTIHG---------AKIHDFALIGMGAVVMDDAEVGEGALVAAG 120
Cdd:cd03354    10 KIGPGLFIDHGTgiVIG-----ETAVIGDNCTIYQGVTLGGkgkgggkrhPTIGDNVVIGAGAKILGNITIGDNVKIGAN 84


                  ....*
gi 1624566576 121 SVVLS 125
Cdd:cd03354    85 AVVTK 89
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 13-123 7.55e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 47.71  E-value: 7.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVL---------RGDVNSIKIGNRVNIQDGSVLHTLYQKSTI-EIGDD--- 79
Cdd:PRK12461   31 EIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHRGTKGGGVtRIGNDnll 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  80 ---VSIGHNVTI-------HGA------KIHDFALIGMGAVVMDDAEVGEGALVAAGSVV 123
Cdd:PRK12461  111 maySHVAHDCQIgnnvilvNGAllaghvTVGDRAIISGNCLVHQFCRIGALAMMAGGSRI 170
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 39-140 8.22e-07

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: 48.21  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  39 WFNTVLRGdvNSIKIGNRVNIqDGSvlhTLYQKSTIEIGDDVSIGHNVTIH------------GAKIHDFALIGMGAVVM 106
Cdd:TIGR02353 588 FLPAILRL--LGVKIGRGVYI-DGT---DLTERDLVTIGDDSTLNEGSVIQthlfedrvmksdTVTIGDGATLGPGAIVL 661

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1624566576 107 DDAEVGEGALVAAGSVVLSRTKIGPNELWGGAPA 140
Cdd:TIGR02353 662 YGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNPA 695
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 53-143 1.51e-06

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: 44.90  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  53 IGNRVNIQDGSVLHTLyqkstieigDDVSIGHNVTI-HGAKI----HDF-----------------ALIGMGAVVMDDAE 110
Cdd:cd05825     6 IGDNSWIGEGVWIYNL---------APVTIGSDACIsQGAYLctgsHDYrspafplitapivigdgAWVAAEAFVGPGVT 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1624566576 111 VGEGALVAAGSVVLsrTKIGPNELWGGAPAKFI 143
Cdd:cd05825    77 IGEGAVVGARSVVV--RDLPAWTVYAGNPAVPV 107
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 14-134 4.05e-06

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: 44.89  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  14 IGKNCFLADNCTIIGDVVMGDDCSIWF-----NTVLRGDVN---------SIkIGNRVNIQDGSVLHTL-YQKSTIEigd 78
Cdd:cd05636    38 IGKGCEIGPNAYIRGYTVLGDGCVVGNsvevkNSIIMDGTKvphlnyvgdSV-LGENVNLGAGTITANLrFDDKPVK--- 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1624566576  79 dvsighnVTIHGAKIhDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPNEL 134
Cdd:cd05636   114 -------VRLKGERV-DTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCV 161
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 53-131 5.40e-06

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: 42.57  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  53 IGNRVNIQDGSVLhtlyqKSTIeIGDDVSIGHNVTIHGAKIHDFALIGMGA-----VVMDDAEVGEGALVAAGSVVLSRT 127
Cdd:cd05787     2 IGRGTSIGEGTTI-----KNSV-IGRNCKIGKNVVIDNSYIWDDVTIEDGCtihhsIVADGAVIGKGCTIPPGSLISFGV 75


                  ....
gi 1624566576 128 KIGP 131
Cdd:cd05787    76 VIGD 79
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-132 1.78e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 41.47  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  51 IKIGNRVNIQDGSVLhtlyqKSTIEIGDDVSIGHNVTIHGAkihDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIG 130
Cdd:cd00208     1 VFIGEGVKIHPKAVI-----RGPVVIGDNVNIGPGAVIGAA---TGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIG 72


                  ..
gi 1624566576 131 PN 132
Cdd:cd00208    73 AG 74
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-83 2.01e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.96  E-value: 2.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGdvnsIKIGNRVNIQDGSVLhtlyqkSTIEIGDDVSIG 83
Cdd:PRK14355  270 VIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG----CRIGDDVTVKAGSVL------EDSVVGDDVAIG 330
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 76-132 5.60e-05

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: 42.70  E-value: 5.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566576  76 IGDDVSIGHNVTIhGAkihdfaligmGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:COG1044   105 IDPSAKIGEGVSI-GP----------FAVIGAGVVIGDGVVIGPGVVIGDGVVIGDD 150
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 13-89 1.57e-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: 40.88  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLHTLYQ-------KSTIEIGDDVSIGHN 85
Cdd:cd03351    13 KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPT---TIGKNNRIFPFASIGEAPQdlkykgePTRLEIGDNNTIREF 89


                  ....
gi 1624566576  86 VTIH 89
Cdd:cd03351    90 VTIH 93
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-132 1.61e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.45  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  14 IGKNCF-----LADNCTIIGDVV----MGDDCSIWFNTVLRGDVN---SIKIGNRVNI------QDGSVLHTLYQKSTiE 75
Cdd:PRK14360  289 IGPGSLiensqIGENVTVLYSVVsdsqIGDGVKIGPYAHLRPEAQigsNCRIGNFVEIkksqlgEGSKVNHLSYIGDA-T 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624566576  76 IGDDVSIGHNvTI---------HGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVlsrTKIGPN 132
Cdd:PRK14360  368 LGEQVNIGAG-TItanydgvkkHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTI---TKDVPD 429
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 13-132 1.63e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIigdvvmGDDCSIWFNTVLRGdvnSIKIGNRVNIQDGSVLHTLYQ-------KSTIEIGDDVSIGHN 85
Cdd:PRK12461   19 EIGPFAVIGANVEI------GDGTWIGPHAVILG---PTRIGKNNKIHQGAVVGDEPQdftykgeESRLEIGDRNVIREG 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  86 VTIH-GAKIHDFALIGMGAVVMD------DAEVGE------GALVAAGSVVLSRTKIGPN 132
Cdd:PRK12461   90 VTIHrGTKGGGVTRIGNDNLLMAyshvahDCQIGNnvilvnGALLAGHVTVGDRAIISGN 149
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
13-89 1.68e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.85  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLHTLYQ-------KSTIEIGDDVSIGHN 85
Cdd:PRK05289   16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHT---TIGKNNRIFPFASIGEDPQdlkykgePTRLVIGDNNTIREF 92


                  ....
gi 1624566576  86 VTIH 89
Cdd:PRK05289   93 VTIN 96
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 76-131 1.70e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624566576  76 IGDDVSIGHNVTIH-GAKIHDFALIGMGAVV-----MDDAEVGEGALV----AAGSVVLSRTKIGP 131
Cdd:PRK14352  268 IDVDVTIGRDVVIHpGTQLLGRTTIGEDAVVgpdttLTDVTVGEGASVvrthGSESEIGAGATVGP 333
PRK10502 PRK10502
putative acyl transferase; Provisional
 53-145 1.76e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 40.32  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  53 IGNRVNIQDGSVLHTLYQkstIEIGDDVSIGHNVTI----HGAKIHDFAL------IGMGAVVMDDA------EVGEGAL 116
Cdd:PRK10502   74 IGDYAWIGDDVWLYNLGE---ITIGAHCVISQKSYLctgsHDYSDPHFDLntapivIGEGCWLAADVfvapgvTIGSGAV 150

                          90       100
                  ....*....|....*....|....*....
gi 1624566576 117 VAAGSVVLsrTKIGPNELWGGAPAKFIKM 145
Cdd:PRK10502  151 VGARSSVF--KSLPANTICRGNPAVPIRP 177
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 13-89 2.08e-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: 40.77  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLHTLYQ-------KSTIEIGDDVSIGHN 85
Cdd:COG1043    15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPT---TIGKNNRIFPFASIGEEPQdlkykgePTRLEIGDNNTIREF 91


                  ....
gi 1624566576  86 VTIH 89
Cdd:COG1043    92 VTIH 95
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 16-128 2.93e-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: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  16 KNCFLADNC-----TIIGDVVMGDDCSIWFNTVLR-----------GDVNSIK--------------------IGNRVNI 59
Cdd:PRK09451  299 KNCVIGDDCeispySVVEDANLGAACTIGPFARLRpgaelaegahvGNFVEMKkarlgkgskaghltylgdaeIGDNVNI 378

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624566576  60 QDGsVLHTLY---QKSTIEIGDDVSIGHNVT-IHGAKIHDFALIGMGAVVMDDaevgegalVAAGSVVLSRTK 128
Cdd:PRK09451  379 GAG-TITCNYdgaNKFKTIIGDDVFVGSDTQlVAPVTVGKGATIGAGTTVTRD--------VAENELVISRVP 442
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-117 2.99e-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: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  28 GDVVMGDDCSIWFNTVLRGDVnsiKIGNRVNIQDGSVLhtlyqkSTIEIGDDVSIGHNVTIHGAKIHDFALIGMGAVVMD 107
Cdd:PRK09451  264 GTLTHGRDVEIDTNVIIEGNV---TLGNRVKIGAGCVL------KNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRP 334

                          90
                  ....*....|
gi 1624566576 108 DAEVGEGALV 117
Cdd:PRK09451  335 GAELAEGAHV 344
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 72-129 4.21e-04

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: 38.90  E-value: 4.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566576  72 STIEIGDDVSIGHNVTIHG---------AKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKI 129
Cdd:cd03350    48 SCAQIGKNVHLSAGAVIGGvleplqatpVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPI 114
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 76-138 4.66e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 4.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  76 IGDDVSIGHNVTIhgakihdfaliGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN-ELWGGA 138
Cdd:PRK00892  109 IDPSAKIGEGVSI-----------GPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADcRLHANV 161
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 80-132 4.82e-04

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: 39.40  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  80 VSIGHN------VTIHGAKIHDFA-LIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:TIGR03570  64 VAIGDNklrrrlVEKLKAKGYRFAtLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDN 123
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 14-124 6.30e-04

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 37.42  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  14 IGKNCFLADNCTIIGDVVMGddcsiwfNTVLRGDVNSIKIGNRVNIQDGSVLhtlyqkstieIGdDVSIGHNVTihgaki 93
Cdd:cd03354    25 IGETAVIGDNCTIYQGVTLG-------GKGKGGGKRHPTIGDNVVIGAGAKI----------LG-NITIGDNVK------ 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1624566576  94 hdfalIGMGAVVMDDaevgegalVAAGSVVL 124
Cdd:cd03354    81 -----IGANAVVTKD--------VPANSTVV 98
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-123 1.09e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.98  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  13 EIG-----KNCFLADNCTII-----GDVVMgDDCSIW-FNTVLRGDV--NSIKIGNRVNIQDGSV------LHTLYQKST 73
Cdd:PRK14357  281 EIGpmtriVDCEIGNNVKIIrseceKSVIE-DDVSVGpFSRLREGTVlkKSVKIGNFVEIKKSTIgentkaQHLTYLGDA 359

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  74 IeIGDDVSIGHNvTI---------HGAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVV 123
Cdd:PRK14357  360 T-VGKNVNIGAG-TItcnydgkkkNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVI 416
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-130 1.14e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.96  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  29 DVVMGDDCSIWFNTVLRGDVnsikignrvniqdgsvlhtlyqkstiEIGDDVSIGHNVTIHGAKIHDFALIGMGAV---- 104
Cdd:PRK14355  268 GVVIGRDTTIYPGVCISGDT--------------------------RIGEGCTIEQGVVIKGCRIGDDVTVKAGSVleds 321

                          90       100
                  ....*....|....*....|....*..
gi 1624566576 105 -VMDDAEVGEGALVAAGSVVLSRTKIG 130
Cdd:PRK14355  322 vVGDDVAIGPMAHLRPGTELSAHVKIG 348
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 13-91 1.73e-03

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 38.01  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566576  13 EIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVNSIKIGNrvniqdgsvlhtlyQKSTIEIGDDVSIGHNVTIHGA 91
Cdd:TIGR01852  30 KIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKG--------------EKTRLIIGDNNTIREFVTINRG 94
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 91-132 1.81e-03

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: 37.77  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1624566576  91 AKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDD 43
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 16-130 1.87e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.93  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  16 KNCFLADNCTIIGDVvmgddcsiwFNTVLRGDVnsiKIGNRVNIQDgSVLHTlyqkstieigdDVSIGHNVTIHGakihd 95
Cdd:PRK05293  292 KNSLVVEGCVVYGTV---------EHSVLFQGV---QVGEGSVVKD-SVIMP-----------GAKIGENVVIER----- 342

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1624566576  96 fALIGMGAVVMDDAEVGEG----ALVAAGSVVLSRTKIG 130
Cdd:PRK05293  343 -AIIGENAVIGDGVIIGGGkeviTVIGENEVIGVGTVIG 380
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 8-108 1.99e-03

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: 37.80  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576   8 RGYTpEIGKNCFLADNCTIIGDVVMGDDCSIWFNTVLRGDVnsikignrvniqdgsvlhtlyqkstiEIGDDVSIGHNVT 87
Cdd:cd03351   100 GGVT-RIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHV--------------------------EIGDYAIIGGLSA 152

                          90       100
                  ....*....|....*....|..
gi 1624566576  88 IHG-AKIHDFALIGMGAVVMDD 108
Cdd:cd03351   153 VHQfCRIGRHAMVGGGSGVVQD 174
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 22-130 2.06e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.99  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  22 DNCTIIGDVVMGDDCSIWFNTVLRGdvnSIKIGNRVNIQDGSVLhtlyqkstieigDDVSIGHNVTIHGAKIHDfaligm 101
Cdd:PRK14360  255 ASCTISETVELGPDVIIEPQTHLRG---NTVIGSGCRIGPGSLI------------ENSQIGENVTVLYSVVSD------ 313

                          90       100
                  ....*....|....*....|....*....
gi 1624566576 102 gAVVMDDAEVGEGALVAAGSVVLSRTKIG 130
Cdd:PRK14360  314 -SQIGDGVKIGPYAHLRPEAQIGSNCRIG 341
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 16-123 2.96e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566576  16 KNCFLADNCTI-----IGDVVMGDDCSIW------FNTVLRGDVnsiKIGN-----RVNIQDGSVLHTLYQKSTIEIGDD 79
Cdd:PRK14355  302 KGCRIGDDVTVkagsvLEDSVVGDDVAIGpmahlrPGTELSAHV---KIGNfvetkKIVMGEGSKASHLTYLGDATIGRN 378

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1624566576  80 VSIGHNvTI----HGAKIHDfALIGMGAVVMDDAE------VGEGALVAAGSVV 123
Cdd:PRK14355  379 VNIGCG-TItcnyDGVKKHR-TVIEDDVFVGSDVQfvapvtVGRNSLIAAGTTV 430
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 67-131 3.03e-03

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: 37.31  E-value: 3.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624566576  67 TLYQKSTIEIGDDVSIGH------NVTIHGA-KIHDFALIGMGaVVMDDAEVGEGALV----AAGSVVLSRTKIGP 131
Cdd:COG1207   254 TIIDPATTYIDGDVEIGRdvvidpNVILEGKtVIGEGVVIGPN-CTLKDSTIGDGVVIkysvIEDAVVGAGATVGP 328
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 90-132 4.74e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.54  E-value: 4.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1624566576  90 GAKIHDFALIGMGAVVMDDAEVGEGALVAAGSVVLSRTKIGPN 132
Cdd:PRK12461   11 SAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKN 53
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
12-39 5.52e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1624566576  12 PEIGKNCFLADNCTIIGDVVMGDDCSIW 39
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
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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