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Conserved domains on  [gi|496080928|ref|WP_008805435|]
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MULTISPECIES: maltose O-acetyltransferase [Klebsiella]

Protein Classification

maltose O-acetyltransferase( domain architecture ID 11484575)

maltose O-acetyltransferase catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 2.67e-143

maltose O-acetyltransferase; Provisional


:

Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 395.72  E-value: 2.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   1 MSEEKRKMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAGDAYIEPSFRCDYGYNIFLGNAF 80
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  81 YANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGA 160
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 496080928 161 VVTKDVPAGAVVGGNPAQIIKRL 183
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 2.67e-143

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 395.72  E-value: 2.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   1 MSEEKRKMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAGDAYIEPSFRCDYGYNIFLGNAF 80
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  81 YANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGA 160
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 496080928 161 VVTKDVPAGAVVGGNPAQIIKRL 183
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-180 5.03e-107

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: 303.57  E-value: 5.03e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  13 LYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAGD-AYIEPSFRCDYGYNIFLGNAFYANFDCVMLDV 91
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGEnVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  92 CPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAV 171
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 496080928 172 VGGNPAQII 180
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
59-184 3.62e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.21  E-value: 3.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  59 DAYIEPSFRCdYGYNIFLGNAFYANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARnsGQEYGKPVTIGHNVWI 138
Cdd:COG0110   14 GVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWI 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 496080928 139 GGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIKRLP 184
Cdd:COG0110   91 GAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 128-182 2.34e-23

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 91.76  E-value: 2.34e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 496080928  128 KPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIKR 182
Cdd:TIGR03308 107 KRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRR 161
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-58 8.49e-23

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 86.01  E-value: 8.49e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496080928    7 KMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAG 58
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-183 2.67e-143

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 395.72  E-value: 2.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   1 MSEEKRKMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAGDAYIEPSFRCDYGYNIFLGNAF 80
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  81 YANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGA 160
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 496080928 161 VVTKDVPAGAVVGGNPAQIIKRL 183
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-180 5.03e-107

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: 303.57  E-value: 5.03e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  13 LYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAGD-AYIEPSFRCDYGYNIFLGNAFYANFDCVMLDV 91
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGEnVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  92 CPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAV 171
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 496080928 172 VGGNPAQII 180
Cdd:cd03357  161 AAGNPARVI 169
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 5-183 8.15e-61

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 187.90  E-value: 8.15e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   5 KRKMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAG-DAYIEPSFRCDYGYNIFLGNAFYAN 83
Cdd:PRK09527   6 TERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGeNAWVEPPVYFSYGSNIHIGRNFYAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  84 FDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVT 163
Cdd:PRK09527  86 FNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVT 165

                        170       180
                 ....*....|....*....|
gi 496080928 164 KDVPAGAVVGGNPAQIIKRL 183
Cdd:PRK09527 166 KDIPPNVVAAGVPCRVIREI 185
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
59-184 3.62e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.21  E-value: 3.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  59 DAYIEPSFRCdYGYNIFLGNAFYANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARnsGQEYGKPVTIGHNVWI 138
Cdd:COG0110   14 GVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWI 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 496080928 139 GGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIKRLP 184
Cdd:COG0110   91 GAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 73-180 1.04e-44

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: 143.75  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  73 NIFLGNAFYANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHPLDAEARNSGQEY-GKPVTIGHNVWIGGRAVINPGVTIG 151
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVtSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 496080928 152 DNAVIASGAVVTKDVPAGAVVGGNPAQII 180
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 73-181 7.22e-37

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: 124.96  E-value: 7.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  73 NIFLGNAFYANFDCVMLDVCPIHIGDNCMLAPGVHI---------YTATHPL-------DAEARNSGQEYGKPVTIGHNV 136
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIglggnhptdWVSTYPFyifggewEDDAKFDDWPSKGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496080928 137 WIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 93-180 1.07e-25

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: 94.98  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  93 PIHIGDNCMLAPGVHIYTATH-------PLDAearnsgqeygKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKD 165
Cdd:cd05825   23 PVTIGSDACISQGAYLCTGSHdyrspafPLIT----------APIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRD 92

                         90
                 ....*....|....*
gi 496080928 166 VPAGAVVGGNPAQII 180
Cdd:cd05825   93 LPAWTVYAGNPAVPV 107
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 128-182 2.34e-23

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 91.76  E-value: 2.34e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 496080928  128 KPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIKR 182
Cdd:TIGR03308 107 KRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRR 161
PRK10502 PRK10502
putative acyl transferase; Provisional
 62-181 2.78e-23

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 91.16  E-value: 2.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  62 IEPSFRCDYGYNIFLGNAFYANFDCVMLDVCPIHIGDNCMLAPGVHIYTATHpldaeaRNSGQEYG---KPVTIGHNVWI 138
Cdd:PRK10502  60 IRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSH------DYSDPHFDlntAPIVIGEGCWL 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496080928 139 GGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK10502 134 AADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 71-181 4.03e-23

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: 88.71  E-value: 4.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  71 GYNIFLGNAFYANFDCVMLDVCPIH----------IGDNCMLAPGVhiyTATHPLDAEARNSGQEYGKPVTIGHNVWIGG 140
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNVKIQsnvsiyegvtIEDDVFIGPNV---VFTNDLYPRSKIYRKWELKGTTVKRGASIGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496080928 141 RAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:cd03358   79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-58 8.49e-23

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 86.01  E-value: 8.49e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496080928    7 KMIAGELYLSGDPTLRADRLRARQLLHRYNHSSPDAQEERQHILAELFGRAG 58
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 95-176 2.11e-21

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: 86.38  E-value: 2.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnSGQeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGG 174
Cdd:cd03360  134 VIGDFVHIAPGVVL-------------SGG-----VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVG 195


                 ..
gi 496080928 175 NP 176
Cdd:cd03360  196 NP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 96-182 6.82e-21

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: 84.75  E-value: 6.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  96 IGDNCMLAPGVhiyT--AThpldaearnsGQEYGK--PvTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAV 171
Cdd:COG1045   94 IGDNVTIYQGV---TlgGT----------GKEKGKrhP-TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                         90
                 ....*....|.
gi 496080928 172 VGGNPAQIIKR 182
Cdd:COG1045  160 VVGVPARIVKR 170
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-177 7.33e-20

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: 82.54  E-value: 7.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   95 HIGDNCMLAPGVHIytathpldaearnSGQeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGG 174
Cdd:TIGR03570 137 VIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198


                  ...
gi 496080928  175 NPA 177
Cdd:TIGR03570 199 VPA 201
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 74-163 3.78e-19

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: 77.29  E-value: 3.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  74 IFLGNAFYANFDCVMLDvcPIHIGDNCMLAPGVHIYTATHPldaearnsgqEYGKPVTIGHNVWIGGRAVINPGVTIGDN 153
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                         90
                 ....*....|
gi 496080928 154 AVIASGAVVT 163
Cdd:cd00208   69 AVIGAGAVVT 78
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 95-176 1.05e-17

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: 74.40  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaeARNSGQEYGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGG 174
Cdd:cd03354   30 VIGDNCTIYQGVTL----------GGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVG 99


                 ..
gi 496080928 175 NP 176
Cdd:cd03354  100 VP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-182 2.44e-17

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: 75.91  E-value: 2.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnSGQeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGG 174
Cdd:cd03352  134 RIGENCLIAAQVGI-------------AGS-----TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195


                 ....*...
gi 496080928 175 NPAQIIKR 182
Cdd:cd03352  196 TPAQPHRE 203
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 94-181 3.82e-16

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 72.60  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  94 IHIGDNCMLAPGVHIYTATHPLDAEARNSGQEY---------GKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK 164
Cdd:PRK09677  86 ITIGRDTLIASKVFITDHNHGSFKHSDDFSSPNlppdmrtleSSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTK 165

                         90
                 ....*....|....*..
gi 496080928 165 DVPAGAVVGGNPAQIIK 181
Cdd:PRK09677 166 SIPENTVIAGNPAKIIK 182
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 90-183 3.46e-15

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: 68.98  E-value: 3.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  90 DVCPIHIG------DNCMLapgvHIyTATHPLdaearnsgqEYGKPVTIGH-----------NVWIGGRAVINPGVTIGD 152
Cdd:cd04645   35 DVNPIRIGertniqDGSVL----HV-DPGYPT---------IIGDNVTVGHgavlhgctigdNCLIGMGAIILDGAVIGK 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496080928 153 NAVIASGAVVT--KDVPAGAVVGGNPAQIIKRL 183
Cdd:cd04645  101 GSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 90-183 4.55e-15

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 69.29  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  90 DVCPIHIG------DNCMLapgvHIyTATHPLdaearnsgqEYGKPVTIGH-----------NVWIGGRAVINPGVTIGD 152
Cdd:COG0663   46 DVGPIRIGegsniqDGVVL----HV-DPGYPL---------TIGDDVTIGHgailhgctigdNVLIGMGAIVLDGAVIGD 111

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496080928 153 NAVIASGAVVT--KDVPAGAVVGGNPAQIIKRL 183
Cdd:COG0663  112 GSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-184 7.53e-15

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: 71.20  E-value: 7.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnSGQeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGG 174
Cdd:COG1044  242 RIGEHTAIAAQVGI-------------AGS-----TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG 303

                         90       100
                 ....*....|....*....|
gi 496080928 175 NPAQ----------IIKRLP 184
Cdd:COG1044  304 SPAQphrewlrnaaALRRLP 323
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-184 1.14e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.78  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnSGQeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPA-GAVVG 173
Cdd:PRK00892 245 VIGRHTAIAAQVGI-------------AGS-----TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSS 306

                         90       100
                 ....*....|....*....|.
gi 496080928 174 GNPAQ----------IIKRLP 184
Cdd:PRK00892 307 GIPAQpnkewlrtaaRLRRLD 327
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 92-184 1.02e-11

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: 59.92  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  92 CPIHIGDNCMLAPGVHIYTAThpldaearnsgqeygkpvtIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKD--VPAG 169
Cdd:cd03359   71 FPLHIGDYVFIGENCVVNAAQ-------------------IGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPY 131

                         90
                 ....*....|....*
gi 496080928 170 AVVGGNPAQIIKRLP 184
Cdd:cd03359  132 SVVSGRPARFIGELP 146
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 85-179 3.13e-10

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: 57.44  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  85 DCVmldvcpihIGDNCMLAPGVHIytATHpldaearnsgqeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK 164
Cdd:cd03351  120 DCV--------IGNNVILANNATL--AGH----------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQ 173

                         90
                 ....*....|....*
gi 496080928 165 DVPAGAVVGGNPAQI 179
Cdd:cd03351  174 DVPPYVIAAGNRARL 188
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-181 3.80e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 54.87  E-value: 3.80e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496080928 131 TIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 85-179 4.76e-09

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: 54.25  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  85 DCVmldvcpihIGDNCMLAPGVHIytATHpldaearnsgqeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK 164
Cdd:COG1043  122 DCV--------VGNNVILANNATL--AGH----------------VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVK 175

                         90
                 ....*....|....*
gi 496080928 165 DVPAGAVVGGNPAQI 179
Cdd:COG1043  176 DVPPYVLAAGNPARL 190
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 95-172 1.39e-08

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 51.23  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIYTATHPLDAearnsgqeygKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK---------- 164
Cdd:cd03350   51 QIGKNVHLSAGAVIGGVLEPLQA----------TPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretg 120

                         90
                 ....*....|...
gi 496080928 165 -----DVPAGAVV 172
Cdd:cd03350  121 eiyygRVPPGSVV 133
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 131-181 4.66e-08

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: 51.57  E-value: 4.66e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496080928 131 TIGHNVWIGGRAV-INPgVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:COG1207  396 VIGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPAGALAIARARQRNI 446
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 125-183 4.82e-08

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: 49.88  E-value: 4.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080928 125 EYGKPVTIGHN-----------VWIGGRAVINPGVTIGDNAVIASGAVVT--KDVPAGAVVGGNPAQIIKRL 183
Cdd:cd04650   63 EIGDYVTIGHNavvhgakvgnyVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 131-172 6.95e-08

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: 50.11  E-value: 6.95e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 496080928 131 TIGHNVWIG-GRAVINPgVTIGDNAVIASGAVVTKDVPAGAVV 172
Cdd:cd03353  146 VIGDNVFIGsNSQLVAP-VTIGDGATIAAGSTITKDVPPGALA 187
PLN02739 PLN02739
serine acetyltransferase
 96-188 8.39e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 50.80  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  96 IGDNCMLAPGVHIYTAThPLDAEARNSGQEYGKpvtIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGN 175
Cdd:PLN02739 228 IGETAVIGDRVSILHGV-TLGGTGKETGDRHPK---IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303

                         90
                 ....*....|...
gi 496080928 176 PAQIIKRLPLPNP 188
Cdd:PLN02739 304 PAKLIGFVDEQDP 316
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-174 1.04e-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: 49.71  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnsgqeyGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVP------- 167
Cdd:cd03352    3 KIGENVSIGPNAVI------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIigdrvii 64


                 ....*...
gi 496080928 168 -AGAVVGG 174
Cdd:cd03352   65 hSGAVIGS 72
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 68-177 1.48e-07

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: 50.52  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   68 CDYGYNIFLGNAFYANFDCVmldvcpiHIGDNCMLAPGVHIytATHPLDAEARNSGQeygkpVTIGHNVWIGGRAVINPG 147
Cdd:TIGR02353 598 VKIGRGVYIDGTDLTERDLV-------TIGDDSTLNEGSVI--QTHLFEDRVMKSDT-----VTIGDGATLGPGAIVLYG 663

                          90       100       110
                  ....*....|....*....|....*....|..
gi 496080928  148 VTIGDNAVIASGAVVTK--DVPAGAVVGGNPA 177
Cdd:TIGR02353 664 VVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
PLN02296 PLN02296
carbonate dehydratase
 86-183 2.21e-07

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 49.35  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  86 CVML-DVCPIHIG------DNCMlapgVHIytathpldAEARNSGQEY----GKPVTIGHNV-----------WIGGRAV 143
Cdd:PLN02296  83 CVLRgDVNSISVGsgtniqDNSL----VHV--------AKTNLSGKVLptiiGDNVTIGHSAvlhgctvedeaFVGMGAT 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496080928 144 INPGVTIGDNAVIASGAVVTKD--VPAGAVVGGNPAQIIKRL 183
Cdd:PLN02296 151 LLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-162 2.90e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 2.90e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080928  96 IGDNCMLAPGVHIytathpldaearnsgqeyGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVV 162
Cdd:PRK00892 133 IGDGVVIGAGAVI------------------GDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
PLN02357 PLN02357
serine acetyltransferase
 96-180 3.00e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 49.50  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  96 IGDNCMLAPGVhiytathPLDAEARNSGQEYGKpvtIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGN 175
Cdd:PLN02357 255 VGNNVSILHNV-------TLGGTGKQSGDRHPK---IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGN 324


                 ....*
gi 496080928 176 PAQII 180
Cdd:PLN02357 325 PARLI 329
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-174 3.45e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.86  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnsgqeyGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVP------- 167
Cdd:COG1044  110 KIGEGVSIGPFAVI------------------GAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVigdrvii 171


                 ....*...
gi 496080928 168 -AGAVVGG 174
Cdd:COG1044  172 hSGAVIGA 179
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
129-158 3.96e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 44.64  E-value: 3.96e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 496080928  129 PVTIGHNVWIGGRAVINPGVTIGDNAVIAS 158
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 96-183 5.93e-07

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 48.26  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  96 IGDNCMLAPGVHIYTATHPLDAearnsgqeygKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK-----D----- 165
Cdd:PRK11830 153 IGKNVHLSGGVGIGGVLEPLQA----------NPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiyDretge 222

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496080928 166 -----VPAGAVV-GGN-----------PAQIIKRL 183
Cdd:PRK11830 223 vhygrVPAGSVVvPGSlpskdggyslyCAVIVKKV 257
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-174 6.11e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.21  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  95 HIGDNCMLAPGVHIytathpldaearnsgqeyGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVP------- 167
Cdd:PRK00892 114 KIGEGVSIGPNAVI------------------GAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRignrvii 175


                 ....*...
gi 496080928 168 -AGAVVGG 174
Cdd:PRK00892 176 hSGAVIGS 183
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 130-166 7.14e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.09  E-value: 7.14e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496080928 130 VTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDV 166
Cdd:COG1044  109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
85-179 8.75e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.79  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  85 DCVmldvcpihIGDNCMLAPGVHIytATHpldaearnsgqeygkpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK 164
Cdd:PRK05289 123 DCV--------VGNHVILANNATL--AGH----------------VEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQ 176

                         90
                 ....*....|....*
gi 496080928 165 DVPAGAVVGGNPAQI 179
Cdd:PRK05289 177 DVPPYVLAEGNPARL 191
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
130-164 9.03e-07

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 43.58  E-value: 9.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 496080928  130 VTIGHNVWIGGRAVInpGVTIGDNAVIASGAVVTK 164
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-181 1.30e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.52  E-value: 1.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496080928 131 TIGHNVWIGGRA-VINPgVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK14354 395 IIGDNAFIGCNSnLVAP-VTVGDNAYIAAGSTITKDVPEDALAIARARQVNK 445
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-181 1.82e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 46.91  E-value: 1.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496080928 131 TIGHNVWIGGRA-VINPgVTIGDNAVIASGAVVTKDVPAGA-VVGGNPAQIIK 181
Cdd:PRK14359 369 IIGKNVFIGSDTqLVAP-VNIEDNVLIAAGSTVTKDVPKGSlAISRAPQKNIK 420
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 130-166 2.70e-06

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: 45.86  E-value: 2.70e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496080928 130 VTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDV 166
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 95-180 3.09e-06

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: 46.10  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   95 HIGDNCMLAPGVHI----YTATHPLDAearNSGQEYGKpVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGA 170
Cdd:TIGR01852 103 RIGNNNLLMAYSHIahdcVVGNHVILA---NNATLAGH-VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYC 178

                          90
                  ....*....|
gi 496080928  171 VVGGNPAQII 180
Cdd:TIGR01852 179 LAEGNRARLR 188
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 130-166 3.90e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.90  E-value: 3.90e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496080928 130 VTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDV 166
Cdd:PRK00892 113 AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 131-183 5.75e-06

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 44.28  E-value: 5.75e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496080928 131 TIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTK--DVPAGAVVGGNPAQIIKRL 183
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIREL 134
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-180 6.16e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 45.70  E-value: 6.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496080928 131 TIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGA-VVGGNPAQII 180
Cdd:PRK14352 401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGAlAVSEGPQRNI 451
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-171 6.19e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.49  E-value: 6.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAV 171
Cdd:PRK14356 401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-181 7.54e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 45.30  E-value: 7.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK14360 393 IGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
PLN02694 PLN02694
serine O-acetyltransferase
 115-180 9.07e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 45.02  E-value: 9.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080928 115 LDAEARNSGQEYGKpvtIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQII 180
Cdd:PLN02694 201 LGGTGKACGDRHPK---IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 93-184 9.58e-06

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 43.77  E-value: 9.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  93 PIHIGDNCMLAPGVHIytatHPLDAEARNSGQE---------YGkPVTIGHNVWIGGRAVINpGVTIGDNAVIASGAVVT 163
Cdd:cd00710   42 PIIIGANVNIQDGVVI----HALEGYSVWIGKNvsiahgaivHG-PAYIGDNCFIGFRSVVF-NAKVGDNCVIGHNAVVD 115

                         90       100
                 ....*....|....*....|....*...
gi 496080928 164 -------KDVPAGAVVGgnPAQIIKRLP 184
Cdd:cd00710  116 gveippgRYVPAGAVIT--SQTQADALP 141
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 94-178 1.28e-05

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: 44.74  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928   94 IHIGDNCMLAPGVHIytATHPLDAEARNSGqeygkPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKD--VPAGAV 171
Cdd:TIGR02353 132 LTIGAGTIVRKEVML--LGYRAERGRLHTG-----PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGER 204


                  ....*..
gi 496080928  172 VGGNPAQ 178
Cdd:TIGR02353 205 WHGSPAQ 211
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 129-181 1.28e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 44.75  E-value: 1.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496080928 129 PVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 127-162 2.20e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.47  E-value: 2.20e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496080928 127 GKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVV 162
Cdd:COG1043   29 GPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
96-162 2.67e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 2.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080928  96 IGDNCMLAPGVHIytathpldaearnsgqeyGKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVV 162
Cdd:PRK05289  17 IGENVEIGPFCVI------------------GPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-181 1.64e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.27  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQIIK 181
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNK 449
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
132-181 1.97e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.85  E-value: 1.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVT------KD--VPAGAVVGGNPaQIIK 181
Cdd:PRK05289  17 IGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDghttigKNnrIFPFASIGEDP-QDLK 73
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 94-179 1.97e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.78  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  94 IHIGDNCMLAPGVHIYTATHPLDAEARNSGQEYGKPVTIGHNVWIGGRAVINPG------VTIGDNAVI----------- 156
Cdd:PRK12461  78 LEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGallaghVTVGDRAIIsgnclvhqfcr 157

                         90       100       110
                 ....*....|....*....|....*....|
gi 496080928 157 -------ASGAVVTKDVPAGAVVGGNPAQI 179
Cdd:PRK12461 158 igalammAGGSRISKDVPPYCMMAGHPTNV 187
PRK10191 PRK10191
putative acyl transferase; Provisional
 129-179 2.26e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 39.87  E-value: 2.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496080928 129 PVtIGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVVGGNPAQI 179
Cdd:PRK10191  93 PH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 127-162 2.55e-04

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 40.49  E-value: 2.55e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496080928 127 GKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVV 162
Cdd:cd03351   27 GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-172 5.94e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 39.62  E-value: 5.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKDVPAGAVV 172
Cdd:PRK09451 397 IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 96-166 8.82e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.84  E-value: 8.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080928  96 IGDNCMLAPGVHIytaTHPLDAEArnsgqeygkpVTIGHNVWIGGrAVINPGVTIGDNAVIASGAVVTKDV 166
Cdd:cd03356   19 IGDNVRIGDGVTI---TNSILMDN----------VTIGANSVIVD-SIIGDNAVIGENVRVVNLCIIGDDV 75
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 132-176 1.04e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 38.57  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVT------KD--VPAGAVVGGNP 176
Cdd:cd03351   14 IGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgpttigKNnrIFPFASIGEAP 66
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 125-173 1.07e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496080928 125 EYGKPVTIGHNVWIGgravinPGVTIGDNAVIAS-----GAVVTkdvpAGAVVG 173
Cdd:PRK14353 270 VIGRDVVIEPNVVFG------PGVTVASGAVIHAfshleGAHVG----EGAEVG 313
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 127-162 1.21e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.46  E-value: 1.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496080928 127 GKPVTIGHNVWIGGRAVINPGVTIGDNAVIASGAVV 162
Cdd:PRK12461  27 GANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 132-176 2.10e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 37.69  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496080928 132 IGHNVWIGGRAVINPGVTIGDNAVIASGAVVTKD--------VPAGAVVGGNP 176
Cdd:COG1043   16 LGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPttigknnrIFPFASIGEEP 68
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 93-162 2.51e-03

Dynactin 6 (or subunit p27): 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 p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the 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: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 36.92  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080928  93 PIHIGDNCMLAPGVHIytaTHPLDaearnSGQEYGKPVTIG-HNVW----------IGGRAVINPGVTIGDNAVIASGAV 161
Cdd:cd04646   38 PIIIGENNIIEEQVTI---VNKKP-----KDPAEPKPMIIGsNNVFevgckcealkIGNNNVFESKSFVGKNVIITDGCI 109


                 .
gi 496080928 162 V 162
Cdd:cd04646  110 I 110
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 131-171 4.47e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 36.88  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 496080928 131 TIGHNVWIGGRA-VINPGVtIGDNAVIASGAVVTKDVPAGAV 171
Cdd:PRK14358 401 KVGAGVFIGSNTtLIAPRV-VGDAAFIAAGSAVHDDVPEGAM 441
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 138-175 4.71e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 4.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 496080928 138 IGGRAVINPGVTIGDNAVIASGAVVTKDVP--AGAVVGGN 175
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVigAGAVIGDG 148
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 127-175 7.08e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.09  E-value: 7.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496080928 127 GKPVTIGHNVWIGGrAVINPGVTIGDNAVI-----ASGAVVTKD--VPAGAVVGGN 175
Cdd:cd05787   20 GRNCKIGKNVVIDN-SYIWDDVTIEDGCTIhhsivADGAVIGKGctIPPGSLISFG 74
 
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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