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Conserved domains on  [gi|16129998|ref|NP_416562|]
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colanic acid biosynthesis acetyltransferase WcaB [Escherichia coli str. K-12 substr. MG1655]

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
 17-162 1.19e-100

putative acyl transferase; Provisional


:

Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.19e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   17 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 96
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129998   97 TIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 162
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
 
Name Accession Description Interval E-value
PRK10191 PRK10191
putative acyl transferase; Provisional
 17-162 1.19e-100

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.19e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   17 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 96
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129998   97 TIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 162
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
WcaB TIGR04016
colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases ...
 17-162 1.15e-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: 282.99  E-value: 1.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998    17 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 96
Cdd:TIGR04016   1 MVLAYRIAHFCSVWRKKNVLNNLWAAPVLVLYRLITECLFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129998    97 TIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 162
Cdd:TIGR04016  81 TIGNRGADSLACPVIGNGVELGANVIILGDITIGNNVTIGAGSVVLDSIPDNALVVGEKARVKVIK 146
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 18-158 3.11e-42

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: 138.29  E-value: 3.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  18 VLAYRVAHFcsvwrkknvlnnLWAAPLLVLYRIITE---CFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRH 94
Cdd:COG1045  35 LALHRLAHW------------LWKRGLPLLARLLSErarFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQ 102

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129998  95 GVTIGNRGADNMA-CPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:COG1045 103 GVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 56-153 9.96e-40

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: 129.48  E-value: 9.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  56 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGAD-NMACPHIGNGVELGANVIILGDITLGNNVT 134
Cdd:cd03354   1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGgGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                        90
                ....*....|....*....
gi 16129998 135 VGAGSVVLDSVPDNALVVG 153
Cdd:cd03354  81 IGANAVVTKDVPANSTVVG 99
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
109-137 5.76e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 5.76e-04
                          10        20
                  ....*....|....*....|....*....
gi 16129998   109 PHIGNGVELGANVIILGDITLGNNVTVGA 137
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PRK10191 PRK10191
putative acyl transferase; Provisional
 17-162 1.19e-100

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 285.63  E-value: 1.19e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   17 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 96
Cdd:PRK10191   1 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129998   97 TIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 162
Cdd:PRK10191  81 TIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
WcaB TIGR04016
colanic acid biosynthesis acetyltransferase WcaB; This gene is one of the acetyl transferases ...
 17-162 1.15e-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: 282.99  E-value: 1.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998    17 MVLAYRVAHFCSVWRKKNVLNNLWAAPLLVLYRIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 96
Cdd:TIGR04016   1 MVLAYRIAHFCSVWRKKNVLNNLWAAPVLVLYRLITECLFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129998    97 TIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 162
Cdd:TIGR04016  81 TIGNRGADSLACPVIGNGVELGANVIILGDITIGNNVTIGAGSVVLDSIPDNALVVGEKARVKVIK 146
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 18-158 3.11e-42

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: 138.29  E-value: 3.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  18 VLAYRVAHFcsvwrkknvlnnLWAAPLLVLYRIITE---CFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRH 94
Cdd:COG1045  35 LALHRLAHW------------LWKRGLPLLARLLSErarFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQ 102

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129998  95 GVTIGNRGADNMA-CPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:COG1045 103 GVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 56-153 9.96e-40

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: 129.48  E-value: 9.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  56 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGAD-NMACPHIGNGVELGANVIILGDITLGNNVT 134
Cdd:cd03354   1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGgGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                        90
                ....*....|....*....
gi 16129998 135 VGAGSVVLDSVPDNALVVG 153
Cdd:cd03354  81 IGANAVVTKDVPANSTVVG 99
PLN02739 PLN02739
serine acetyltransferase
 20-158 2.00e-24

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 96.64  E-value: 2.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   20 AYRVAHfcSVWRKKNVLnnlwaaPLLVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIG 99
Cdd:PLN02739 177 AYRVAH--KLWKQGRKL------LALALQSRVSEVF-GIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLG 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  100 NRGADNM-ACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:PLN02739 248 GTGKETGdRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307
PLN02694 PLN02694
serine O-acetyltransferase
 4-158 1.51e-21

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 88.16  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998    4 DLRANSwsLR-PCCM-----VLAYRVAHFCSVWRkknVLNNLWAA---PL-LVLYRIITECFfGYEIQAAATIGRRFTIH 73
Cdd:PLN02694 103 DLRAAR--VRdPACVsfshcLLNYKGFLACQAHR---VAHKLWTQsrrPLaLALHSRISDVF-AVDIHPAAKIGKGILFD 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   74 HGYAVVINKNVVAGDDFTIRHGVTIGNRGAdnmAC----PHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNA 149
Cdd:PLN02694 177 HATGVVIGETAVIGNNVSILHHVTLGGTGK---ACgdrhPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRT 253


                 ....*....
gi 16129998  150 LVVGEKARV 158
Cdd:PLN02694 254 TAVGNPARL 262
PLN02357 PLN02357
serine acetyltransferase
 20-158 8.85e-21

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 86.86  E-value: 8.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   20 AYRVAHfcSVWRK-KNVLnnlwaaPLLVLYRIiTECFfGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTI 98
Cdd:PLN02357 198 AHRIAH--KLWTQgRKIL------ALLIQNRV-SEAF-AVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129998   99 GNRGAdnmAC----PHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:PLN02357 268 GGTGK---QSgdrhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARL 328
cysE PRK11132
serine acetyltransferase; Provisional
 20-158 1.07e-18

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 80.13  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   20 AYRVAHFcsVWRKKNVlnnlwaAPLLVLYRIITECFfGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIG 99
Cdd:PRK11132 113 AYRIGHW--LWNQGRR------ALAIYLQNQISVAF-QVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLG 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129998  100 NRGAdnmAC----PHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:PRK11132 184 GTGK---TSgdrhPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 64-158 9.59e-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: 9.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  64 ATIGRRFTIHHGYAVVINKNVVAGDDFTIRHG--VTIGN---------------------RGAD-NMACP-HIGNGVELG 118
Cdd:cd03357  49 VYIEPPFHCDYGYNIHIGDNFYANFNCTILDVapVTIGDnvligpnvqiytaghpldpeeRNRGlEYAKPiTIGDNVWIG 128

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16129998 119 ANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:cd03357 129 GGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARV 168
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
65-158 4.95e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 70.28  E-value: 4.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  65 TIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGN---------RGADNMACPHIGNGVELGANVIILGDITLGNNVTV 135
Cdd:COG0110  29 TIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTgnhpiddpaTFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVV 108

                        90       100
                ....*....|....*....|...
gi 16129998 136 GAGSVVLDSVPDNALVVGEKARV 158
Cdd:COG0110 109 GAGSVVTKDVPPYAIVAGNPARV 131
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 65-158 4.78e-15

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: 66.71  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  65 TIGRRFTIHHGYAVVINKNVVAGDDFTIR---HGVTIGNRGADNMACP---HIGNGVELGANVIILGDITLGNNVTVGAG 138
Cdd:cd04647   9 YIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSapiVIGDDVWIGANVVILPGVTIGDGAVVGAG 88

                        90       100
                ....*....|....*....|
gi 16129998 139 SVVLDSVPDNALVVGEKARV 158
Cdd:cd04647  89 SVVTKDVPPNSIVAGNPAKV 108
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 59-159 7.73e-15

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: 66.76  E-value: 7.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  59 EIQAAATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGN--------RGADNMACPHIGNGVELGANVIILGDITLG 130
Cdd:cd03358  12 FIENDVKIGDNVKIQSN--VSIYEGVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANATILPGVTIG 89

                        90       100
                ....*....|....*....|....*....
gi 16129998 131 NNVTVGAGSVVLDSVPDNALVVGEKARVK 159
Cdd:cd03358  90 EYALVGAGAVVTKDVPPYALVVGNPARII 118
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 60-153 3.38e-14

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: 66.75  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998    60 IQAAATIGRrftihhgyAVVINKNVVAGDDFTIRHGVTIGNrGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGS 139
Cdd:TIGR03570 114 INPDVRIGD--------NVIINTGAIVEHDCVIGDFVHIAP-GVTLSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGA 184

                          90
                  ....*....|....
gi 16129998   140 VVLDSVPDNALVVG 153
Cdd:TIGR03570 185 VVTKDIPDGGVVVG 198
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 60-153 8.06e-13

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: 62.89  E-value: 8.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRrftihhgyAVVINKNVVAGDDFTIRHGVTIGNRGADNMACpHIGNGVELGANVIILGDITLGNNVTVGAGS 139
Cdd:cd03360 111 INPDARIGD--------NVIINTGAVIGHDCVIGDFVHIAPGVVLSGGV-TIGEGAFIGAGATIIQGVTIGAGAIIGAGA 181

                        90
                ....*....|....
gi 16129998 140 VVLDSVPDNALVVG 153
Cdd:cd03360 182 VVTKDVPDGSVVVG 195
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 64-142 8.45e-12

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 57.64  E-value: 8.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  64 ATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGNRGADNMACP-HIGNGVELGANVIILGDITLGNNVTVGAGSVVL 142
Cdd:cd00208   1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPtIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 110-162 1.31e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 58.40  E-value: 1.31e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129998  110 HIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGeKARVKVIK 162
Cdd:PRK14360 392 VIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA-RSRQVIKE 443
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 66-158 5.50e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 55.39  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   66 IGRRF------TIHHGYAVVINKNVVAGDDFTIR---HGVTIGNRGADNM-ACP-HIGNGVELGANVIILGDITLGNNVT 134
Cdd:PRK09527  78 IGRNFyanfnlTIVDDYTVTIGDNVLIAPNVTLSvtgHPVHHELRKNGEMySFPiTIGNNVWIGSHVVINPGVTIGDNSV 157

                         90       100
                 ....*....|....*....|....
gi 16129998  135 VGAGSVVLDSVPDNALVVGEKARV 158
Cdd:PRK09527 158 IGAGSVVTKDIPPNVVAAGVPCRV 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 60-141 2.19e-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: 51.94  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGS 139
Cdd:COG1044 105 IDPSAKIGEGVSIGPF--AVIGAGVVIGDGVVIGPGVVIG-DGV------VIGDDCVLHPNVTIYERCVIGDRVIIHSGA 175


                ..
gi 16129998 140 VV 141
Cdd:COG1044 176 VI 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 64-141 2.52e-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: 50.87  E-value: 2.52e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129998  64 ATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGNrGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGSVV 141
Cdd:cd03352   2 AKIGENVSIGPN--AVIGEGVVIGDGVVIGPGVVIGD-GV------VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 65-159 3.28e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 50.03  E-value: 3.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  65 TIGRRF------TIH--HGYAVVInknvvaGDDFTIRHGVTIgnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVG 136
Cdd:COG0663  51 RIGEGSniqdgvVLHvdPGYPLTI------GDDVTIGHGAIL--HGC------TIGDNVLIGMGAIVLDGAVIGDGSIVG 116

                        90       100
                ....*....|....*....|....*
gi 16129998 137 AGSVVLD--SVPDNALVVGEKARVK 159
Cdd:COG0663 117 AGALVTEgkVVPPGSLVVGSPAKVV 141
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 111-162 3.81e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 50.26  E-value: 3.81e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16129998  111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKArvKVIK 162
Cdd:PRK09677 133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPA--KIIK 182
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 60-141 7.95e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.14  E-value: 7.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   60 IQAAATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGS 139
Cdd:PRK00892 109 IDPSAKIGEGVSIGPN--AVIGAGVVIGDGVVIGAGAVIG-DGV------KIGADCRLHANVTIYHAVRIGNRVIIHSGA 179


                 ..
gi 16129998  140 VV 141
Cdd:PRK00892 180 VI 181
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 110-158 9.27e-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: 48.31  E-value: 9.27e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16129998 110 HIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:cd03349  75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKV 123
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 111-158 1.06e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 49.04  E-value: 1.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16129998  111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:PRK10092 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARI 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 92-153 1.43e-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: 48.94  E-value: 1.43e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129998  92 IRHGVTIGNR----GADNMA-CPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVG 153
Cdd:cd03352 129 IAHNVRIGENcliaAQVGIAgSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 65-159 2.55e-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: 2.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  65 TIGRRF------TIH--HGYAVVInknvvaGDDFTIRHGVTIgnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVG 136
Cdd:cd04645  40 RIGERTniqdgsVLHvdPGYPTII------GDNVTVGHGAVL--HGC------TIGDNCLIGMGAIILDGAVIGKGSIVA 105

                        90       100
                ....*....|....*....|....*
gi 16129998 137 AGSVVL--DSVPDNALVVGEKARVK 159
Cdd:cd04645 106 AGSLVPpgKVIPPGSLVAGSPAKVV 130
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 111-159 2.97e-07

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: 48.87  E-value: 2.97e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16129998 111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVgekARVK 159
Cdd:COG1207 397 IGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAI---ARAR 442
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 111-154 3.28e-07

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: 47.80  E-value: 3.28e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16129998 111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGE 154
Cdd:cd03353 147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIAR 190
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 71-158 2.04e-06

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: 44.87  E-value: 2.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  71 TIH--HGYAVVInknvvaGDDFTIRHGVTIgnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDS--VP 146
Cdd:cd04650  53 SIHtdHGYPTEI------GDYVTIGHNAVV--HGA------KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGkeIP 118

                        90
                ....*....|..
gi 16129998 147 DNALVVGEKARV 158
Cdd:cd04650 119 DYSLVLGVPAKV 130
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 60-141 2.20e-06

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: 46.16  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRRFTIHHGyaVVINKNVVAGDDF------TIRHGVTIGNR---------GAD-----------NMACPH--- 110
Cdd:COG1044 123 IGAGVVIGDGVVIGPG--VVIGDGVVIGDDCvlhpnvTIYERCVIGDRviihsgaviGADgfgfapdedggWVKIPQlgr 200

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16129998 111 --IGNGVELGANVII----LGDITLGN------------NVTVGAGSVV 141
Cdd:COG1044 201 vvIGDDVEIGANTTIdrgaLGDTVIGDgtkidnlvqiahNVRIGEHTAI 249
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 60-153 3.90e-06

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: 45.39  E-value: 3.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRRFTIHH---------GYAVVINK---------NVVAGDDFTIRHGVTIgNRGA------------DNMAcp 109
Cdd:COG1044 159 IYERCVIGDRVIIHSgavigadgfGFAPDEDGgwvkipqlgRVVIGDDVEIGANTTI-DRGAlgdtvigdgtkiDNLV-- 235

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129998 110 HIGNGVELGANVII-----------LGD-------------ITLGNNVTVGAGSVVLDSVPDNALVVG 153
Cdd:COG1044 236 QIAHNVRIGEHTAIaaqvgiagstkIGDnvviggqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSG 303
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 60-141 5.98e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 5.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   60 IQAAATIGRRFTIHHGyaVVINKNVVAGDD------FTIRHGVTIGNR---------GAD-----NMACPH--------- 110
Cdd:PRK00892 127 IGAGVVIGDGVVIGAG--AVIGDGVKIGADcrlhanVTIYHAVRIGNRviihsgaviGSDgfgfaNDRGGWvkipqlgrv 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 16129998  111 -IGNGVELGANVII----LGDITLGN------------NVTVGAGSVV 141
Cdd:PRK00892 205 iIGDDVEIGANTTIdrgaLDDTVIGEgvkidnlvqiahNVVIGRHTAI 252
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 110-157 6.82e-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: 42.59  E-value: 6.82e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16129998 110 HIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKAR 157
Cdd:cd05825  58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAV 105
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 112-145 7.04e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.63  E-value: 7.04e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 16129998  112 GNGVELGANVIILGDITLGNNVTVGAGSVVLDSV 145
Cdd:PRK09451 269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCV 302
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 92-153 9.62e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.36  E-value: 9.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129998   92 IRHGVTIGNRGAdnMA-------CPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVG 153
Cdd:PRK00892 240 IAHNVVIGRHTA--IAaqvgiagSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSS 306
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-159 2.65e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.17  E-value: 2.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129998  100 NRGADNMACPH---------IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVgekARVK 159
Cdd:PRK14356 381 NIGAGTITCNYdgvnkhrtvIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAI---ARGR 446
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 69-158 3.96e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 42.02  E-value: 3.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  69 RFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRgadnmacPHIGNGVELGANVIIlGDITLGNNVTVGAGSVVLDSVPDN 148
Cdd:cd03353   1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGK-------TVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVIEGAVIGN 72

                        90
                ....*....|
gi 16129998 149 ALVVGEKARV 158
Cdd:cd03353  73 GATVGPFAHL 82
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 77-159 3.98e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.42  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   77 AVVINKNVVAGDDFTIRHGVTIGNRgadnmacPHIGNGVELGANVIIlGDITLGNNVTVGAGSVVLDSVPDNALVVGEKA 156
Cdd:PRK14355 262 TTYIDRGVVIGRDTTIYPGVCISGD-------TRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLEDSVVGDDVAIGPMA 333


                 ...
gi 16129998  157 RVK 159
Cdd:PRK14355 334 HLR 336
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 111-159 4.52e-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: 42.32  E-value: 4.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16129998 111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSvpdnalVVGEKARVK 159
Cdd:COG1207 269 IGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDS------TIGDGVVIK 311
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
60-141 5.35e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   60 IQAAATIGRRFTIHHGyAVVINKN-----------VVAGDDFTIRHGVTIgNR-----------GADN--MACPHI---- 111
Cdd:PRK05289  47 IDGHTTIGKNNRIFPF-ASIGEDPqdlkykgeptrLVIGDNNTIREFVTI-NRgtvqgggvtriGDNNllMAYVHVahdc 124

                         90       100       110
                 ....*....|....*....|....*....|..
gi 16129998  112 --GNGVELGANVIILGDITLGNNVTVGAGSVV 141
Cdd:PRK05289 125 vvGNHVILANNATLAGHVEVGDYAIIGGLTAV 156
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 110-153 7.34e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.77  E-value: 7.34e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 16129998  110 HIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVG 153
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 60-141 9.55e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 41.16  E-value: 9.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRRFTIHHG-----------YA-----VVInknvvaGDDFTIRHGVTIgNR-----------GADN--MACPH 110
Cdd:COG1043  46 IEGPTTIGKNNRIFPFasigeepqdlkYKgeptrLEI------GDNNTIREFVTI-HRgtvqgggvtriGDDNllMAYVH 118

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16129998 111 ------IGNGVELGANVIILGDITLGNNVTVGAGSVV 141
Cdd:COG1043 119 vahdcvVGNNVILANNATLAGHVEVGDHAIIGGLSAV 155
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 60-141 9.75e-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: 40.88  E-value: 9.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  60 IQAAATIGRRFTIHHGyAVVINKN-----------VVAGDDFTIRHGVTIgNR-----------GADN--MACPHI---- 111
Cdd:cd03351  44 IDGPTTIGKNNRIFPF-ASIGEAPqdlkykgeptrLEIGDNNTIREFVTI-HRgtaqgggvtriGNNNllMAYVHVahdc 121

                        90       100       110
                ....*....|....*....|....*....|..
gi 16129998 112 --GNGVELGANVIILGDITLGNNVTVGAGSVV 141
Cdd:cd03351 122 viGNNVILANNATLAGHVEIGDYAIIGGLSAV 153
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 79-145 1.65e-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: 40.39  E-value: 1.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129998  79 VINKNVVAGDDFTIRHGVTIGnRGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSV 145
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIG-AGV------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC 163
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 111-153 1.94e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 1.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 16129998  111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVG 153
Cdd:PRK14354 396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
PRK10502 PRK10502
putative acyl transferase; Provisional
 111-159 1.95e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.93  E-value: 1.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 16129998  111 IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGEKARVK 159
Cdd:PRK10502 127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 79-145 2.02e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 2.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129998   79 VINKNVVAGDDFTIRHGVTIGNrGAdnmacpHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSV 145
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGA-GV------VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-159 2.03e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.40  E-value: 2.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129998   87 GDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVgekARVK 159
Cdd:PRK09451 373 GDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVI---SRVP 442
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 110-154 2.10e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.31  E-value: 2.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16129998  110 HIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGE 154
Cdd:PRK14352 401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSE 445
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 60-136 3.01e-04

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 39.55  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998    60 IQAAATIGRRFTIHHGyAVVINKN-----------VVAGDDFTIRHGVTIgNRGADN-------------MACPHIGNGV 115
Cdd:TIGR01852  43 ILGHTTIGEGTRIFPG-AVIGGVPqdlkykgektrLIIGDNNTIREFVTI-NRGTASgggvtrignnnllMAYSHIAHDC 120

                          90       100
                  ....*....|....*....|.
gi 16129998   116 ELGANVIILGDITLGNNVTVG 136
Cdd:TIGR01852 121 VVGNHVILANNATLAGHVEVG 141
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
109-137 5.76e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 5.76e-04
                          10        20
                  ....*....|....*....|....*....
gi 16129998   109 PHIGNGVELGANVIILGDITLGNNVTVGA 137
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 84-136 8.81e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.46  E-value: 8.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129998   84 VVAGDDFTIRHGVTI--GNR-------GADN--MACPHIGNGVELGANVIILGDITLGNNVTVG 136
Cdd:PRK12461  78 LEIGDRNVIREGVTIhrGTKgggvtriGNDNllMAYSHVAHDCQIGNNVILVNGALLAGHVTVG 141
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 97-162 9.57e-04

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: 9.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129998   97 TIG---NRGADNMACPH---------IGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVVGeKARvKVIK 162
Cdd:PRK14357 360 TVGknvNIGAGTITCNYdgkkknptfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALG-RAR-QIVK 435
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-159 1.44e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   69 RFTIHHGYAVVINKNVVagddftIRHGVTIGNRgadnmacPHIGNGVelganviILGDITLGNNVTVGAGSVVLDSVPDN 148
Cdd:PRK09451 263 RGTLTHGRDVEIDTNVI------IEGNVTLGNR-------VKIGAGC-------VLKNCVIGDDCEISPYSVVEDANLGA 322

                         90
                 ....*....|.
gi 16129998  149 ALVVGEKARVK 159
Cdd:PRK09451 323 ACTIGPFARLR 333
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 83-152 2.81e-03

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.27  E-value: 2.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   83 NVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGSVVLDSVPDNALVV 152
Cdd:PRK14358 374 DVTIGAETNVGAGTIVANFDGVNKHQSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAV 443
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 64-140 3.96e-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: 36.24  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998  64 ATIGRRFTIH---HGYAVVINKNVVAGDDFTIRHGVTIGNRGadnmacpHIGNGVE-----LGANVII-----LGDITLG 130
Cdd:cd03353  51 STIGDGVVIKassVIEGAVIGNGATVGPFAHLRPGTVLGEGV-------HIGNFVEikkstIGEGSKAnhlsyLGDAEIG 123

                        90
                ....*....|
gi 16129998 131 NNVTVGAGSV 140
Cdd:cd03353 124 EGVNIGAGTI 133
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 60-140 4.79e-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: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129998   60 IQAAATIGRRFTIhhGYAVVInKNVVAGDDFTIR-----HGVTIGNR-----------GADNMACPHIGNGVE-----LG 118
Cdd:PRK09451 280 IEGNVTLGNRVKI--GAGCVL-KNCVIGDDCEISpysvvEDANLGAActigpfarlrpGAELAEGAHVGNFVEmkkarLG 356

                         90       100
                 ....*....|....*....|....*..
gi 16129998  119 ----AN-VIILGDITLGNNVTVGAGSV 140
Cdd:PRK09451 357 kgskAGhLTYLGDAEIGDNVNIGAGTI 383
COG4801 COG4801
Predicted acyltransferase, contains DUF342 domain [General function prediction only];
113-158 5.27e-03

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


Pssm-ID: 443829 [Multi-domain]  Cd Length: 283  Bit Score: 36.04  E-value: 5.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 16129998 113 NGVELGANVIILGDITLGN-NVTVGAGSVVLDSVPDNALVVGEKARV 158
Cdd:COG4801 217 GDIVVGSGTTIHGDVTTRNgTVTIEAGAHVLGDVSAEDLVLHEGARV 263
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 111-159 6.08e-03

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: 34.14  E-value: 6.08e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16129998 111 IGNGVELGANVIILGDItLGNNVTVGAGSVVLDSVPDNALVVGEKARVK 159
Cdd:cd03356  19 IGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIIGDNAVIGENVRVV 66
 
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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