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Conserved domains on  [gi|489525709|ref|WP_003430469|]
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CatB-related O-acetyltransferase [Clostridioides difficile]

Protein Classification

CatB-related O-acetyltransferase( domain architecture ID 10129626)

CatB-related O-acetyltransferase may catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin A

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0046677|GO:0016746
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 29-190 3.87e-71

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: 212.79  E-value: 3.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  29 NIEVGDYTIYNDFYNDprdfeknnvlyhypINNDKLIIGKFCSIACNAKFLMTsGNHSMKSNSTYTFPIFYEEWKLDINH 108
Cdd:cd03349    1 NISVGDYSYGSGPDCD--------------VGGDKLSIGKFCSIAPGVKIGLG-GNHPTDWVSTYPFYIFGGEWEDDAKF 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709 109 itDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKLLEIKWWD 188
Cdd:cd03349   66 --DDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWD 143


                 ..
gi 489525709 189 WP 190
Cdd:cd03349  144 WP 145
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 29-190 3.87e-71

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: 212.79  E-value: 3.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  29 NIEVGDYTIYNDFYNDprdfeknnvlyhypINNDKLIIGKFCSIACNAKFLMTsGNHSMKSNSTYTFPIFYEEWKLDINH 108
Cdd:cd03349    1 NISVGDYSYGSGPDCD--------------VGGDKLSIGKFCSIAPGVKIGLG-GNHPTDWVSTYPFYIFGGEWEDDAKF 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709 109 itDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKLLEIKWWD 188
Cdd:cd03349   66 --DDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWD 143


                 ..
gi 489525709 189 WP 190
Cdd:cd03349  144 WP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 55-203 5.72e-40

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: 135.67  E-value: 5.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709   55 YHYPINNDKLI---IGKFCSIACNAKflMTSGNHSMKSNSTYTF---PIFYEEWKLDinhitDA----WDNKGNIIIGND 124
Cdd:TIGR03308  42 YSYVMRDCDIIyttIGKFCSIAAMVR--INATNHPMERPTLHHFtyrAAMYFDDASD-----DAdffaWRRAKRVTIGHD 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525709  125 VWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKLLEIKWWDWPYKKIQSNIKHIQS 203
Cdd:TIGR03308 115 VWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPEIAARIEALAWWDWDHETLREALPDFRD 193
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-177 4.23e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 118.43  E-value: 4.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  24 VITRENIEVGDYTIYNDfyndprdfekNNVLYhypiNNDKLIIGKFCSIACNAKFlmTSGNHsmksnstytfpifyeewk 103
Cdd:COG0110   22 RIYGGNITIGDNVYIGP----------GVTID----DPGGITIGDNVLIGPGVTI--LTGNH------------------ 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525709 104 lDINHITDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDT 177
Cdd:COG0110   68 -PIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 119-171 4.05e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 70.23  E-value: 4.05e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKK 171
Cdd:PRK10092 130 VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
118-146 6.56e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.86  E-value: 6.56e-05
                          10        20
                  ....*....|....*....|....*....
gi 489525709  118 NIIIGNDVWIGYDSIIMSGIHIGDGAIIG 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 29-190 3.87e-71

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: 212.79  E-value: 3.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  29 NIEVGDYTIYNDFYNDprdfeknnvlyhypINNDKLIIGKFCSIACNAKFLMTsGNHSMKSNSTYTFPIFYEEWKLDINH 108
Cdd:cd03349    1 NISVGDYSYGSGPDCD--------------VGGDKLSIGKFCSIAPGVKIGLG-GNHPTDWVSTYPFYIFGGEWEDDAKF 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709 109 itDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKLLEIKWWD 188
Cdd:cd03349   66 --DDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWD 143


                 ..
gi 489525709 189 WP 190
Cdd:cd03349  144 WP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 55-203 5.72e-40

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: 135.67  E-value: 5.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709   55 YHYPINNDKLI---IGKFCSIACNAKflMTSGNHSMKSNSTYTF---PIFYEEWKLDinhitDA----WDNKGNIIIGND 124
Cdd:TIGR03308  42 YSYVMRDCDIIyttIGKFCSIAAMVR--INATNHPMERPTLHHFtyrAAMYFDDASD-----DAdffaWRRAKRVTIGHD 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525709  125 VWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKLLEIKWWDWPYKKIQSNIKHIQS 203
Cdd:TIGR03308 115 VWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPEIAARIEALAWWDWDHETLREALPDFRD 193
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-177 4.23e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 118.43  E-value: 4.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  24 VITRENIEVGDYTIYNDfyndprdfekNNVLYhypiNNDKLIIGKFCSIACNAKFlmTSGNHsmksnstytfpifyeewk 103
Cdd:COG0110   22 RIYGGNITIGDNVYIGP----------GVTID----DPGGITIGDNVLIGPGVTI--LTGNH------------------ 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525709 104 lDINHITDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDT 177
Cdd:COG0110   68 -PIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 62-169 1.29e-26

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: 98.30  E-value: 1.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  62 DKLIIGKFCSIACNAKFlmTSGNHSMKsnstytfpifyeewklDINHITDAWDNKGNIIIGNDVWIGYDSIIMSGIHIGD 141
Cdd:cd04647   20 GGITIGDNVLIGPNVTI--YDHNHDID----------------DPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                         90       100
                 ....*....|....*....|....*...
gi 489525709 142 GAIIGTRAVVTNDVPPYSIVGGVPAKII 169
Cdd:cd04647   82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 119-169 4.79e-19

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: 80.16  E-value: 4.79e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKII 169
Cdd:cd03357  119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 60-169 5.67e-16

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: 70.33  E-value: 5.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709  60 NNDKLIIGKFCSIACNAkfLMTSGNHSMKSNstyTFPIfyeewkldinhitdawdNKGNIIIGNDVWIGYDSIIMSGIHI 139
Cdd:cd05825   20 NLAPVTIGSDACISQGA--YLCTGSHDYRSP---AFPL-----------------ITAPIVIGDGAWVAAEAFVGPGVTI 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 489525709 140 GDGAIIGTRAVVTNDVPPYSIVGGVPAKII 169
Cdd:cd05825   78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 120-172 9.39e-16

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: 71.65  E-value: 9.39e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKR 172
Cdd:COG1045  119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 119-171 4.05e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 70.23  E-value: 4.05e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKK 171
Cdd:PRK10092 130 VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
PRK10502 PRK10502
putative acyl transferase; Provisional
 119-173 5.24e-14

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 67.28  E-value: 5.24e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRF 173
Cdd:PRK10502 125 IVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRV 179
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 119-172 8.52e-13

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 64.13  E-value: 8.52e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKR 172
Cdd:PRK09677 131 VVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 119-176 8.72e-13

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 64.25  E-value: 8.72e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNND 176
Cdd:PRK09527 132 ITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRD 189
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 121-171 1.83e-12

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: 62.43  E-value: 1.83e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTND--VPPYSIVGGVPAKIIKK 171
Cdd:cd04645   80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRE 132
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 117-166 1.83e-12

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 63.28  E-value: 1.83e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489525709  117 GNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPA 166
Cdd:TIGR03570 152 GGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 119-170 1.97e-12

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 61.36  E-value: 1.97e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIK 170
Cdd:cd03358   68 TTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 113-165 2.48e-12

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: 60.53  E-value: 2.48e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 113 WDNKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVP 165
Cdd:cd03354   49 GGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 117-165 1.50e-11

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 60.96  E-value: 1.50e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489525709 117 GNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVP 165
Cdd:cd03360  149 GGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 121-170 1.72e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 60.04  E-value: 1.72e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTND--VPPYSIVGGVPAKIIK 170
Cdd:COG0663   91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVR 142
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 121-171 8.21e-10

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: 55.27  E-value: 8.21e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVT--NDVPPYSIVGGVPAKIIKK 171
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRK 133
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 121-167 1.61e-09

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 54.61  E-value: 1.61e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489525709  121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAK 167
Cdd:TIGR01172 116 IGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPAR 162
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 117-171 1.88e-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: 55.11  E-value: 1.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489525709 117 GNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKK 171
Cdd:cd03352  149 GSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 117-181 2.67e-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: 55.41  E-value: 2.67e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525709 117 GNIIIGNDVWIGYdsiiMSGIH----IGDGAIIGTRAVVTNDVPPYSIVGGVPAKI-------IKKR-FNNDTISKL 181
Cdd:COG1043  139 GHVEVGDHAIIGG----LSAVHqfvrIGAHAMVGGGSGVVKDVPPYVLAAGNPARLrglnlvgLKRRgFSREQIRAL 211
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 117-181 6.22e-09

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: 54.36  E-value: 6.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525709 117 GNIIIGNDVWIGYdsiiMSGIH----IGDGAIIGTRAVVTNDVPPYSIVGGVPAKI-------IKKR-FNNDTISKL 181
Cdd:cd03351  137 GHVEIGDYAIIGG----LSAVHqfcrIGRHAMVGGGSGVVQDVPPYVIAAGNRARLrglnlvgLKRRgFSREEIRAL 209
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
118-184 1.68e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 53.18  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525709 118 NIIIGND------VWIGYDSII--MSGIH----IGDGAIIGTRAVVTNDVPPYSIVGGVPAKI-------IKKR-FNNDT 177
Cdd:PRK05289 129 HVILANNatlaghVEVGDYAIIggLTAVHqfvrIGAHAMVGGMSGVSQDVPPYVLAEGNPARLrglnlvgLKRRgFSREE 208


                 ....*..
gi 489525709 178 ISKLLEI 184
Cdd:PRK05289 209 IHALRRA 215
cysE PRK11132
serine acetyltransferase; Provisional
 125-171 2.32e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 52.78  E-value: 2.32e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489525709 125 VWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKK 171
Cdd:PRK11132 200 VMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
PLN02357 PLN02357
serine acetyltransferase
 121-181 1.35e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 50.65  E-value: 1.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKKRFNNDTISKL 181
Cdd:PLN02357 281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKI 341
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 117-170 4.34e-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: 47.98  E-value: 4.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525709 117 GNIIIGNDVWIGYDSI-----IMSGIHIGDGAIIGTRA------------VVTND--VPPYSIVGGVPAKIIK 170
Cdd:cd03359   71 FPLHIGDYVFIGENCVvnaaqIGSYVHIGKNCVIGRRCiikdcvkildgtVVPPDtvIPPYSVVSGRPARFIG 143
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 115-161 1.56e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 46.64  E-value: 1.56e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489525709 115 NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIV 161
Cdd:cd03353  141 NKHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-157 1.78e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 47.55  E-value: 1.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489525709 109 ITDAWD--NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPP 157
Cdd:PRK14353 369 ITCNYDgfNKHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPD 419
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 120-170 1.86e-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: 45.82  E-value: 1.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTN--DVPPYSIVGGVPAKIIK 170
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR 132
PLN02694 PLN02694
serine O-acetyltransferase
 121-169 9.43e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 45.02  E-value: 9.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKII 169
Cdd:PLN02694 215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 121-167 9.70e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 45.01  E-value: 9.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAK 167
Cdd:COG1044  261 IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 120-161 1.61e-05

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 44.63  E-value: 1.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIV 161
Cdd:COG1207  396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALA 437
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-156 2.05e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.33  E-value: 2.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489525709 109 ITDAWD--NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVP 156
Cdd:PRK14356 387 ITCNYDgvNKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVP 436
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-155 2.25e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.25  E-value: 2.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489525709 109 ITDAWD--NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDV 155
Cdd:PRK09451 383 ITCNYDgaNKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDV 431
PLN02739 PLN02739
serine acetyltransferase
 121-170 3.37e-05

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 43.87  E-value: 3.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIK 170
Cdd:PLN02739 260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-171 4.56e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.21  E-value: 4.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489525709 116 KGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKIIKK 171
Cdd:PRK14357 381 KNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
118-146 6.56e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.86  E-value: 6.56e-05
                          10        20
                  ....*....|....*....|....*....
gi 489525709  118 NIIIGNDVWIGYDSIIMSGIHIGDGAIIG 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 119-166 1.58e-04

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: 40.44  E-value: 1.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVT---------------NDVPPYSIV-GGVPA 166
Cdd:cd03350   76 VIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTqstpiydretgeiyyGRVPPGSVVvAGSLP 139
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 115-160 2.45e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 2.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489525709 115 NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSI 160
Cdd:PRK14354 390 NKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 115-167 2.59e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.08  E-value: 2.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525709 115 NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPP----YS------IVGGVPAK 167
Cdd:PRK14352 396 NKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPgalaVSegpqrnIEGWVQRK 458
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-160 2.83e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.88  E-value: 2.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489525709 109 ITDAWD--NKGNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSI 160
Cdd:PRK14355 386 ITCNYDgvKKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSL 439
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 119-152 5.64e-04

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: 37.23  E-value: 5.64e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489525709 119 IIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVT 152
Cdd:cd00208   45 TIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 121-170 6.86e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 6.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489525709 121 IGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPY-SIVGGVPAKIIK 170
Cdd:PRK00892 264 IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQPNK 314
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 117-168 1.06e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489525709 117 GNIIIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKI 168
Cdd:PRK12461 136 GHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNV 187
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 120-155 1.62e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.16  E-value: 1.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDV 155
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
119-152 3.24e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 3.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489525709  119 IIIGNDVWIGYDSIImsGIHIGDGAIIGTRAVVT 152
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVIT 32
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 120-165 4.31e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 37.03  E-value: 4.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRavvtNDVPPYSIVGGVP 165
Cdd:cd03351   25 VIGPNVEIGDGTVIGSHVVIDGPTTIGKN----NRIFPFASIGEAP 66
PRK10191 PRK10191
putative acyl transferase; Provisional
 120-168 5.45e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 36.02  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489525709 120 IIGNDVWIGYDSIIMSGIHIGDGAIIGTRAVVTNDVPPYSIVGGVPAKI 168
Cdd:PRK10191  94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
 
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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