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Conserved domains on  [gi|755043478|ref|WP_042395969|]
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gamma carbonic anhydrase family protein [Pseudescherichia vulneris]

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 ...
 4-178 2.61e-87

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.41  E-value: 2.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   4 ALRSYKDLYPKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThkssynpEGNPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  84 GEDVTVGHKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....*
gi 755043478 164 SANNYVKWKDDYLDQ 178
Cdd:COG0663  155 SAENYVELARRYLAE 169
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-178 2.61e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.41  E-value: 2.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   4 ALRSYKDLYPKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThkssynpEGNPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  84 GEDVTVGHKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....*
gi 755043478 164 SANNYVKWKDDYLDQ 178
Cdd:COG0663  155 SAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 14-173 5.83e-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: 221.90  E-value: 5.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVTHkssynpeGNPLIIGEDVTVGHKV 93
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  94 MLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKYSANNYVKWKD 173
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 13-168 1.74e-49

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 161.06  E-value: 1.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThKSSYNPEGNPLIIGEDVTVGHK 92
Cdd:PLN02296  53 PVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVA-KTNLSGKVLPTIIGDNVTIGHS 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  93 VMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKYSANNY 168
Cdd:PLN02296 132 AVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNY 207
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 14-132 1.28e-08

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: 52.65  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIGEDVT---- 88
Cdd:TIGR01852  12 EIGENVEIGPFCIVGPGVKIGDGVELKSHVVILG---HTTIGEGTRIFPGAVIgGVPQDLKYKGEKTRLIIGDNNTiref 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478   89 ---------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:TIGR01852  89 vtinrgtasgggvtrIGNNNLLmayshiaHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQ 154
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
97-126 5.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 5.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 755043478   97 GCTVGNRVLVGMGSILLDGVVVEDDVMIGA 126
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-178 2.61e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.41  E-value: 2.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   4 ALRSYKDLYPKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThkssynpEGNPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  84 GEDVTVGHKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....*
gi 755043478 164 SANNYVKWKDDYLDQ 178
Cdd:COG0663  155 SAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 14-173 5.83e-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: 221.90  E-value: 5.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVTHkssynpeGNPLIIGEDVTVGHKV 93
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  94 MLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKYSANNYVKWKD 173
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 13-168 1.74e-49

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 161.06  E-value: 1.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThKSSYNPEGNPLIIGEDVTVGHK 92
Cdd:PLN02296  53 PVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVA-KTNLSGKVLPTIIGDNVTIGHS 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  93 VMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKYSANNY 168
Cdd:PLN02296 132 AVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNY 207
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 13-170 6.43e-45

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: 145.79  E-value: 6.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVTHkssynpeGNPLIIGEDVTVGHK 92
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDH-------GYPTEIGDYVTIGHN 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755043478  93 VMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIEGLKYSANNYVK 170
Cdd:cd04650   74 AVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVE 151
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 13-159 3.93e-30

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: 107.84  E-value: 3.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVThkssynpEGNPLIIGEDVTVGHK 92
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGF-------PGQDTVLEENGHIGHG 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755043478  93 VMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEIE 159
Cdd:cd04745   74 AILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVA 140
PLN02472 PLN02472
uncharacterized protein
 13-158 7.68e-29

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 107.36  E-value: 7.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHVTHKSsynPEGNP--LIIGEDVTVG 90
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNS---PTGLPaeTLIDRYVTIG 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755043478  91 HKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEI 158
Cdd:PLN02472 137 AYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEET 204
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 7-158 3.89e-25

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 96.42  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   7 SYKDLYPKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGARSNIQDGSVLHvthksSYNpeGNPLIIGED 86
Cdd:PRK13627   5 AFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMH-----GYC--DTDTIVGEN 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755043478  87 VTVGHKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTEAEI 158
Cdd:PRK13627  78 GHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDEL 149
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 13-135 6.38e-23

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: 89.61  E-value: 6.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  13 PKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNY-VQIGARSNIQDGSVLHVThkssynpEGNPLIIGEDVTVGH 91
Cdd:cd00710    3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTpIIIGANVNIQDGVVIHAL-------EGYSVWIGKNVSIAH 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  92 KVMLHG-CTVGNRVLVGMGSILL-----DGVVVE-----DDVMIGAGSLVPQNKR 135
Cdd:cd00710   76 GAIVHGpAYIGDNCFIGFRSVVFnakvgDNCVIGhnavvDGVEIPPGRYVPAGAV 130
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-158 5.69e-15

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 67.97  E-value: 5.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  24 TSVVIGDVRVADDVGIWPLVAIRGdvNYVQIGARSNIQDGSVLHVTHKssynpegnpLIIGEDVTVGHKVML-------- 95
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIDDPGG---------ITIGDNVLIGPGVTIltgnhpid 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755043478  96 ---------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVpqNKRLVSGFLYLGSPVKQIRPLTEAEI 158
Cdd:COG0110   71 dpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVV--TKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-151 4.09e-09

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: 52.12  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  35 DDVGIWPLVAIRGDVnyvQIGARSNIQDGSvlHVTHKSsynpegnplIIGEDVTVGHKVM----------------LHGC 98
Cdd:cd03358    3 DNCIIGTNVFIENDV---KIGDNVKIQSNV--SIYEGV---------TIEDDVFIGPNVVftndlyprskiyrkweLKGT 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755043478  99 TVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVpqNKRLVSGFLYLGSPVKQIR 151
Cdd:cd03358   69 TVKRGASIGANATILPGVTIGEYALVGAGAVV--TKDVPPYALVVGNPARIIG 119
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 14-132 1.28e-08

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: 52.65  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIGEDVT---- 88
Cdd:TIGR01852  12 EIGENVEIGPFCIVGPGVKIGDGVELKSHVVILG---HTTIGEGTRIFPGAVIgGVPQDLKYKGEKTRLIIGDNNTiref 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478   89 ---------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:TIGR01852  89 vtinrgtasgggvtrIGNNNLLmayshiaHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQ 154
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 52-150 1.90e-08

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 50.15  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  52 VQIGARSNIQDGSVLHvthkssynpEGNPLIIGEDVTVGHKVMLHGC--------------------TVGNRVLVGMGSI 111
Cdd:cd04647    2 ISIGDNVYIGPGCVIS---------AGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVV 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755043478 112 LLDGVVVEDDVMIGAGSLVpqNKRLVSGFLYLGSPVKQI 150
Cdd:cd04647   73 ILPGVTIGDGAVVGAGSVV--TKDVPPNSIVAGNPAKVI 109
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 11-128 5.55e-08

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: 51.17  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  11 LYPKIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVnyvQIGARSNIQDGSVlhvthkssynpegnpliIGEDVTVG 90
Cdd:COG1044   89 FYPPPAPAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGV---VIGDGVVIGPGVV-----------------IGDGVVIG 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  91 HKVMLH-------GCTVGNRVLVGMGSIL--------------------LDGVVVEDDVMIGAGS 128
Cdd:COG1044  149 DDCVLHpnvtiyeRCVIGDRVIIHSGAVIgadgfgfapdedggwvkipqLGRVVIGDDVEIGANT 213
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 82-130 5.66e-08

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: 50.56  E-value: 5.66e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755043478  82 IIGEDVTVGHKVMLHG-CTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:cd03360  134 VIGDFVHIAPGVVLSGgVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV 183
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 39-155 1.10e-07

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: 49.14  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  39 IWPLVAIRGDVNYVQIGARSNIQDGSVLHVTHK-SSYNPEGNPLIIGEDVTVGHKVMLHGCTVGNRVLVGMGSILLDGVV 117
Cdd:cd03359   30 IQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKkFSKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCI 109

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755043478 118 VEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTE 155
Cdd:cd03359  110 IKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPE 147
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 14-113 1.19e-07

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: 47.24  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVgiwplvairgdvnyvqigarsNIQDGSVLHVTHkssYNPEGNPLIIGEDVTVGHKV 93
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNV---------------------NIGPGAVIGAAT---GPNEKNPTIIGDNVEIGANA 57

                         90       100
                 ....*....|....*....|.
gi 755043478  94 MLHG-CTVGNRVLVGMGSILL 113
Cdd:cd00208   58 VIHGgVKIGDNAVIGAGAVVT 78
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 14-132 1.55e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 49.64  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIG------ED 86
Cdd:PRK12461  13 KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILG---PTRIGKNNKIHQGAVVgDEPQDFTYKGEESRLEIGdrnvirEG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  87 VT------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:PRK12461  90 VTihrgtkgggvtrIGNDNLLmayshvaHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQ 154
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 82-130 3.33e-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: 48.26  E-value: 3.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755043478   82 IIGEDVTVGHKVMLHG-CTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:TIGR03570 137 VIGDFVHIAPGVTLSGgVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVV 186
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 31-130 5.14e-07

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: 45.32  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  31 VRVADDVGIWPLVAIRGDVnyvQIGARSNIQDGSVLHVTHkssYNPEGNPLIIGEDVTVGHKVMLHGctvgnrvlvgmgs 110
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPV---VIGDNVNIGPGAVIGAAT---GPNEKNPTIIGDNVEIGANAVIHG------------- 61

                         90       100
                 ....*....|....*....|
gi 755043478 111 illdGVVVEDDVMIGAGSLV 130
Cdd:cd00208   62 ----GVKIGDNAVIGAGAVV 77
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 14-132 5.85e-07

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: 48.20  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIG------ED 86
Cdd:cd03351   13 KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDG---PTTIGKNNRIFPFASIgEAPQDLKYKGEPTRLEIGdnntirEF 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  87 VT-------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:cd03351   90 VTihrgtaqgggvtrIGNNNLLmayvhvaHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQ 155
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 81-130 2.38e-06

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 44.35  E-value: 2.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  81 LIIGEDVTVGHKVML-HGCT--------------VGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:cd03354   23 IVIGETAVIGDNCTIyQGVTlggkgkgggkrhptIGDNVVIGAGAKILGNITIGDNVKIGANAVV 87
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 14-151 3.21e-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: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVnyvQIGARSNIQDGSVLHVTHKSSYNPEGNPL--------IIGE 85
Cdd:cd03352   21 VIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC---IIGDRVIIHSGAVIGSDGFGFAPDGGGWVkipqlggvIIGD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  86 DVTVG----------------------------HKV------MLHGC-------TVGNRVLVGMGSILLDGVVVEDDVMI 124
Cdd:cd03352   98 DVEIGanttidrgalgdtvigdgtkidnlvqiaHNVrigencLIAAQvgiagstTIGDNVIIGGQVGIAGHLTIGDGVVI 177

                        170       180
                 ....*....|....*....|....*..
gi 755043478 125 GAGSLVPQNKRlvSGFLYLGSPVKQIR 151
Cdd:cd03352  178 GAGSGVTSIVP--PGEYVSGTPAQPHR 202
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 14-136 5.72e-06

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 44.24  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDVNYVQIGaRSNIQDGSVLHVTHKSSYNPEGNPLIIGEdvtvgHKV 93
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIG-ENNIIEEQVTIVNKKPKDPAEPKPMIIGS-----NNV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755043478  94 MLHGCT-----VGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRL 136
Cdd:cd04646   75 FEVGCKcealkIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEIL 122
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 52-150 1.04e-05

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 42.59  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  52 VQIGARSNIQDGSVLhvthkssYNPEgnPLIIGEDVTVGHKVMLhgCT------------------VGNRVLVGMGSILL 113
Cdd:cd05825    4 LTIGDNSWIGEGVWI-------YNLA--PVTIGSDACISQGAYL--CTgshdyrspafplitapivIGDGAWVAAEAFVG 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755043478 114 DGVVVEDDVMIGAGSLVpqNKRLVSGFLYLGSPVKQI 150
Cdd:cd05825   73 PGVTIGEGAVVGARSVV--VRDLPAWTVYAGNPAVPV 107
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 20-125 1.44e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.56  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  20 MVDATSVVI-GDVRVADDVGIWPLVAIRGDvnyVQIGARSNIQDGSVLhvthkssynpegNPLIIGEDVTVGHKVMLHGC 98
Cdd:cd03353    4 LIDPETTYIdGDVEIGVDVVIDPGVILEGK---TVIGEDCVIGPNCVI------------KDSTIGDGVVIKASSVIEGA 68

                         90       100
                 ....*....|....*....|....*..
gi 755043478  99 TVGNRVLVGMGSILLDGVVVEDDVMIG 125
Cdd:cd03353   69 VIGNGATVGPFAHLRPGTVLGEGVHIG 95
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 78-130 3.42e-05

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: 42.41  E-value: 3.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755043478  78 GNPLIIGEDV---------TVGH----KVMLHGC------TVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:cd03357   80 VAPVTIGDNVligpnvqiyTAGHpldpEERNRGLeyakpiTIGDNVWIGGGVIILPGVTIGDNSVIGAGSVV 151
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
14-132 5.27e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.39  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIG------ED 86
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDG---HTTIGKNNRIFPFASIgEDPQDLKYKGEPTRLVIGdnntirEF 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  87 VT-------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:PRK05289  93 VTinrgtvqgggvtrIGDNNLLmayvhvaHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQ 158
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 14-132 7.24e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 41.93  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGdvnYVQIGARSNIQDGSVL-HVTHKSSYNPEGNPLIIGEDVT---- 88
Cdd:COG1043   15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEG---PTTIGKNNRIFPFASIgEEPQDLKYKGEPTRLEIGDNNTiref 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  89 ---------------VGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQ 132
Cdd:COG1043   92 vtihrgtvqgggvtrIGDDNLLmayvhvaHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQ 157
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 14-128 9.57e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 41.25  E-value: 9.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDV-------------------NYVQIGARSNIQDGSVL----HV-- 68
Cdd:cd03353   17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTigdgvvikassviegavigNGATVGPFAHLRPGTVLgegvHIgn 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  69 ---THKSSynpegnpliIGEDVTVGHKVMLHGCTVGNRVLVGMGSILL--DGV-----VVEDDVMIGAGS 128
Cdd:cd03353   97 fveIKKST---------IGEGSKANHLSYLGDAEIGEGVNIGAGTITCnyDGVnkhrtVIGDNVFIGSNS 157
PRK10502 PRK10502
putative acyl transferase; Provisional
 14-152 1.15e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.09  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATS-------VVIGD-VRVADDVGIWPLVAIrgdvnyvQIGARSNIQDGSVL----HVTHKSSYNPEGNPL 81
Cdd:PRK10502  53 KIGKGVVIRPSVritypwkLTIGDyAWIGDDVWLYNLGEI-------TIGAHCVISQKSYLctgsHDYSDPHFDLNTAPI 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755043478  82 IIGEdvtvghkvmlhGCTVGNRVLVGmgsillDGVVVEDDVMIGAGSLVPQNkrLVSGFLYLGSPVKQIRP 152
Cdd:PRK10502 126 VIGE-----------GCWLAADVFVA------PGVTIGSGAVVGARSSVFKS--LPANTICRGNPAVPIRP 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 14-128 1.19e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDAtSVVIGD-VRVADDVGIWPLVAIrGDvnYVQIGARSNIQDGSVLHvthkssynpegnpliigedvtvghk 92
Cdd:PRK00892 114 KIGEGVSIGP-NAVIGAgVVIGDGVVIGAGAVI-GD--GVKIGADCRLHANVTIY------------------------- 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  93 vmlHGCTVGNRVLVGMGSIL-------------------LDGVVVEDDVMIGAGS 128
Cdd:PRK00892 165 ---HAVRIGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGDDVEIGANT 216
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 14-133 1.65e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVVIGDVRVADDVGIWPLVAIRGDvnyVQIGARSNIQDGSVL------HVTHKSSYN--PE-GNpLIIG 84
Cdd:PRK00892 132 VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA---VRIGNRVIIHSGAVIgsdgfgFANDRGGWVkiPQlGR-VIIG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  85 EDVTVG----------------------------HKV------MLHGC-------TVGNRVLVGMGSILLDGVVVEDDVM 123
Cdd:PRK00892 208 DDVEIGanttidrgalddtvigegvkidnlvqiaHNVvigrhtAIAAQvgiagstKIGRYCMIGGQVGIAGHLEIGDGVT 287

                        170
                 ....*....|
gi 755043478 124 IGAGSLVPQN 133
Cdd:PRK00892 288 ITAMSGVTKS 297
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 83-129 2.36e-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: 2.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755043478  83 IGEDVTVGHkvmlhGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSL 129
Cdd:COG1044  111 IGEGVSIGP-----FAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 96-150 2.68e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.74  E-value: 2.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  96 HGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVpqNKRLVSGFLYLgSPVKQI 150
Cdd:PRK14359 366 HKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTV--TKDVPKGSLAI-SRAPQK 417
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 20-125 3.78e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.01  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  20 MVDATSVVI-GDVRVADDVGIWPLVAIRGDvnyVQIGARSNIQDGSVLhvthKSSynpegnplIIGEDVTVGHKVmLHGC 98
Cdd:COG1207  255 IIDPATTYIdGDVEIGRDVVIDPNVILEGK---TVIGEGVVIGPNCTL----KDS--------TIGDGVVIKYSV-IEDA 318

                         90       100
                 ....*....|....*....|....*..
gi 755043478  99 TVGNRVLVGMGSILLDGVVVEDDVMIG 125
Cdd:COG1207  319 VVGAGATVGPFARLRPGTVLGEGVKIG 345
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 100-171 3.88e-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: 40.12  E-value: 3.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755043478  100 VGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVKQIRPLTE--AEIEGLKYSANNYVKW 171
Cdd:TIGR02353 404 IGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGSPPFELPRRVNrdDELEALTFEPDPRRRL 477
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 78-159 3.97e-04

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 39.60  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  78 GNPLIIGEDVT-------VGHKVMLHG------CTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVpqNKRLVSGFLYLG 144
Cdd:PRK09527  99 GDNVLIAPNVTlsvtghpVHHELRKNGemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVV--TKDIPPNVVAAG 176

                         90
                 ....*....|....*
gi 755043478 145 SPVKQIRPLTEAEIE 159
Cdd:PRK09527 177 VPCRVIREINDRDKQ 191
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-133 4.87e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.91  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  27 VIGDVRVADDVGIWPLVAIRGDV---------NYV-----QIGARSNIQDGSVLhvthkssynpeGNPlIIGEDVTVG-- 90
Cdd:PRK14360 310 VVSDSQIGDGVKIGPYAHLRPEAqigsncrigNFVeikksQLGEGSKVNHLSYI-----------GDA-TLGEQVNIGag 377

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755043478  91 ------HKVMLHGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQN 133
Cdd:PRK14360 378 titanyDGVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKD 426
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-133 5.08e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.73  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDATSVvIGDVRVADDVGIWPLVAIRgdvnyvqigarsniqDGSVLHVTHKSSYNPEGNPLIIGEDVTVGHKV 93
Cdd:PRK14355 305 RIGDDVTVKAGSV-LEDSVVGDDVAIGPMAHLR---------------PGTELSAHVKIGNFVETKKIVMGEGSKASHLT 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755043478  94 MLHGCTVGNRVLVGMGSIL--LDGV-----VVEDDV------------------MIGAGSLVPQN 133
Cdd:PRK14355 369 YLGDATIGRNVNIGCGTITcnYDGVkkhrtVIEDDVfvgsdvqfvapvtvgrnsLIAAGTTVTKD 433
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 82-136 5.64e-04

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 37.17  E-value: 5.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755043478  82 IIGEDVTVGHK------VMLHGCTVGNRVLVgMGSILLDGVVVEDDV-----MIGAGSLVPQNKRL 136
Cdd:cd04652    1 LVGENTQVGEKtsikrsVIGANCKIGKRVKI-TNCVIMDNVTIEDGCtlencIIGNGAVIGEKCKL 65
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 81-150 5.84e-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: 39.73  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   81 LIIGEDVTVGHKVMLHG------------CTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYLGSPVK 148
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211


                  ..
gi 755043478  149 QI 150
Cdd:TIGR02353 212 KT 213
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-125 6.12e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.73  E-value: 6.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755043478  52 VQIGARSNIQDGSVLhvthkssynpeGNPLIIGEDVTVGHKVMLHGCTVGNRVLVGMGSILLDGvVVEDDVMIG 125
Cdd:PRK14355 269 VVIGRDTTIYPGVCI-----------SGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDS-VVGDDVAIG 330
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 82-130 9.81e-04

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: 38.54  E-value: 9.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755043478  82 IIGEDVTVGHkvmlhGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:cd03352    3 KIGENVSIGP-----NAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 86-126 1.19e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.68  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755043478  86 DVTVGHKVMLHGCTVGNRVlVGMGSILLDGVVVEDDVMIGA 126
Cdd:PLN02241 315 DSIISHGCFLRECKIEHSV-VGLRSRIGEGVEIEDTVMMGA 354
PLN02357 PLN02357
serine acetyltransferase
 78-130 1.20e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 38.71  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755043478  78 GNPLIIGEDVTVGHKVMLHGC---------TVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:PLN02357 250 GETAVVGNNVSILHNVTLGGTgkqsgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 311
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-128 1.21e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVdaTSVVIGDVRVADDVGIWPLVAIRGDV---------NYVQIgARSNIQDGS-VLHVTHkssynpegnpliI 83
Cdd:PRK14354 302 TIGDGVTI--TNSVIEESKVGDNVTVGPFAHLRPGSvigeevkigNFVEI-KKSTIGEGTkVSHLTY------------I 366

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  84 GeDVTVGHKVMLhGC---------------TVGNRVLVGMGSILLDGVVVEDDVMIGAGS 128
Cdd:PRK14354 367 G-DAEVGENVNI-GCgtitvnydgknkfktIIGDNAFIGCNSNLVAPVTVGDNAYIAAGS 424
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 82-130 1.44e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 1.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755043478  82 IIGEDVTVGHkvmlhGCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:PRK00892 114 KIGEGVSIGP-----NAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRL 157
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 82-130 1.78e-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: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755043478  82 IIGEDVTVGHKVMLH-GCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:cd03352   15 VIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVII 64
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 14-151 1.97e-03

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: 37.69  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  14 KIGQRVMVDAtSVVIGD-VRVADDVGIWPLVAIRGDvnyVQIGARSNIQDGSVL------HVThkssyNPEGNPL----- 81
Cdd:COG1044  128 VIGDGVVIGP-GVVIGDgVVIGDDCVLHPNVTIYER---CVIGDRVIIHSGAVIgadgfgFAP-----DEDGGWVkipql 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  82 ---IIGEDV---------------TV-------------GHKV------MLHGC-------TVGNRVLVGMGSILLDGVV 117
Cdd:COG1044  199 grvVIGDDVeiganttidrgalgdTVigdgtkidnlvqiAHNVrigehtAIAAQvgiagstKIGDNVVIGGQVGIAGHLT 278

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755043478 118 VEDDVMIGAGSLVPQNkrLVSGFLYLGSPVKQIR 151
Cdd:COG1044  279 IGDGVIIGAQSGVTKS--IPEGGVYSGSPAQPHR 310
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 76-146 2.10e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 38.19  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478   76 PEGNPLIIGEDVTV--GHKVMLH----------GCTVGNRVLVGMGSILLDGVVVEDDVMIGAGSLVPQNKRLVSGFLYL 143
Cdd:TIGR02353 612 TERDLVTIGDDSTLneGSVIQTHlfedrvmksdTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWR 691


                  ...
gi 755043478  144 GSP 146
Cdd:TIGR02353 692 GNP 694
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 54-136 2.15e-03

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: 37.46  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755043478  54 IGARSNIQDGSVLHvthkssynpEGNplIIGEDVTVGHKVML-------HGCTVGNRVLVGMGSILLDGVVVEDDVMIGA 126
Cdd:cd03360   93 VSPSAVIGEGCVIM---------AGA--VINPDARIGDNVIIntgavigHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGA 161

                         90
                 ....*....|
gi 755043478 127 GSLVPQNKRL 136
Cdd:cd03360  162 GATIIQGVTI 171
PLN02694 PLN02694
serine O-acetyltransferase
 78-130 3.53e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 37.31  E-value: 3.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755043478  78 GNPLIIGEDVTVGHKVMLHGC---------TVGNRVLVGMGSILLDGVVVEDDVMIGAGSLV 130
Cdd:PLN02694 184 GETAVIGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVV 245
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
97-126 5.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 5.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 755043478   97 GCTVGNRVLVGMGSILLDGVVVEDDVMIGA 126
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
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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