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Conserved domains on  [gi|742932864|ref|WP_039025009|]
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MULTISPECIES: colanic acid biosynthesis acetyltransferase WcaB [Enterobacter]

Protein Classification

serine acetyltransferase( domain architecture ID 11484606)

serine acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10191 PRK10191
putative acyl transferase; Provisional
 18-163 1.15e-100

putative acyl transferase; Provisional


:

Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  18 MVLAYRIAHFCSVWRKKNVLNNIWAAPVLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGV 97
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742932864  98 TIGNRGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVKVIK 163
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
 
Name Accession Description Interval E-value
PRK10191 PRK10191
putative acyl transferase; Provisional
 18-163 1.15e-100

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  18 MVLAYRIAHFCSVWRKKNVLNNIWAAPVLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGV 97
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742932864  98 TIGNRGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVKVIK 163
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
WcaB TIGR04016
colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases ...
 18-163 5.49e-99

colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188531  Cd Length: 146  Bit Score: 281.45  E-value: 5.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864   18 MVLAYRIAHFCSVWRKKNVLNNIWAAPVLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGV 97
Cdd:TIGR04016   1 MVLAYRIAHFCSVWRKKNVLNNLWAAPVLVLYRLITECLFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742932864   98 TIGNRGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVKVIK 163
Cdd:TIGR04016  81 TIGNRGADSLACPVIGNGVELGANVIILGDITIGNNVTIGAGSVVLDSIPDNALVVGEKARVKVIK 146
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 19-159 1.55e-41

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: 136.75  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  19 VLAYRIAHFCsvWRKKnvlnniwaapVLVLYRIITE---CFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRH 95
Cdd:COG1045   35 LALHRLAHWL--WKRG----------LPLLARLLSErarFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQ 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742932864  96 GVTIGNRGPDSLA-CPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:COG1045  103 GVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 57-154 3.32e-39

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: 128.33  E-value: 3.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  57 FGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIGNRGPDSLA-CPVIGNNVELGANVVIIGDITIGNNVT 135
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKrHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90
                 ....*....|....*....
gi 742932864 136 IGAGSVVLDTIPDNALVVG 154
Cdd:cd03354   81 IGANAVVTKDVPANSTVVG 99
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
110-138 1.30e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 1.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 742932864  110 PVIGNNVELGANVVIIGDITIGNNVTIGA 138
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PRK10191 PRK10191
putative acyl transferase; Provisional
 18-163 1.15e-100

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  18 MVLAYRIAHFCSVWRKKNVLNNIWAAPVLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGV 97
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742932864  98 TIGNRGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVKVIK 163
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
WcaB TIGR04016
colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases ...
 18-163 5.49e-99

colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.


Pssm-ID: 188531  Cd Length: 146  Bit Score: 281.45  E-value: 5.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864   18 MVLAYRIAHFCSVWRKKNVLNNIWAAPVLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGV 97
Cdd:TIGR04016   1 MVLAYRIAHFCSVWRKKNVLNNLWAAPVLVLYRLITECLFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742932864   98 TIGNRGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVKVIK 163
Cdd:TIGR04016  81 TIGNRGADSLACPVIGNGVELGANVIILGDITIGNNVTIGAGSVVLDSIPDNALVVGEKARVKVIK 146
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 19-159 1.55e-41

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: 136.75  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  19 VLAYRIAHFCsvWRKKnvlnniwaapVLVLYRIITE---CFFGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRH 95
Cdd:COG1045   35 LALHRLAHWL--WKRG----------LPLLARLLSErarFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQ 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742932864  96 GVTIGNRGPDSLA-CPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:COG1045  103 GVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 57-154 3.32e-39

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: 128.33  E-value: 3.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  57 FGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIGNRGPDSLA-CPVIGNNVELGANVVIIGDITIGNNVT 135
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKrHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90
                 ....*....|....*....
gi 742932864 136 IGAGSVVLDTIPDNALVVG 154
Cdd:cd03354   81 IGANAVVTKDVPANSTVVG 99
PLN02739 PLN02739
serine acetyltransferase
 21-159 4.24e-22

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 90.48  E-value: 4.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  21 AYRIAHfcSVWRKKNVLnniwaaPVLVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIG 100
Cdd:PLN02739 177 AYRVAH--KLWKQGRKL------LALALQSRVSEVF-GIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLG 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864 101 NRGPDS-LACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PLN02739 248 GTGKETgDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307
PLN02357 PLN02357
serine acetyltransferase
 21-159 2.13e-19

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 83.01  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  21 AYRIAHfcSVWRK-KNVLnniwaapVLVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTI 99
Cdd:PLN02357 198 AHRIAH--KLWTQgRKIL-------ALLIQNRVSEAF-AVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742932864 100 GNRGPDS-LACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PLN02357 268 GGTGKQSgDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARL 328
PLN02694 PLN02694
serine O-acetyltransferase
 21-159 1.87e-18

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 79.69  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  21 AYRIAHfcSVWRKKNvlnniwaAPV-LVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTI 99
Cdd:PLN02694 132 AHRVAH--KLWTQSR-------RPLaLALHSRISDVF-AVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTL 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742932864 100 GNRGPdslAC----PVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PLN02694 202 GGTGK---ACgdrhPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARL 262
cysE PRK11132
serine acetyltransferase; Provisional
 21-159 4.24e-17

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 75.89  E-value: 4.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  21 AYRIAHFcsVWRKKNVlnniwaAPVLVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIG 100
Cdd:PRK11132 113 AYRIGHW--LWNQGRR------ALAIYLQNQISVAF-QVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLG 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864 101 NRGPDS-LACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PRK11132 184 GTGKTSgDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 108-159 8.87e-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: 72.84  E-value: 8.87e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 108 ACPV-IGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:cd03357  116 AKPItIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARV 168
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
66-159 9.87e-15

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 66.82  E-value: 9.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  66 TIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIGN---------RGPDSLACPVIGNNVELGANVVIIGDITIGNNVTI 136
Cdd:COG0110   29 TIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTgnhpiddpaTFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVV 108

                         90       100
                 ....*....|....*....|...
gi 742932864 137 GAGSVVLDTIPDNALVVGEKARV 159
Cdd:COG0110  109 GAGSVVTKDVPPYAIVAGNPARV 131
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 66-159 8.26e-13

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 60.93  E-value: 8.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  66 TIGRRFTIHHGYAVVINKFVVAGDDFTIR---HGVTIGNRGPDSLACP---VIGNNVELGANVVIIGDITIGNNVTIGAG 139
Cdd:cd04647    9 YIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSapiVIGDDVWIGANVVILPGVTIGDGAVVGAG 88

                         90       100
                 ....*....|....*....|
gi 742932864 140 SVVLDTIPDNALVVGEKARV 159
Cdd:cd04647   89 SVVTKDVPPNSIVAGNPAKV 108
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 61-154 1.13e-12

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: 62.90  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864   61 IQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGnrgpdslACPVIGNNVELGANVVIIGDITIGNNVTIGAGS 140
Cdd:TIGR03570 114 INPDVRIGDNVIINTG--AIVEHDCVIGDFVHIAPGVTLS-------GGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGA 184

                          90
                  ....*....|....
gi 742932864  141 VVLDTIPDNALVVG 154
Cdd:TIGR03570 185 VVTKDIPDGGVVVG 198
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 60-160 1.54e-12

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: 60.59  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  60 EIQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGN--------RGPDSLACPVIGNNVELGANVVIIGDITIG 131
Cdd:cd03358   12 FIENDVKIGDNVKIQSN--VSIYEGVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANATILPGVTIG 89

                         90       100
                 ....*....|....*....|....*....
gi 742932864 132 NNVTIGAGSVVLDTIPDNALVVGEKARVK 160
Cdd:cd03358   90 EYALVGAGAVVTKDVPPYALVVGNPARII 118
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 67-159 3.38e-12

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 61.56  E-value: 3.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  67 IGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIGNRG-P---------DSLACPV-IGNNVELGANVVIIGDITIGNNVT 135
Cdd:PRK09527  78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhPvhhelrkngEMYSFPItIGNNVWIGSHVVINPGVTIGDNSV 157

                         90       100
                 ....*....|....*....|....
gi 742932864 136 IGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PRK09527 158 IGAGSVVTKDIPPNVVAAGVPCRV 181
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-163 6.59e-12

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 62.25  E-value: 6.59e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGeKARVKVIK 163
Cdd:PRK14360 392 VIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA-RSRQVIKE 443
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 61-154 8.43e-12

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 60.19  E-value: 8.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRrftihhgyAVVINKFVVAGDDFTIRHGVTIgnrgpdslaCP--------VIGNNVELGANVVIIGDITIGN 132
Cdd:cd03360  111 INPDARIGD--------NVIINTGAVIGHDCVIGDFVHI---------APgvvlsggvTIGEGAFIGAGATIIQGVTIGA 173

                         90       100
                 ....*....|....*....|..
gi 742932864 133 NVTIGAGSVVLDTIPDNALVVG 154
Cdd:cd03360  174 GAIIGAGAVVTKDVPDGSVVVG 195
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 65-143 1.24e-10

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: 54.56  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  65 ATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGN-RGPDSLACPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVL 143
Cdd:cd00208    1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAaTGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 111-160 1.47e-09

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: 55.42  E-value: 1.47e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVgekARVK 160
Cdd:COG1207  396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAI---ARAR 442
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 111-155 2.59e-09

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 53.58  E-value: 2.59e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGE 155
Cdd:cd03353  146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIAR 190
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 111-163 7.76e-09

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 52.19  E-value: 7.76e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKArvKVIK 163
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPA--KIIK 182
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 107-159 8.81e-09

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 52.12  E-value: 8.81e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 742932864 107 LACPV-IGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PRK10092 126 LGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARI 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 65-142 2.07e-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: 51.25  E-value: 2.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742932864  65 ATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGNRGpdslacpVIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:cd03352    2 AKIGENVSIGPN--AVIGEGVVIGDGVVIGPGVVIGDGV-------VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 61-142 2.57e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.56  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGnrgPDSlacpVIGNNVELGANVVIIGDITIGNNVTIGAGS 140
Cdd:COG1044  105 IDPSAKIGEGVSIGPF--AVIGAGVVIGDGVVIGPGVVIG---DGV----VIGDDCVLHPNVTIYERCVIGDRVIIHSGA 175


                 ..
gi 742932864 141 VV 142
Cdd:COG1044  176 VI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 61-142 3.03e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.29  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGnrgPDSlacpVIGNNVELGANVVIIGDITIGNNVTIGAGS 140
Cdd:PRK00892 109 IDPSAKIGEGVSIGPN--AVIGAGVVIGDGVVIGAGAVIG---DGV----KIGADCRLHANVTIYHAVRIGNRVIIHSGA 179


                 ..
gi 742932864 141 VV 142
Cdd:PRK00892 180 VI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 93-154 4.94e-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: 50.10  E-value: 4.94e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  93 IRHGVTIGNRgpdSLACP--------VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVG 154
Cdd:cd03352  129 IAHNVRIGEN---CLIAAqvgiagstTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 66-160 5.29e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 49.64  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  66 TIGRRF------TIH--HGYAVVInkfvvaGDDFTIRHGVTIgnrgpdsLACpVIGNNVELGANVVIIGDITIGNNVTIG 137
Cdd:COG0663   51 RIGEGSniqdgvVLHvdPGYPLTI------GDDVTIGHGAIL-------HGC-TIGDNVLIGMGAIVLDGAVIGDGSIVG 116

                         90       100
                 ....*....|....*....|....*
gi 742932864 138 AGSVVLD--TIPDNALVVGEKARVK 160
Cdd:COG0663  117 AGALVTEgkVVPPGSLVVGSPAKVV 141
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 61-142 7.95e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 50.40  E-value: 7.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGNRG----PD---------SLACPVIGNNVELGANVVI--- 124
Cdd:COG1044  141 IGDGVVIGDDCVLHPN--VTIYERCVIGDRVIIHSGAVIGADGfgfaPDedggwvkipQLGRVVIGDDVEIGANTTIdrg 218

                         90       100       110
                 ....*....|....*....|....*....|.
gi 742932864 125 ------IGD-------ITIGNNVTIGAGSVV 142
Cdd:COG1044  219 algdtvIGDgtkidnlVQIAHNVRIGEHTAI 249
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 72-159 2.24e-07

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: 47.56  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  72 TIH--HGYAVVINKFVVAGDDFTIrHGVTIGNrgpdslacpvignNVELGANVVIIGDITIGNNVTIGAGSVVLD--TIP 147
Cdd:cd04650   53 SIHtdHGYPTEIGDYVTIGHNAVV-HGAKVGN-------------YVIVGMGAILLNGAKIGDHVIIGAGAVVTPgkEIP 118

                         90
                 ....*....|..
gi 742932864 148 DNALVVGEKARV 159
Cdd:cd04650  119 DYSLVLGVPAKV 130
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 66-160 2.35e-07

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 47.41  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  66 TIGRRF------TIH--HGYAVVInkfvvaGDDFTIRHGVTIGnrgpdslACpVIGNNVELGANVVIIGDITIGNNVTIG 137
Cdd:cd04645   40 RIGERTniqdgsVLHvdPGYPTII------GDNVTVGHGAVLH-------GC-TIGDNCLIGMGAIILDGAVIGKGSIVA 105

                         90       100
                 ....*....|....*....|....*
gi 742932864 138 AGSVVL--DTIPDNALVVGEKARVK 160
Cdd:cd04645  106 AGSLVPpgKVIPPGSLVAGSPAKVV 130
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 61-142 2.93e-07

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: 47.79  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVINKFVVAGDDFTIRHGVTIGNRG----PD--------SLACPVIGNNVELGANVVI---- 124
Cdd:cd03352   34 IGDGVVIGDDCVIHPN--VTIYEGCIIGDRVIIHSGAVIGSDGfgfaPDgggwvkipQLGGVIIGDDVEIGANTTIdrga 111

                         90       100       110
                 ....*....|....*....|....*....|
gi 742932864 125 -----IGD-------ITIGNNVTIGAGSVV 142
Cdd:cd03352  112 lgdtvIGDgtkidnlVQIAHNVRIGENCLI 141
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 111-154 3.30e-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: 48.48  E-value: 3.30e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVG 154
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG 303
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 66-159 4.08e-07

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 46.77  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  66 TIGRRFTIHHGYAVVINKFVVAGDDFTIRHGVTIGNRG---------------------------PDSLACPVIGNNVEL 118
Cdd:cd03349    3 SVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGnhptdwvstypfyifggeweddakfddWPSKGDVIIGNDVWI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 742932864 119 GANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:cd03349   83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKV 123
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 111-154 4.90e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.83  E-value: 4.90e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVG 154
Cdd:PRK00892 263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSS 306
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 61-142 1.44e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.67  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVINKFVVAGDD------FTIRHGVTIGNR---------GPD---------------SLACP 110
Cdd:PRK00892 127 IGAGVVIGDGVVIGAG--AVIGDGVKIGADcrlhanVTIYHAVRIGNRviihsgaviGSDgfgfandrggwvkipQLGRV 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 742932864 111 VIGNNVELGANVVI---------IGD-------ITIGNNVTIGAGSVV 142
Cdd:PRK00892 205 IIGDDVEIGANTTIdrgalddtvIGEgvkidnlVQIAHNVVIGRHTAI 252
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-160 1.65e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 46.56  E-value: 1.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVgekARVK 160
Cdd:PRK09451 396 IIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVI---SRVP 442
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-154 3.31e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.59  E-value: 3.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVG 154
Cdd:PRK14354 395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-159 6.48e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 6.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742932864 113 GNNVELGANVVIIGDITIGNNVTIGAGSVVLD-TIPDNALV----VGEKARV 159
Cdd:PRK09451 269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNcVIGDDCEIspysVVEDANL 320
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 70-159 7.52e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.95  E-value: 7.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  70 RFTIHHGYAVVINKFVVAGDDFTIRHGVTIGNRgpdslacPVIGNNVELGANVVIIgDITIGNNVTIGAGSVVLDTIPDN 149
Cdd:cd03353    1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGK-------TVIGEDCVIGPNCVIK-DSTIGDGVVIKASSVIEGAVIGN 72

                         90
                 ....*....|
gi 742932864 150 ALVVGEKARV 159
Cdd:cd03353   73 GATVGPFAHL 82
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
110-138 1.30e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 1.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 742932864  110 PVIGNNVELGANVVIIGDITIGNNVTIGA 138
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-160 1.80e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.56  E-value: 1.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVgekARVK 160
Cdd:PRK14356 400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAI---ARGR 446
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 91-160 1.81e-05

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: 43.48  E-value: 1.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  91 FTIRHGVTIGnrgPDslacpvignnVELGANVVIIGDITIGNNVTIGAGSVVLDTipdnalVVGEKARVK 160
Cdd:COG1207  261 TYIDGDVEIG---RD----------VVIDPNVILEGKTVIGEGVVIGPNCTLKDS------TIGDGVVIK 311
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-155 3.12e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 43.00  E-value: 3.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGE 155
Cdd:PRK14352 401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSE 445
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-154 3.79e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.54  E-value: 3.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVG 154
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 61-142 4.76e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.03  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyAVV-----INKF------VVAGDDFTIRHGVTIgNRGPDS-------------LA-------C 109
Cdd:cd03351   44 IDGPTTIGKNNRIFPF-ASIgeapqDLKYkgeptrLEIGDNNTIREFVTI-HRGTAQgggvtrignnnllMAyvhvahdC 121

                         90       100       110
                 ....*....|....*....|....*....|...
gi 742932864 110 pVIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:cd03351  122 -VIGNNVILANNATLAGHVEIGDYAIIGGLSAV 153
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 111-161 5.21e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 5.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLD--TIPDNALVvgeKARVKV 161
Cdd:PRK00892 114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDgvKIGADCRL---HANVTI 163
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 61-144 6.43e-05

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: 41.48  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864   61 IQAAATIGRRFTIHHGyAVV-----INKF------VVAGDDFTIRHGVTIgNRGPDS-LACPVIGNNVELGANVVIIGDI 128
Cdd:TIGR01852  43 ILGHTTIGEGTRIFPG-AVIggvpqDLKYkgektrLIIGDNNTIREFVTI-NRGTASgGGVTRIGNNNLLMAYSHIAHDC 120

                          90       100
                  ....*....|....*....|.
gi 742932864  129 TIGNNVTIG-----AGSVVLD 144
Cdd:TIGR01852 121 VVGNHVILAnnatlAGHVEVG 141
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-160 6.83e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  78 AVVINKFVVAGDDFTIRHGVTIGnrGPdslacPVIGNNVELGANVVIiGDITIGNNVTIGAGSVVLDTIPDNALVVGEKA 157
Cdd:PRK14355 262 TTYIDRGVVIGRDTTIYPGVCIS--GD-----TRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLEDSVVGDDVAIGPMA 333


                 ...
gi 742932864 158 RVK 160
Cdd:PRK14355 334 HLR 336
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
61-142 7.18e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyAVV-----INKF------VVAGDDFTIRHGVTIgNRGPDS-------------LA-------C 109
Cdd:PRK05289  47 IDGHTTIGKNNRIFPF-ASIgedpqDLKYkgeptrLVIGDNNTIREFVTI-NRGTVQgggvtrigdnnllMAyvhvahdC 124

                         90       100       110
                 ....*....|....*....|....*....|...
gi 742932864 110 pVIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:PRK05289 125 -VVGNHVILANNATLAGHVEVGDYAIIGGLTAV 156
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 61-142 1.45e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.77  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  61 IQAAATIGRRFTIHHGyaVVI------NKF------VVAGDDFTIRHGVTIgNRGPDS-------------LA------- 108
Cdd:COG1043   46 IEGPTTIGKNNRIFPF--ASIgeepqdLKYkgeptrLEIGDNNTIREFVTI-HRGTVQgggvtrigddnllMAyvhvahd 122

                         90       100       110
                 ....*....|....*....|....*....|....
gi 742932864 109 CpVIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:COG1043  123 C-VVGNNVILANNATLAGHVEVGDHAIIGGLSAV 155
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 111-161 1.46e-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: 1.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLD--TIPDNALVvgeKARVKV 161
Cdd:COG1044  110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDgvVIGDDCVL---HPNVTI 159
PRK10502 PRK10502
putative acyl transferase; Provisional
 111-160 1.71e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.93  E-value: 1.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARVK 160
Cdd:PRK10502 126 VIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 111-160 1.95e-04

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: 39.71  E-value: 1.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTipdnalVVGEKARVK 160
Cdd:cd03353   17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDS------TIGDGVVIK 60
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-163 3.35e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.97  E-value: 3.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVgEKARVKVIK 163
Cdd:PRK14359 369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAI-SRAPQKNIK 420
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
111-142 3.58e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 3.58e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:PRK05289  34 VIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 111-142 5.48e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 38.85  E-value: 5.48e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:COG1043   33 EIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-163 5.92e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.98  E-value: 5.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGeKARvKVIK 163
Cdd:PRK14357 385 FIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALG-RAR-QIVK 435
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 111-160 6.20e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.84  E-value: 6.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDItIGNNVTIGAGSVVLDTIPDNALVVGEKARVK 160
Cdd:cd03356   18 VIGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIIGDNAVIGENVRVV 66
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 111-158 7.54e-04

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 37.20  E-value: 7.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKAR 158
Cdd:cd05825   58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAV 105
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 84-144 1.40e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.39  E-value: 1.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742932864  84 FVVAGDDFTIRHGVTIGNRgpdslacPVIGNNVELGANVVIIGDITIGNNVTIGAGSVVLD 144
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEG-------VVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYE 54
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-159 1.95e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:PRK14355 399 VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQV 447
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 111-142 2.09e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 37.03  E-value: 2.09e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 742932864 111 VIGNNVELGANVVIIGDITIGNNVTIGAGSVV 142
Cdd:cd03351   31 EIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 70-160 4.27e-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: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742932864  70 RFTIHHGYAVVINKFVVagddftIRHGVTIGNRgpdslacpvignnVELGANVVIiGDITIGNNVTIGAGSVVLDTIPDN 149
Cdd:PRK09451 263 RGTLTHGRDVEIDTNVI------IEGNVTLGNR-------------VKIGAGCVL-KNCVIGDDCEISPYSVVEDANLGA 322

                         90
                 ....*....|.
gi 742932864 150 ALVVGEKARVK 160
Cdd:PRK09451 323 ACTIGPFARLR 333
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 111-145 5.25e-03

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: 34.74  E-value: 5.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 742932864 111 VIGNNVELGANVVII--GDITIGNNVTIGAGSVVLDT 145
Cdd:cd04647    3 SIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDH 39
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 111-160 5.74e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.09  E-value: 5.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 742932864 111 VIGNNVELGANVVIIGDItIGNNVTIGAGSVVLDTIPDNALVVGEKARVK 160
Cdd:cd05787   18 VIGRNCKIGKNVVIDNSY-IWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
COG4801 COG4801
Predicted acyltransferase, contains DUF342 domain [General function prediction only];
114-159 7.04e-03

Predicted acyltransferase, contains DUF342 domain [General function prediction only];


Pssm-ID: 443829 [Multi-domain]  Cd Length: 283  Bit Score: 35.66  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 742932864 114 NNVELGANVVIIGDITIGN-NVTIGAGSVVLDTIPDNALVVGEKARV 159
Cdd:COG4801  217 GDIVVGSGTTIHGDVTTRNgTVTIEAGAHVLGDVSAEDLVLHEGARV 263
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 112-150 7.76e-03

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: 34.40  E-value: 7.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 742932864 112 IGNNVELGANVVIIGDITIGNNVTIGAGSVVLD--TIPDNA 150
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEgvTIEDDV 41
 
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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