NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489126955|ref|WP_003036750|]
View 

MULTISPECIES: colanic acid biosynthesis acetyltransferase WcaF [Citrobacter]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1-180 1.75e-130

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


The actual alignment was detected with superfamily member TIGR04008:

Pssm-ID: 469633  Cd Length: 180  Bit Score: 363.13  E-value: 1.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955    1 MQDLSGFKVPGGFRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   81 GDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 489126955  161 LPANVICRGNPAVVTRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
 
Name Accession Description Interval E-value
WcaF TIGR04008
colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl ...
 1-180 1.75e-130

colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)


Pssm-ID: 188523  Cd Length: 180  Bit Score: 363.13  E-value: 1.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955    1 MQDLSGFKVPGGFRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   81 GDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 489126955  161 LPANVICRGNPAVVTRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 3.27e-121

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 339.62  E-value: 3.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   1 MQDLSGFKVPGGFRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502   1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  81 GDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:PRK10502  81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                        170       180
                 ....*....|....*....|..
gi 489126955 161 LPANVICRGNPAVVTRERVEKV 182
Cdd:PRK10502 161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 3-178 1.35e-76

hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic acid biosynthesis acetyltransferase WcaF, which acts on a fucose residue in a disaccharide attached to a lipid carrier.


Pssm-ID: 439606  Cd Length: 178  Bit Score: 226.80  E-value: 1.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   3 DLSGFKvpggfRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGD 82
Cdd:NF038307   8 DQSWFD-----RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  83 DAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLP 162
Cdd:NF038307  83 DVVLYSLDRIRIGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMP 162

                        170
                 ....*....|....*.
gi 489126955 163 ANVICRGNPAVVTRER 178
Cdd:NF038307 163 AGQVCWGSPCRPRYPR 178
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 69-173 8.69e-58

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: 176.64  E-value: 8.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  69 PWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDG 148
Cdd:cd05825    1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*
gi 489126955 149 TVVGARSSVFKSLPANVICRGNPAV 173
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAV 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
50-181 1.89e-46

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 148.87  E-value: 1.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  50 FGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINAT-PIVVG 128
Cdd:COG0110    7 FGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTgPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489126955 129 DKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRERVEK 181
Cdd:COG0110   86 DDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 1.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 489126955  124 PIVVGDKCWLATDVFVAPGVTIGDGTVVGA 153
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WcaF TIGR04008
colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl ...
 1-180 1.75e-130

colanic acid biosynthesis acetyltransferase WcaF; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species. This acetyltransferase is believed to catalyze the addition of the acetyl group that is attached through an O linkage to the first fucosyl residue of the colanic acid repetitive unit (E unit)


Pssm-ID: 188523  Cd Length: 180  Bit Score: 363.13  E-value: 1.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955    1 MQDLSGFKVPGGFRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:TIGR04008   1 MQDLSGFSVPKGFRGGNAIKVQLWWAVQATLFAWSPQVLYRWRAFLLRLFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   81 GDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:TIGR04008  81 GDDAVLYTLGEITIGAHSVISQKSYLCTGSHDYMSKHFDINATPIVIGEKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160

                         170       180
                  ....*....|....*....|
gi 489126955  161 LPANVICRGNPAVVTRERVE 180
Cdd:TIGR04008 161 LPANKICRGNPAVVTRERVE 180
PRK10502 PRK10502
putative acyl transferase; Provisional
 1-182 3.27e-121

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 339.62  E-value: 3.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   1 MQDLSGFKVPGGFRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWV 80
Cdd:PRK10502   1 MQDLSGYSVPKGFRGASAWKVQLWWAVQATLFAWSPQPLYRWRAFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDYAWI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  81 GDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKS 160
Cdd:PRK10502  81 GDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160

                        170       180
                 ....*....|....*....|..
gi 489126955 161 LPANVICRGNPAVVTRERVEKV 182
Cdd:PRK10502 161 LPANTICRGNPAVPIRPRVETE 182
EPS_acetyl_HpsU NF038307
hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic ...
 3-178 1.35e-76

hormogonium polysaccharide biosynthesis acetyltransferase HpsU; HpsU is related to the colanic acid biosynthesis acetyltransferase WcaF, which acts on a fucose residue in a disaccharide attached to a lipid carrier.


Pssm-ID: 439606  Cd Length: 178  Bit Score: 226.80  E-value: 1.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   3 DLSGFKvpggfRGGGAIKVQLWWAVQATLFRWSPQVMYRWRAFLLRMFGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGD 82
Cdd:NF038307   8 DQSWFD-----RGRPGWYILLWWLVQAIAFPLTPHNFNGFRCWLLRLFGAKIGKGVLIRPTARFTYPWKVEIGDYSWIGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  83 DAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLP 162
Cdd:NF038307  83 DVVLYSLDRIRIGSHCVISQKSYLCTGSHDIQDPAFGLKTAPITIGNGVWVATDCFVAPGVKIGANAVIGARSSVFKDMP 162

                        170
                 ....*....|....*.
gi 489126955 163 ANVICRGNPAVVTRER 178
Cdd:NF038307 163 AGQVCWGSPCRPRYPR 178
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 69-173 8.69e-58

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: 176.64  E-value: 8.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  69 PWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDG 148
Cdd:cd05825    1 PWNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*
gi 489126955 149 TVVGARSSVFKSLPANVICRGNPAV 173
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAV 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
50-181 1.89e-46

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 148.87  E-value: 1.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  50 FGAKIGKNVVIRPSVKItYPWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDINAT-PIVVG 128
Cdd:COG0110    7 FGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTgPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489126955 129 DKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRERVEK 181
Cdd:COG0110   86 DDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 71-174 1.52e-30

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: 107.54  E-value: 1.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  71 KLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFDIN----ATPIVVGDKCWLATDVFVAPGVTIG 146
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEqgvtSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*...
gi 489126955 147 DGTVVGARSSVFKSLPANVICRGNPAVV 174
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKV 108
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 41-174 8.66e-25

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: 94.41  E-value: 8.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  41 RWRAFLLRMFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSH--DYASQHF 118
Cdd:cd03357   33 ERRELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHplDPEERNR 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489126955 119 DI-NATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVV 174
Cdd:cd03357  112 GLeYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARV 168
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 36-177 4.34e-19

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 80.43  E-value: 4.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  36 PQVMYRWRAFLLRMFGaKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYas 115
Cdd:PRK09527  41 PSEVEKRESLIKEMFA-TVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPV-- 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489126955 116 qHFDIN------ATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRE 177
Cdd:PRK09527 118 -HHELRkngemySFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 71-178 1.60e-16

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 73.37  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  71 KLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSYLCTGSHDYASQHFD------------INATPIVVGDKCWLATDVF 138
Cdd:PRK09677  65 KLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHGSFKHSDDfsspnlppdmrtLESSAVVIGQRVWIGENVT 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489126955 139 VAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRER 178
Cdd:PRK09677 145 ILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 60-176 7.07e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 69.07  E-value: 7.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  60 IRPSVKITYPWKLTLGDYAWVGDDAVLYTLGDITIGAHAVisqksyLCTGSHDYASQHfDINAT----------PIVVGD 129
Cdd:PRK10092  62 IEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCM------LAPGVHIYTATH-PLDPVarnsgaelgkPVTIGN 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489126955 130 KCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTR 176
Cdd:PRK10092 135 NVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 71-178 5.42e-12

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: 60.25  E-value: 5.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  71 KLTLGDYAWVGDDAVLYTLGDITIGAHAVISQKSY-LCTGSH--DYASQHFD----------------INATPIVVGDKC 131
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKiGLGGNHptDWVSTYPFyifggeweddakfddwPSKGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489126955 132 WLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRER 178
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 52-171 7.15e-10

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: 55.57  E-value: 7.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  52 AKIGKNVVIRPSVKITYpwkltlgdYAWVGDDAVLYT---LG-DITIGAHAVISQKSYLCTGshdyasqhfdinatpIVV 127
Cdd:cd03360   97 AVIGEGCVIMAGAVINP--------DARIGDNVIINTgavIGhDCVIGDFVHIAPGVVLSGG---------------VTI 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489126955 128 GDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNP 171
Cdd:cd03360  154 GEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-177 5.00e-09

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: 53.57  E-value: 5.00e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489126955 126 VVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRE 177
Cdd:cd03352  152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 53-172 1.91e-08

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 50.19  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  53 KIGKNVVIRPSVKItypwkltlGDYAWVGDDAVLY---TLGD-ITIGAHAVISQKSYLctgshdYASQHFDINATPIVVG 128
Cdd:cd03358    6 IIGTNVFIENDVKI--------GDNVKIQSNVSIYegvTIEDdVFIGPNVVFTNDLYP------RSKIYRKWELKGTTVK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489126955 129 DKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPA 172
Cdd:cd03358   72 RGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPA 115
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 51-172 2.20e-08

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: 51.73  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   51 GAKIGKNVVIRPSVKITYpwkltlgdyawvgddavlytlgDITIGAHAVISQKSYLCTGshdyasqhfdinatpIVVGDK 130
Cdd:TIGR03570 117 DVRIGDNVIINTGAIVEH----------------------DCVIGDFVHIAPGVTLSGG---------------VVIGEG 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489126955  131 CWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPA 172
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 42-172 2.90e-08

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 52.45  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   42 WRAFLLRMFGAKIGKNVVIRpsvkiTYpwKLTLGDYAWVGDDAvlytlgdiTIGAHAVISqksylctgSHDYASQHFDIN 121
Cdd:TIGR02353 588 FLPAILRLLGVKIGRGVYID-----GT--DLTERDLVTIGDDS--------TLNEGSVIQ--------THLFEDRVMKSD 644

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489126955  122 AtpIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFK--SLPANVICRGNPA 172
Cdd:TIGR02353 645 T--VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 54-162 4.38e-07

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 47.21  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  54 IGKNVVIRPSVKIT------YPwkLTLGDYAWVGDDAVLY--TLGD-ITIGAHAVISQKSylctgshdyasqhfdinatp 124
Cdd:cd03359   51 LSEGCVIRPPFKKFskgvafFP--LHIGDYVFIGENCVVNaaQIGSyVHIGKNCVIGRRC-------------------- 108

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489126955 125 iVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVF-KSLP 162
Cdd:cd03359  109 -IIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFiGELP 146
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 51-177 9.37e-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: 46.25  E-value: 9.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIGKNVVIRPSVKitypwKLTLGDYAWVGDDAVLYT-------LGD-ITIGAHAVIsqksYLCTgshdyasqhfdina 122
Cdd:cd04645   23 GSSVWFGAVLRGDVN-----PIRIGERTNIQDGSVLHVdpgyptiIGDnVTVGHGAVL----HGCT-------------- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489126955 123 tpivVGDKCWLATDVFVAPGVTIGDGTVVGARSSVF--KSLPANVICRGNPAVVTRE 177
Cdd:cd04645   80 ----IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 24-175 1.17e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 47.82  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955   24 WWAVQaTLFRWSPQVMYR---WRAFLLRMFGAKIGKNVVIRPSVKITYpwkltlgdyawvgddavlytlGDITIGAHAVI 100
Cdd:TIGR02353  83 FWTVK-RLVDAAPTVLLSgspLYSLYLRALGAKIGKGVDIGSLPPVCT---------------------DLLTIGAGTIV 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489126955  101 SQKSYLCTgshdYASQHFDINATPIVVGDKCWLATDVFVAPGVTIGDGTVVGARSSV--FKSLPANVICRGNPAVVT 175
Cdd:TIGR02353 141 RKEVMLLG----YRAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALqgGQSIPDGERWHGSPAQKT 213
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 52-157 1.44e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 44.16  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDDAvlytlgdiTIGAHAVIsqksylctgshdyASQHFDINATPIVVGDKC 131
Cdd:cd00208    1 VFIGEGVKIHPKAVI--------RGPVVIGDNV--------NIGPGAVI-------------GAATGPNEKNPTIIGDNV 51

                         90       100
                 ....*....|....*....|....*.
gi 489126955 132 WLATDVFVAPGVTIGDGTVVGARSSV 157
Cdd:cd00208   52 EIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 50-171 3.48e-06

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 43.58  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  50 FGAKIGKNVVIRPSVKITYPWKLTLGDYAWVGDDAVLYtlGDITIGAHAVISQKSYlctgshdyasqhfdinatpIVVGD 129
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIY--QGVTLGGKGKGGGKRH-------------------PTIGD 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489126955 130 KCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNP 171
Cdd:cd03354   60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 78-157 2.17e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.47  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  78 AWVGDDAvlyTLG-DITIGAHAVISQksylctgshdyasqhfdiNAtpiVVGDKCWLATDVFVAPGVTIGDGTVVGARSS 156
Cdd:COG1044  103 AVIDPSA---KIGeGVSIGPFAVIGA------------------GV---VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT 158


                 .
gi 489126955 157 V 157
Cdd:COG1044  159 I 159
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-173 2.57e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.47  E-value: 2.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489126955 126 VVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAV 173
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-178 3.55e-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: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIG-----KNVVIRPSVKITYpwkltlgdyawvgddavLYTLGDITIGAHAVISQKSYLCtgSHDYASQHfdinatPI 125
Cdd:PRK14356 345 GARVGnfvemKKAVLGKGAKANH-----------------LTYLGDAEIGAGANIGAGTITC--NYDGVNKH------RT 399

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489126955 126 VVGDKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN--VICRGNPAVVTRER 178
Cdd:PRK14356 400 VIGEGAFIGSNtALVAP-VTIGDGALVGAGSVITKDVPDGslAIARGRQKNLPRKK 454
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 51-181 8.29e-05

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: 41.22  E-value: 8.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIGKN--------VVIrpsvkitypwkltlGDYAWVGDDAVLYtlGDITIGAHAVISQKSYlctgshdyasqhfdina 122
Cdd:COG1045   71 GATIGRGffidhgtgVVI--------------GETAVIGDNVTIY--QGVTLGGTGKEKGKRH----------------- 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489126955 123 tPiVVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRERVEK 181
Cdd:COG1045  118 -P-TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK 174
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 51-154 9.30e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 9.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIGKNVVIrpsvkitypwkltlGDYAWVGDDAVLytlGD-ITIGAHAVISQKSylctgshdyasqhfdinatpiVVGD 129
Cdd:COG1044  108 SAKIGEGVSI--------------GPFAVIGAGVVI---GDgVVIGPGVVIGDGV---------------------VIGD 149

                         90       100
                 ....*....|....*....|....*
gi 489126955 130 KCWLAtdvfvaPGVTIGDGTVVGAR 154
Cdd:COG1044  150 DCVLH------PNVTIYERCVIGDR 168
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 78-157 2.26e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  78 AWVGDDAVLytlG-DITIGAHAVIsqksylctGSHdyasqhfdinatpIVVGDKCWLATDVFVAPGVTIGDGTVVGARSS 156
Cdd:PRK00892 107 AVIDPSAKI---GeGVSIGPNAVI--------GAG-------------VVIGDGVVIGAGAVIGDGVKIGADCRLHANVT 162


                 .
gi 489126955 157 V 157
Cdd:PRK00892 163 I 163
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 86-164 4.09e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  86 LYTLGDITIGAHAVISQKSYLCtgSHDYASQHfdinatPIVVGDKCWLATDV-FVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:PRK14355 367 LTYLGDATIGRNVNIGCGTITC--NYDGVKKH------RTVIEDDVFVGSDVqFVAP-VTVGRNSLIAAGTTVTKDVPPD 437
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-177 8.38e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.07  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIG-----KNVVIRPSVKI---TYpwkltlgdyawvgddavlytLGDITIGAHAVISQKSYLCtgSHDYASQHFdina 122
Cdd:PRK14353 327 GAKVGnfvevKNAKLGEGAKVnhlTY--------------------IGDATIGAGANIGAGTITC--NYDGFNKHR---- 380

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489126955 123 tpIVVGDKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPANVICRGNPAVVTRE 177
Cdd:PRK14353 381 --TEIGAGAFIGSNsALVAP-VTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
124-153 1.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 489126955  124 PIVVGDKCWLATDVFVAPGVTIGDGTVVGA 153
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 73-181 1.97e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 37.31  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  73 TLGDYAWVGDDAVLytLGDITIGAH------AVIsqksylcTGshdyasqhfDINatPIVVGDKC--------------- 131
Cdd:COG0663   12 QIHPSAFVAPTAVV--IGDVTIGEDvsvwpgAVL-------RG---------DVG--PIRIGEGSniqdgvvlhvdpgyp 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126955 132 -WLATDVFVAPGV-----TIGDGTVVGARSSVF--------------------KSLPANVICRGNPAVVTRERVEK 181
Cdd:COG0663   72 lTIGDDVTIGHGAilhgcTIGDNVLIGMGAIVLdgavigdgsivgagalvtegKVVPPGSLVVGSPAKVVRELTEE 147
PLN02357 PLN02357
serine acetyltransferase
 51-172 2.23e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 37.94  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  51 GAKIGKNVVIRPSVKITypwkltLGDYAWVGDDAVLytLGDITIGAHAVISqksylctgshdyASQHFDINATPIVVGDK 130
Cdd:PLN02357 232 GAKIGQGILLDHATGVV------IGETAVVGNNVSI--LHNVTLGGTGKQS------------GDRHPKIGDGVLIGAGT 291

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489126955 131 CWLATdvfvapgVTIGDGTVVGARSSVFKSLPANVICRGNPA 172
Cdd:PLN02357 292 CILGN-------ITIGEGAKIGAGSVVLKDVPPRTTAVGNPA 326
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-168 2.33e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.70  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  89 LGDITIGAHAVISQKSYLCtgSHDYASQHFDInatpivVGDKCWLATDV-FVAPgVTIGDGTVVGARSSVFKSLPAN--V 165
Cdd:PRK09451 367 LGDAEIGDNVNIGAGTITC--NYDGANKFKTI------IGDDVFVGSDTqLVAP-VTVGKGATIGAGTTVTRDVAENelV 437


                 ...
gi 489126955 166 ICR 168
Cdd:PRK09451 438 ISR 440
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 52-153 2.70e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.43  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  52 AKIGKNVVIRPSVKItypwkltlGDYAWVGDDAVlytlgditIGAHAVISQKSylctgshdyasqhfdinatpiVVGDKC 131
Cdd:PRK00892 113 AKIGEGVSIGPNAVI--------GAGVVIGDGVV--------IGAGAVIGDGV---------------------KIGADC 155

                         90       100
                 ....*....|....*....|....*...
gi 489126955 132 WLATDVFVAPGVTIGD------GTVVGA 153
Cdd:PRK00892 156 RLHANVTIYHAVRIGNrviihsGAVIGS 183
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 126-164 5.95e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.27  E-value: 5.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489126955 126 VVGDKCWLATDVFVAPGVTIGDGTVVGARSSVFKSLPAN 164
Cdd:PRK00892 263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEP 301
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 126-164 6.16e-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: 35.86  E-value: 6.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489126955 126 VVGDKCWLATD-VFVAPgVTIGDGTVVGARSSVFKSLPAN 164
Cdd:cd03353  146 VIGDNVFIGSNsQLVAP-VTIGDGATIAAGSTITKDVPPG 184
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-168 9.19e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.06  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126955  52 AKIGKNVVIRPSVKITypwKLTLGDYAWVgddAVLYTLGDITIGAHAVISQKSylCTGSHDYASQHfdinatPIVVGDKC 131
Cdd:PRK14360 332 AQIGSNCRIGNFVEIK---KSQLGEGSKV---NHLSYIGDATLGEQVNIGAGT--ITANYDGVKKH------RTVIGDRS 397

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489126955 132 WL-ATDVFVAPgVTIGDGTVVGARSSVFKSLPAN--VICR 168
Cdd:PRK14360 398 KTgANSVLVAP-ITLGEDVTVAAGSTITKDVPDNslAIAR 436
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH