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Conserved domains on  [gi|1035737233|ref|WP_064573498|]
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NeuD/PglB/VioB family sugar acetyltransferase [Hafnia paralvei]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 4-199 6.08e-56

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.


The actual alignment was detected with superfamily member TIGR03570:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 201  Bit Score: 176.14  E-value: 6.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233   4 KLIIIGAGGFAKSVIDSLDYGLYELVGFIDSYKTGM---HQGLSILANSIESIE-CADKYSYFIAIGDPDIRAMWFELLD 79
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQgteVDGLPVLGGDEDLLRyPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  80 SYHLDMINVFDATAIISKRAKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKS 159
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1035737233 160 FIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:TIGR03570 161 FIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 4-199 6.08e-56

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: 176.14  E-value: 6.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233   4 KLIIIGAGGFAKSVIDSLDYGLYELVGFIDSYKTGM---HQGLSILANSIESIE-CADKYSYFIAIGDPDIRAMWFELLD 79
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQgteVDGLPVLGGDEDLLRyPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  80 SYHLDMINVFDATAIISKRAKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKS 159
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1035737233 160 FIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:TIGR03570 161 FIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 7-199 4.11e-51

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: 163.42  E-value: 4.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233   7 IIGAGGFAKSVIDSLD-YGLYELVGFIDSYKTGMHQ---GLSILANSIESIECADKYSYFIAIGDPDIRAMWFELLDSYH 82
Cdd:cd03360     1 IIGAGGHARVVADILEaDSGYEVVGFLDDDPELKGTeglGLPVGLDELLLLYPPPDDEFVVAIGDNKLRRKLAEKLLAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  83 LDMINVFDATAIISKRAKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKSFIG 162
Cdd:cd03360    81 YRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1035737233 163 SCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 4-78 1.90e-15

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 68.36  E-value: 1.90e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1035737233   4 KLIIIGAGGFAKSVIDSLDY-GLYELVGFIDSYKTGMHQGLSILANSIESIE--CADKYSYFIAIGDPDIRAMWFELL 78
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAmGEYEIIGFLDDNKKTEVNGYPVLGGDIDLLAslSPDEYDVVIAIGNNKVRKKIAEKL 78
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
92-206 1.55e-14

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 67.59  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  92 TAIISKRAKLGICIYIGKMAIVN-CDSIIENGVVINTRALVE--HGNRIGFCTNISTNVVL----------------NGD 152
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIKVR 206
Cdd:COG0110    82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
PLN02739 PLN02739
serine acetyltransferase
 122-205 1.18e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 59.66  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 122 GVVINTRALVehGNRIgfctNISTNVVLNGD--------VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNI 193
Cdd:PLN02739  225 GVVIGETAVI--GDRV----SILHGVTLGGTgketgdrhPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHS 298

                          90
                  ....*....|..
gi 1035737233 194 VVAGSPTKLIKV 205
Cdd:PLN02739  299 MVAGNPAKLIGF 310
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 4-199 6.08e-56

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: 176.14  E-value: 6.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233   4 KLIIIGAGGFAKSVIDSLDYGLYELVGFIDSYKTGM---HQGLSILANSIESIE-CADKYSYFIAIGDPDIRAMWFELLD 79
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADILERSGWEVVGFLDDNPALQgteVDGLPVLGGDEDLLRyPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  80 SYHLDMINVFDATAIISKRAKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKS 159
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1035737233 160 FIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:TIGR03570 161 FIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 7-199 4.11e-51

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: 163.42  E-value: 4.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233   7 IIGAGGFAKSVIDSLD-YGLYELVGFIDSYKTGMHQ---GLSILANSIESIECADKYSYFIAIGDPDIRAMWFELLDSYH 82
Cdd:cd03360     1 IIGAGGHARVVADILEaDSGYEVVGFLDDDPELKGTeglGLPVGLDELLLLYPPPDDEFVVAIGDNKLRRKLAEKLLAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  83 LDMINVFDATAIISKRAKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKSFIG 162
Cdd:cd03360    81 YRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1035737233 163 SCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 4-78 1.90e-15

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 68.36  E-value: 1.90e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1035737233   4 KLIIIGAGGFAKSVIDSLDY-GLYELVGFIDSYKTGMHQGLSILANSIESIE--CADKYSYFIAIGDPDIRAMWFELL 78
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAmGEYEIIGFLDDNKKTEVNGYPVLGGDIDLLAslSPDEYDVVIAIGNNKVRKKIAEKL 78
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
92-206 1.55e-14

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 67.59  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  92 TAIISKRAKLGICIYIGKMAIVN-CDSIIENGVVINTRALVE--HGNRIGFCTNISTNVVL----------------NGD 152
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIKVR 206
Cdd:COG0110    82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
PLN02739 PLN02739
serine acetyltransferase
 122-205 1.18e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 59.66  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 122 GVVINTRALVehGNRIgfctNISTNVVLNGD--------VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNI 193
Cdd:PLN02739  225 GVVIGETAVI--GDRV----SILHGVTLGGTgketgdrhPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHS 298

                          90
                  ....*....|..
gi 1035737233 194 VVAGSPTKLIKV 205
Cdd:PLN02739  299 MVAGNPAKLIGF 310
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-199 2.32e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.79  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 116 DSIIENGVVI-NtraLVE--HGNRIGFCTNISTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNN 192
Cdd:COG1044   222 DTVIGDGTKIdN---LVQiaHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEG 298


                  ....*..
gi 1035737233 193 IVVAGSP 199
Cdd:COG1044   299 GVYSGSP 305
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 116-204 3.62e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.15  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 116 DSIIENGVVI-NtraLVE--HGNRIGFCTNISTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNI-SN 191
Cdd:PRK00892  225 DTVIGEGVKIdN---LVQiaHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEP 301

                          90
                  ....*....|...
gi 1035737233 192 NIVVAGSPTKLIK 204
Cdd:PRK00892  302 GEYSSGIPAQPNK 314
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 153-204 3.65e-09

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 54.05  E-value: 3.65e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIK 204
Cdd:PRK10092  130 VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 105-203 7.08e-09

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: 51.69  E-value: 7.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 105 IYIGKmaivncDSIIENGVVINTRALVEHGNR--IGFCTNISTN-------------VVLNGDVRVGDKSFIGSCTVVNG 169
Cdd:cd04647     2 ISIGD------NVYIGPGCVISAGGGITIGDNvlIGPNVTIYDHnhdiddperpieqGVTSAPIVIGDDVWIGANVVILP 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1035737233 170 QLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLI 203
Cdd:cd04647    76 GVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 107-204 1.50e-08

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: 50.96  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 107 IGKMAIVNCDSIIENGVVIntralvehGNRigfcTNISTNVVLNGDVRVGDKSFIGSC---------------------- 164
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKI--------GDN----VKIQSNVSIYEGVTIEDDVFIGPNvvftndlyprskiyrkwelkgt 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035737233 165 ------------TVVNGqLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIK 204
Cdd:cd03358    69 tvkrgasiganaTILPG-VTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-201 1.84e-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: 52.41  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 116 DSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVV 195
Cdd:cd03352   114 DTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYV 193


                  ....*.
gi 1035737233 196 AGSPTK 201
Cdd:cd03352   194 SGTPAQ 199
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 102-204 2.05e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 52.31  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 102 GICIYIGKMAIVNCDSIIENGVVINTralvehGNRIGFCTNISTNVV---------LNGD-----VRVGDKSFIGSCTVV 167
Cdd:PRK09527   73 GSNIHIGRNFYANFNLTIVDDYTVTI------GDNVLIAPNVTLSVTghpvhhelrKNGEmysfpITIGNNVWIGSHVVI 146

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1035737233 168 NGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIK 204
Cdd:PRK09527  147 NPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 153-203 3.09e-08

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: 51.27  E-value: 3.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLI 203
Cdd:cd03357   119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 150-206 5.71e-08

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: 49.85  E-value: 5.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035737233 150 NGDVRVGDKSFIGS-CTVVNGqLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIKVR 206
Cdd:cd03349    71 KGDVIIGNDVWIGHgATILPG-VTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 95-199 1.30e-07

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 47.82  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  95 ISKRAKLGICIYIGK-MAIV-NCDSIIENGVVINtralveHGNRIGfctnISTNVVLNGDVRVGDKSFIGSCTVVNGQLE 172
Cdd:cd03354     5 IHPGAKIGPGLFIDHgTGIViGETAVIGDNCTIY------QGVTLG----GKGKGGGKRHPTIGDNVVIGAGAKILGNIT 74

                          90       100
                  ....*....|....*....|....*..
gi 1035737233 173 IGSGAIIGSGSVVIRNISNNIVVAGSP 199
Cdd:cd03354    75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 153-206 6.41e-07

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 47.95  E-value: 6.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIKVR 206
Cdd:PRK09677  131 VVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
PLN02357 PLN02357
serine acetyltransferase
 122-203 1.20e-06

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 47.95  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 122 GVVINTRALVehGNRIgfctNISTNVVLNGD--------VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNI 193
Cdd:PLN02357  246 GVVIGETAVV--GNNV----SILHNVTLGGTgkqsgdrhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRT 319

                          90
                  ....*....|
gi 1035737233 194 VVAGSPTKLI 203
Cdd:PLN02357  320 TAVGNPARLI 329
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 153-203 1.88e-06

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 44.90  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLI 203
Cdd:cd05825    57 IVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK10502 PRK10502
putative acyl transferase; Provisional
 153-206 3.69e-06

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 45.33  E-value: 3.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1035737233 153 VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIKVR 206
Cdd:PRK10502  125 IVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
PLN02694 PLN02694
serine O-acetyltransferase
 122-203 4.23e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 46.17  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 122 GVVINTRALVehGNRIgfctNISTNVVLNGD--------VRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNI 193
Cdd:PLN02694  180 GVVIGETAVI--GNNV----SILHHVTLGGTgkacgdrhPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRT 253

                          90
                  ....*....|
gi 1035737233 194 VVAGSPTKLI 203
Cdd:PLN02694  254 TAVGNPARLV 263
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 105-204 5.02e-06

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 44.71  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 105 IYIGKmaivncDSIIENGVVINTRAlvEHGNRIGFCTNISTNVVLNGdVRVGDKSFIG-SCTVVNGQlEIGSGAIIGSGS 183
Cdd:cd04645    39 IRIGE------RTNIQDGSVLHVDP--GYPTIIGDNVTVGHGAVLHG-CTIGDNCLIGmGAIILDGA-VIGKGSIVAAGS 108

                          90       100
                  ....*....|....*....|...
gi 1035737233 184 VVIRN--ISNNIVVAGSPTKLIK 204
Cdd:cd04645   109 LVPPGkvIPPGSLVAGSPAKVVR 131
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 90-185 9.02e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  90 DATAIISKRAKLGICIYIGKMAIvncdsiIENGVVIntralvehGNRigfcTNISTNVVLNGDVRVGDKSFIGSCTVVNG 169
Cdd:PRK00892  104 HPSAVIDPSAKIGEGVSIGPNAV------IGAGVVI--------GDG----VVIGAGAVIGDGVKIGADCRLHANVTIYH 165

                          90
                  ....*....|....*.
gi 1035737233 170 QLEIGSGAIIGSGSVV 185
Cdd:PRK00892  166 AVRIGNRVIIHSGAVI 181
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 154-189 2.69e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.08  E-value: 2.69e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1035737233 154 RVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNI 189
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDV 417
cysE PRK11132
serine acetyltransferase; Provisional
 122-203 3.08e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 43.53  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 122 GVVINTRALVEHGnrigfcTNISTNVVLNGDVRV-GDKS-------FIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNI 193
Cdd:PRK11132  161 GIVIGETAVIEND------VSILQSVTLGGTGKTsGDRHpkiregvMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHT 234

                          90
                  ....*....|
gi 1035737233 194 VVAGSPTKLI 203
Cdd:PRK11132  235 TAAGVPARIV 244
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 91-185 5.94e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.70  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  91 ATAIISKRAKLGICIYIGKMAIvncdsiIENGVVIntralvehGNRigfcTNISTNVVLNGDVRVGDKSFIGSCTVVNGQ 170
Cdd:COG1044   101 PSAVIDPSAKIGEGVSIGPFAV------IGAGVVI--------GDG----VVIGPGVVIGDGVVIGDDCVLHPNVTIYER 162

                          90
                  ....*....|....*
gi 1035737233 171 LEIGSGAIIGSGSVV 185
Cdd:COG1044   163 CVIGDRVIIHSGAVI 177
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 155-192 6.75e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.79  E-value: 6.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1035737233 155 VGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNN 192
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDG 438
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 105-185 9.16e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.54  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 105 IYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNIstnvVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSV 184
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGP----NEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76


                  .
gi 1035737233 185 V 185
Cdd:cd00208    77 V 77
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 143-202 2.15e-04

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 40.88  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 143 ISTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKL 202
Cdd:cd03351   129 LANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 105-204 4.74e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 39.24  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 105 IYIGKmaivncDSIIENGVVIntRALVEHGNRIGFCTNISTNVVLNGdVRVGDKSFIG-SCTVVNGqLEIGSGAIIGSGS 183
Cdd:COG0663    50 IRIGE------GSNIQDGVVL--HVDPGYPLTIGDDVTIGHGAILHG-CTIGDNVLIGmGAIVLDG-AVIGDGSIVGAGA 119

                          90       100
                  ....*....|....*....|...
gi 1035737233 184 VVIRN--ISNNIVVAGSPTKLIK 204
Cdd:COG0663   120 LVTEGkvVPPGSLVVGSPAKVVR 142
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 118-185 1.53e-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: 38.16  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1035737233 118 IIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVV 185
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 155-204 1.65e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.59  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1035737233 155 VGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVVAGSPTKLIK 204
Cdd:PRK14357  386 IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 155-192 2.04e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 37.78  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1035737233 155 VGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNN 192
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPG 184
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 116-202 2.78e-03

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: 37.69  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 116 DSIIENGVVIntralvehgnrigfctniSTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVV 195
Cdd:COG1043   122 DCVVGNNVIL------------------ANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLA 183


                  ....*..
gi 1035737233 196 AGSPTKL 202
Cdd:COG1043   184 AGNPARL 190
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 93-199 2.83e-03

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  93 AIISKRAklgiciYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVG--------------DK 158
Cdd:cd03350     8 AIIRDGA------FIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGgvleplqatpviieDD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035737233 159 SFIGS-CTVVNGQLeIGSGAIIGSGSVVIRNIS----------------NNIVVAGSP 199
Cdd:cd03350    82 VFIGAnCEVVEGVI-VGKGAVLAAGVVLTQSTPiydretgeiyygrvppGSVVVAGSL 138
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 155-189 3.48e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 37.70  E-value: 3.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1035737233 155 VGDKSFIGSctvvNGQL----EIGSGAIIGSGSVVIRNI 189
Cdd:COG1207   397 IGDGAFIGS----NTNLvapvTIGDGATIGAGSTITKDV 431
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 105-204 4.13e-03

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 36.39  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 105 IYIGKmaivncDSIIENGVVINTralvEHG--NRIGFCTNISTNVVLNGdVRVGDKSFIGSCTVVNGQLEIGSGAIIGSG 182
Cdd:cd04650    40 IYIGK------YSNVQENVSIHT----DHGypTEIGDYVTIGHNAVVHG-AKVGNYVIVGMGAILLNGAKIGDHVIIGAG 108

                          90       100
                  ....*....|....*....|....
gi 1035737233 183 SVVIRN--ISNNIVVAGSPTKLIK 204
Cdd:cd04650   109 AVVTPGkeIPDYSLVLGVPAKVVR 132
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 99-201 4.52e-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: 37.42  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  99 AKLGICIYIGKMAIVNCDSI-IENGVVINTRALVE----HGNRIGFctnistnvvlnGDVRVGDKSFIGSCTVVNGQLEI 173
Cdd:TIGR02353 113 AKIGKGVDIGSLPPVCTDLLtIGAGTIVRKEVMLLgyraERGRLHT-----------GPVTLGRDAFIGTRSTLDIDTSI 181

                          90       100       110
                  ....*....|....*....|....*....|
gi 1035737233 174 GSGAIIGSGSVVIRN--ISNNIVVAGSPTK 201
Cdd:TIGR02353 182 GDGAQLGHGSALQGGqsIPDGERWHGSPAQ 211
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 99-181 5.08e-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: 36.62  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233  99 AKLGICIYIGKMAIVNCDSIIENGVVINTRALVEHGNRIGFCTNISTNVVLNGDVRVGDKSfigsctvvngqlEIGSGAI 178
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRV------------IIHSGAV 69


                  ...
gi 1035737233 179 IGS 181
Cdd:cd03352    70 IGS 72
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
116-202 8.51e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.23  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035737233 116 DSIIENGVVIntralvehgnrigfctniSTNVVLNGDVRVGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVV 195
Cdd:PRK05289  123 DCVVGNHVIL------------------ANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLA 184


                  ....*..
gi 1035737233 196 AGSPTKL 202
Cdd:PRK05289  185 EGNPARL 191
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 155-195 8.81e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 36.54  E-value: 8.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1035737233 155 VGDKSFIGSCTVVNGQLEIGSGAIIGSGSVVIRNISNNIVV 195
Cdd:PRK09451  397 IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
 
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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