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Conserved domains on  [gi|2791400049|ref|WP_371418209|]
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MULTISPECIES: gamma carbonic anhydrase family protein [unclassified Anabaena]

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

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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 ...
 19-171 3.44e-74

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 219.90  E-value: 3.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  19 FSQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVE 98
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAILHGCTIG 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791400049  99 RGSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLHA 171
Cdd:COG0663    93 DNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARRYL 167
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 19-171 3.44e-74

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 219.90  E-value: 3.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  19 FSQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVE 98
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAILHGCTIG 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791400049  99 RGSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLHA 171
Cdd:COG0663    93 DNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARRYL 167
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 20-167 8.40e-73

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: 215.74  E-value: 8.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  20 SQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVER 99
Cdd:cd04645     3 DPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTIGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049 100 GSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLA 167
Cdd:cd04645    83 NCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELA 152
PLN02296 PLN02296
carbonate dehydratase
 21-174 8.92e-46

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 151.05  E-value: 8.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  21 QAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILH------GDPGLPTILEDHVTIGHRAVVHS 94
Cdd:PLN02296   57 KDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvaktnlSGKVLPTIIGDNVTIGHSAVLHG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  95 AHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLHAM 172
Cdd:PLN02296  137 CTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAA 216


                  ..
gi 2791400049 173 NN 174
Cdd:PLN02296  217 EN 218
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 18-141 3.42e-18

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  18 IFSQAAFVAANAVI-IGSVnIAArssvwyGSVVRGDVErieVGECTNIQDGAILHGDpglpTILEDHVTIGHRAVVH-SA 95
Cdd:TIGR03570  89 LIHPSAIVSPSASIgEGTV-IMA------GAVINPDVR---IGDNVIINTGAIVEHD----CVIGDFVHIAPGVTLSgGV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2791400049  96 HVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 19-171 3.44e-74

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 219.90  E-value: 3.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  19 FSQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVE 98
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAILHGCTIG 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791400049  99 RGSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLHA 171
Cdd:COG0663    93 DNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARRYL 167
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 20-167 8.40e-73

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: 215.74  E-value: 8.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  20 SQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVER 99
Cdd:cd04645     3 DPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTIGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049 100 GSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLA 167
Cdd:cd04645    83 NCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELA 152
PLN02296 PLN02296
carbonate dehydratase
 21-174 8.92e-46

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 151.05  E-value: 8.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  21 QAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILH------GDPGLPTILEDHVTIGHRAVVHS 94
Cdd:PLN02296   57 KDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvaktnlSGKVLPTIIGDNVTIGHSAVLHG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  95 AHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLHAM 172
Cdd:PLN02296  137 CTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAA 216


                  ..
gi 2791400049 173 NN 174
Cdd:PLN02296  217 EN 218
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 20-168 5.02e-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: 145.41  E-value: 5.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  20 SQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVER 99
Cdd:cd04650     4 SPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAKVGN 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791400049 100 GSLIGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLAL 168
Cdd:cd04650    84 YVIVGMGAILLNGAKIGDHVIIGAGAVVTPGkeIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 23-167 1.09e-39

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: 131.72  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  23 AFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVERGSL 102
Cdd:cd04745     7 SFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCTIGRNAL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791400049 103 IGIGAIILNGVRIGTGSIIGAGAVVTKN--VPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLA 167
Cdd:cd04745    87 VGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQLA 153
PLN02472 PLN02472
uncharacterized protein
 23-170 3.30e-32

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 115.44  E-value: 3.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  23 AFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILH----GDPGLP--TILEDHVTIGHRAVVHSAH 96
Cdd:PLN02472   66 AYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHaawnSPTGLPaeTLIDRYVTIGAYSLLRSCT 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791400049  97 VERGSLIGIGAIILNGVRIGTGSIIGAGAVVT--KNVPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYYQLALLH 170
Cdd:PLN02472  146 IEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLTNEETLEIPKLAVAINDLSQSH 221
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 23-153 4.50e-23

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 90.64  E-value: 4.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  23 AFVAANAVIIGSVNIAARSSVWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHSAHVERGSL 102
Cdd:PRK13627   17 AFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGAILHGCVIGRDAL 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2791400049 103 IGIGAIILNGVRIGTGSIIGAGAVVTKNV--PPGSLVMGVPGKVVRQLTNTEI 153
Cdd:PRK13627   97 VGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVSDDEL 149
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
43-149 1.65e-22

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 87.23  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  43 VWYGSVVRGDVERIEVGECTNIQDGAILHGDPGLptILEDHVTIGHRAVVHSA-----------------HVERGSLIGI 105
Cdd:COG0110    15 VVIGPGVRIYGGNITIGDNVYIGPGVTIDDPGGI--TIGDNVLIGPGVTILTGnhpiddpatfplrtgpvTIGDDVWIGA 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2791400049 106 GAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVRQLT 149
Cdd:COG0110    93 GATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 46-146 1.00e-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: 79.47  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  46 GSVVRGDVErieVGECTNIQDGAILHGDpglpTILEDHVTIGHRAV----------------VHSAHVERGSLIGIGAII 109
Cdd:cd03358    10 NVFIENDVK---IGDNVKIQSNVSIYEG----VTIEDDVFIGPNVVftndlyprskiyrkweLKGTTVKRGASIGANATI 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2791400049 110 LNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVR 146
Cdd:cd03358    83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 103-159 5.94e-19

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: 78.35  E-value: 5.94e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2791400049 103 IGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVRQLTNTEIAELIEH 159
Cdd:cd03349    82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLA 138
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 22-141 1.69e-18

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 78.30  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  22 AAFVAANAVIIGSVNIAARSSVWYGSVVRGDVErieVGECTNIQDGAILHGDpglpTILEDHVTIGHRAVVH-SAHVERG 100
Cdd:cd03360    84 ATLIHPSAVVSPSAVIGEGCVIMAGAVINPDAR---IGDNVIINTGAVIGHD----CVIGDFVHIAPGVVLSgGVTIGEG 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2791400049 101 SLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:cd03360   157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 18-141 3.42e-18

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  18 IFSQAAFVAANAVI-IGSVnIAArssvwyGSVVRGDVErieVGECTNIQDGAILHGDpglpTILEDHVTIGHRAVVH-SA 95
Cdd:TIGR03570  89 LIHPSAIVSPSASIgEGTV-IMA------GAVINPDVR---IGDNVIINTGAIVEHD----CVIGDFVHIAPGVTLSgGV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2791400049  96 HVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 55-145 3.70e-18

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: 75.19  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  55 RIEVGECTNIQDGAILHGDPGLptILEDHVTIGHRAVVHSA--------------------HVERGSLIGIGAIILNGVR 114
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGI--TIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVVILPGVT 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2791400049 115 IGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:cd04647    79 IGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 20-137 5.30e-18

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: 76.51  E-value: 5.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  20 SQAAFVAANAVIIGSVNIAARSSVWYGSVVRGDV-ERIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVVHS-AHV 97
Cdd:cd00710     6 DPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEgTPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVHGpAYI 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2791400049  98 ERGSLIGIGAIILNGvRIGTGSIIGAGAVVTK-NVPPGSLV 137
Cdd:cd00710    86 GDNCFIGFRSVVFNA-KVGDNCVIGHNAVVDGvEIPPGRYV 125
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 103-145 6.08e-17

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: 73.61  E-value: 6.08e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2791400049 103 IGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:cd03357   127 IGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 96-147 1.63e-15

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: 70.11  E-value: 1.63e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2791400049  96 HVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVRQ 147
Cdd:COG1045   119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 25-164 1.64e-13

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: 64.54  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  25 VAANAVIIGSVNI--AARSSVWYGSVVRGDVERIEVGECTNIQDGAIL--------HGDPGLPTILEDHVTIGHRAVVHS 94
Cdd:cd03359    10 VSRKSVICGSQNIvlNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIrppfkkfsKGVAFFPLHIGDYVFIGENCVVNA 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791400049  95 A------HVERGSLIGIGAIILNGVRIGTGSIIGAGAVvtknVPPGSLVMGVPGKVVRQLTNTEIAELIEHAEKYY 164
Cdd:cd03359    90 AqigsyvHIGKNCVIGRRCIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFIGELPECTQELMEEETKEYY 161
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 84-141 1.80e-12

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: 60.15  E-value: 1.80e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791400049  84 VTIGHRAVVH---SAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:cd03354    41 VTLGGKGKGGgkrHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 78-152 9.95e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 58.09  E-value: 9.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  78 TILEDH-VTIGHRAVV----------HSAHVE---RGSL------------IGIGAIILNGVRIGTGSIIGAGAVVTKNV 131
Cdd:PRK09527   89 TIVDDYtVTIGDNVLIapnvtlsvtgHPVHHElrkNGEMysfpitignnvwIGSHVVINPGVTIGDNSVIGAGSVVTKDI 168

                          90       100
                  ....*....|....*....|.
gi 2791400049 132 PPGSLVMGVPGKVVRQLTNTE 152
Cdd:PRK09527  169 PPNVVAAGVPCRVIREINDRD 189
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 84-145 3.04e-09

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: 51.84  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  84 VTIGHRAVV----------H------------SAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:cd05825    24 VTIGSDACIsqgaylctgsHdyrspafplitaPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNP 103


                  ....
gi 2791400049 142 GKVV 145
Cdd:cd05825   104 AVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 103-146 5.65e-09

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 52.96  E-value: 5.65e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2791400049 103 IGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVR 146
Cdd:PRK09677  139 IGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
PRK10502 PRK10502
putative acyl transferase; Provisional
 97-147 1.22e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 51.87  E-value: 1.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2791400049  97 VERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVRQ 147
Cdd:PRK10502  127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 75-148 1.32e-08

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 51.74  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2791400049  75 GLPTILEDHVTIGHRAVVHSahvergsligigaiilnGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVVRQL 148
Cdd:PRK10092  127 GKPVTIGNNVWIGGRAVINP-----------------GVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 46-143 1.90e-08

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: 51.64  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  46 GSVVRGDveRIEVGECTNIQDGAILHGDPGLPTILEDHVTIGHRAVV--H-----------SAHVERGSLIGIGAIILNG 112
Cdd:cd03352    91 GGVIIGD--DVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIgeNcliaaqvgiagSTTIGDNVIIGGQVGIAGH 168

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2791400049 113 VRIGTGSIIGAGAVVTKNVPPGSLVMGVPGK 143
Cdd:cd03352   169 LTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
cysE PRK11132
serine acetyltransferase; Provisional
 97-145 1.96e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 52.01  E-value: 1.96e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2791400049  97 VERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:PRK11132  196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
PLN02739 PLN02739
serine acetyltransferase
 58-159 3.69e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 51.58  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  58 VGECTNIQDG-AILHGdpglptiledhVTIG---HRAVVHSAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPP 133
Cdd:PLN02739  228 IGETAVIGDRvSILHG-----------VTLGgtgKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPS 296

                          90       100
                  ....*....|....*....|....*.
gi 2791400049 134 GSLVMGVPGKVVRQLTNTEIAELIEH 159
Cdd:PLN02739  297 HSMVAGNPAKLIGFVDEQDPSLTMEY 322
PLN02694 PLN02694
serine O-acetyltransferase
 100-145 7.23e-08

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 50.80  E-value: 7.23e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2791400049 100 GSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:PLN02694  218 GVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 46-141 2.10e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 49.25  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  46 GSVVRGDveRIEVGECTNIQDGAIlhGDpglpTILED------HVTIGHRAVV--H-----------SAHVERGSLIGIG 106
Cdd:COG1044   199 GRVVIGD--DVEIGANTTIDRGAL--GD----TVIGDgtkidnLVQIAHNVRIgeHtaiaaqvgiagSTKIGDNVVIGGQ 270

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2791400049 107 AIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:COG1044   271 VGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
PLN02357 PLN02357
serine acetyltransferase
 100-145 2.54e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 49.11  E-value: 2.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2791400049 100 GSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:PLN02357  284 GVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 58-147 1.80e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 46.68  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  58 VGECTNIQDGAI---LHGDPGLPTILEDhvtighravvhsahverGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPG 134
Cdd:PRK14357  361 VGKNVNIGAGTItcnYDGKKKNPTFIED-----------------GAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPY 423

                          90
                  ....*....|...
gi 2791400049 135 SLVMGVPGKVVRQ 147
Cdd:PRK14357  424 SLALGRARQIVKE 436
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 79-131 1.92e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.67  E-value: 1.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2791400049  79 ILEDHVTIGHRAVVHS-AHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNV 131
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAgVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-139 3.97e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.62  E-value: 3.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2791400049  93 HSAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMG 139
Cdd:PRK14353  379 HRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 35-128 8.15e-06

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: 41.85  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  35 VNIAARSSVWYGSVVRGdveRIEVGECTNIQDGAILHGDPG----LPTILEDHVTIGHRAVVHSahvergsligigaiil 110
Cdd:cd00208     1 VFIGEGVKIHPKAVIRG---PVVIGDNVNIGPGAVIGAATGpnekNPTIIGDNVEIGANAVIHG---------------- 61

                          90
                  ....*....|....*...
gi 2791400049 111 nGVRIGTGSIIGAGAVVT 128
Cdd:cd00208    62 -GVKIGDNAVIGAGAVVT 78
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 113-141 9.10e-06

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: 44.63  E-value: 9.10e-06
                          10        20
                  ....*....|....*....|....*....
gi 2791400049 113 VRIGTGSIIGAGAVVTKNVPPGSLVMGVP 141
Cdd:COG1207   413 VTIGDGATIGAGSTITKDVPAGALAIARA 441
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 83-156 1.48e-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: 43.85  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  83 HVTIGHRAVvhsahvergslIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV---------RQLTNTEI 153
Cdd:COG1043   140 HVEVGDHAI-----------IGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRglnlvglkrRGFSREQI 208


                  ...
gi 2791400049 154 AEL 156
Cdd:COG1043   209 RAL 211
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 90-131 1.54e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.97  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2791400049  90 AVVH-SAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNV 131
Cdd:PRK00892  107 AVIDpSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 93-139 2.71e-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: 42.41  E-value: 2.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2791400049  93 HSAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMG 139
Cdd:cd03353   143 HRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 57-139 7.97e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.02  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  57 EVGECTNIQDGAIlhgdpglpTILEDHVTiGHRAVVHsahveRGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSL 136
Cdd:PRK14356  375 EIGAGANIGAGTI--------TCNYDGVN-KHRTVIG-----EGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440


                  ...
gi 2791400049 137 VMG 139
Cdd:PRK14356  441 AIA 443
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 79-131 1.10e-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: 40.85  E-value: 1.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2791400049  79 ILEDHVTIGHRAVVHS-AHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNV 131
Cdd:cd03352     3 KIGENVSIGPNAVIGEgVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 57-137 1.30e-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: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  57 EVGECTNIQDGAIlhgdpglpTILEDHVTiGHRAVVHSaHVERGSligiGAIILNGVRIGTGSIIGAGAVVTKNVPPGSL 136
Cdd:PRK14352  376 DIGEHSNIGASSV--------FVNYDGVN-KHRTTIGS-HVRTGS----DTMFVAPVTVGDGAYTGAGTVIREDVPPGAL 441


                  .
gi 2791400049 137 V 137
Cdd:PRK14352  442 A 442
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 46-141 1.70e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  46 GSVVRGDveRIEVGECTNIQDGAIlhGDpglpTILED------HVTIGHRAVV--H-----------SAHVERGSLIGIG 106
Cdd:PRK00892  202 GRVIIGD--DVEIGANTTIDRGAL--DD----TVIGEgvkidnLVQIAHNVVIgrHtaiaaqvgiagSTKIGRYCMIGGQ 273

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2791400049 107 AIILNGVRIGTGSIIGAGAVVTKNVP-PGSLVMGVP 141
Cdd:PRK00892  274 VGIAGHLEIGDGVTITAMSGVTKSIPePGEYSSGIP 309
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 90-131 1.80e-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: 1.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2791400049  90 AVVH-SAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNV 131
Cdd:COG1044   103 AVIDpSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 83-145 1.96e-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: 40.49  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791400049  83 HVTIGHRAVvhsahvergslIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV 145
Cdd:cd03351   138 HVEIGDYAI-----------IGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLR 189
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 23-142 2.28e-04

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 40.10  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  23 AFVAANAVIIGS-VNIAARssVWYGSVVRGdveRIEVGECTNIQDGAILHG--------DPG--LPTILEDHVTIGHRAV 91
Cdd:COG2171   110 AYLAPGVVLMPSfVNIGAY--VDEGTMVDT---WATVGSCAQIGKNVHLSGgagiggvlEPLqaAPVIIEDNCFIGARSG 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791400049  92 VhsahVErgsligigaiilnGVRIGTGSIIGAGAVVTK---------------NVPPGSLVmgVPG 142
Cdd:COG2171   185 V----VE-------------GVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGSVV--VPG 231
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-136 2.30e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  28 NAVIIGSVNIAARSSVWYGSVVrgdvERIEVGECTNIqdGAILHGDPGlpTILEDHVTIGHRAVVHSAHVERGSL----- 102
Cdd:PRK14355  297 QGVVIKGCRIGDDVTVKAGSVL----EDSVVGDDVAI--GPMAHLRPG--TELSAHVKIGNFVETKKIVMGEGSKashlt 368

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791400049 103 ------------IGIGAIILN-------------------------GVRIGTGSIIGAGAVVTKNVPPGSL 136
Cdd:PRK14355  369 ylgdatigrnvnIGCGTITCNydgvkkhrtvieddvfvgsdvqfvaPVTVGRNSLIAAGTTVTKDVPPDSL 439
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 23-142 2.38e-04

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 40.18  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  23 AFVAANAVIIGS-VNIAARssVWYGSVVrgDVERIeVGECTNIQDGAILHGDPGL----------PTILEDHVTIGHRAV 91
Cdd:PRK11830  116 AYIAPNVVLMPSyVNIGAY--VDEGTMV--DTWAT-VGSCAQIGKNVHLSGGVGIggvleplqanPVIIEDNCFIGARSE 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791400049  92 VhsahVErgsligigaiilnGVRIGTGSIIGAGAVVTK---------------NVPPGSLVmgVPG 142
Cdd:PRK11830  191 V----VE-------------GVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGSVV--VPG 237
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
83-156 4.67e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  83 HVTIGHRAVvhsahvergslIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKVV---------RQLTNTEI 153
Cdd:PRK05289  141 HVEVGDYAI-----------IGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRglnlvglkrRGFSREEI 209


                  ...
gi 2791400049 154 AEL 156
Cdd:PRK05289  210 HAL 212
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 25-144 8.57e-04

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: 38.40  E-value: 8.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  25 VAANAVIIGSVNIAARSSVWYGSVV---------RGDVERIEVGECTNIQDGAILH----GDPGLPTI------------ 79
Cdd:TIGR01852  37 LKSHVVILGHTTIGEGTRIFPGAVIggvpqdlkyKGEKTRLIIGDNNTIREFVTINrgtaSGGGVTRIgnnnllmayshi 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791400049  80 -----LEDHVTIGHRAVVhSAHVERGS--LIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKV 144
Cdd:TIGR01852 117 ahdcvVGNHVILANNATL-AGHVEVGDyaIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 20-127 1.50e-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: 38.07  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  20 SQAAFVAANAVIIGSVNIAArssvwyGSVVRGDVErievgectnIQDGAILHgdPGlpTILEDHVTIGHRAVVHSahver 99
Cdd:COG1044   100 HPSAVIDPSAKIGEGVSIGP------FAVIGAGVV---------IGDGVVIG--PG--VVIGDGVVIGDDCVLHP----- 155

                          90       100
                  ....*....|....*....|....*...
gi 2791400049 100 gsligiGAIILNGVRIGTGSIIGAGAVV 127
Cdd:COG1044   156 ------NVTIYERCVIGDRVIIHSGAVI 177
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 97-136 4.16e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.73  E-value: 4.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2791400049  97 VERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSL 136
Cdd:PRK14354  396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 69-137 4.49e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 36.73  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791400049  69 ILHGDPGLPTILEDHVTIG---HRAVVH------SAHVERGSLIgIGAIILNGVRIGTGSIIGaGAVVTKNV--PPGSLV 137
Cdd:PRK00844  303 FVDGGGRVGSAQDSLVSAGsiiSGATVRnsvlspNVVVESGAEV-EDSVLMDGVRIGRGAVVR-RAILDKNVvvPPGATI 380
PRK10191 PRK10191
putative acyl transferase; Provisional
 84-144 6.13e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 35.25  E-value: 6.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791400049  84 VTIGHRAVVHSA--HVERGSLIGIGAIILNGVRIGTGSIIGAGAVVTKNVPPGSLVMGVPGKV 144
Cdd:PRK10191   80 VTIGNRGADNMAcpHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 57-127 8.01e-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: 35.46  E-value: 8.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791400049  57 EVGECTNIQDGAILhgdpGLPTILEDHVTIGHRAVV-HSAHVERGSLIGIGAIILNGVRIGTGSIIGAGAVV 127
Cdd:cd03352     3 KIGENVSIGPNAVI----GEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
 
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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