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Conserved domains on  [gi|15266476|gb|AAK91783|]
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streptogramin A acetyltransferase [Enterococcus faecium]

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 ...
 29-187 2.10e-67

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: 203.54  E-value: 2.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  29 NIEIGDYTYYDDPVNptdfekhvthhyEFLGDKLIIGKFCSIASGIEFIMnGANHVMKGISTYPFNILGGDWQQyTPELT 108
Cdd:cd03349   1 NISVGDYSYGSGPDC------------DVGGDKLSIGKFCSIAPGVKIGL-GGNHPTDWVSTYPFYIFGGEWED-DAKFD 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15266476 109 DLPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPEVIQALENLAWWNKD 187
Cdd:cd03349  67 DWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 29-187 2.10e-67

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: 203.54  E-value: 2.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  29 NIEIGDYTYYDDPVNptdfekhvthhyEFLGDKLIIGKFCSIASGIEFIMnGANHVMKGISTYPFNILGGDWQQyTPELT 108
Cdd:cd03349   1 NISVGDYSYGSGPDC------------DVGGDKLSIGKFCSIAPGVKIGL-GGNHPTDWVSTYPFYIFGGEWED-DAKFD 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15266476 109 DLPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPEVIQALENLAWWNKD 187
Cdd:cd03349  67 DWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 29-196 1.39e-37

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: 129.51  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476    29 NIEIGDYTYyddpvnptdFEKHVTHHYEflgdklIIGKFCSIASGIEfiMNGANHVMKGISTYPFNILG---GDWQQYTP 105
Cdd:TIGR03308  36 EVALGDYSY---------VMRDCDIIYT------TIGKFCSIAAMVR--INATNHPMERPTLHHFTYRAamyFDDASDDA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476   106 ELTDLPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPEVIQALENLAWWN 185
Cdd:TIGR03308  99 DFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPEIAARIEALAWWD 178

                         170
                  ....*....|.
gi 15266476   186 KDIEWITANVP 196
Cdd:TIGR03308 179 WDHETLREALP 189
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-173 6.19e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.35  E-value: 6.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  24 VIKSPNIEIGDYTYYDDPVNPTDfekhvthhyeflGDKLIIGKFCSIASGIefIMNGANHVMKGISTYPFnilggdwqqy 103
Cdd:COG0110  22 RIYGGNITIGDNVYIGPGVTIDD------------PGGITIGDNVLIGPGV--TILTGNHPIDDPATFPL---------- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476 104 tpeltdlpLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPE 173
Cdd:COG0110  78 --------RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 57-166 2.80e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 71.06  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476   57 FLGDKLIIGKFCSIASgIEFIMNGANhVMKGISTYPFNILGGDWQQYTPELT------DLPLKGDTVV-GNDVWFGQNVT 129
Cdd:PRK09677  67 FFGDNVQVNDYVHIAC-IESITIGRD-TLIASKVFITDHNHGSFKHSDDFSSpnlppdMRTLESSAVViGQRVWIGENVT 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15266476  130 VLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK09677 145 ILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
115-144 5.67e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.55  E-value: 5.67e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 15266476   115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGA 144
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 29-187 2.10e-67

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: 203.54  E-value: 2.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  29 NIEIGDYTYYDDPVNptdfekhvthhyEFLGDKLIIGKFCSIASGIEFIMnGANHVMKGISTYPFNILGGDWQQyTPELT 108
Cdd:cd03349   1 NISVGDYSYGSGPDC------------DVGGDKLSIGKFCSIAPGVKIGL-GGNHPTDWVSTYPFYIFGGEWED-DAKFD 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15266476 109 DLPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPEVIQALENLAWWNKD 187
Cdd:cd03349  67 DWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 29-196 1.39e-37

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: 129.51  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476    29 NIEIGDYTYyddpvnptdFEKHVTHHYEflgdklIIGKFCSIASGIEfiMNGANHVMKGISTYPFNILG---GDWQQYTP 105
Cdd:TIGR03308  36 EVALGDYSY---------VMRDCDIIYT------TIGKFCSIAAMVR--INATNHPMERPTLHHFTYRAamyFDDASDDA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476   106 ELTDLPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPEVIQALENLAWWN 185
Cdd:TIGR03308  99 DFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPEIAARIEALAWWD 178

                         170
                  ....*....|.
gi 15266476   186 KDIEWITANVP 196
Cdd:TIGR03308 179 WDHETLREALP 189
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-173 6.19e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.35  E-value: 6.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  24 VIKSPNIEIGDYTYYDDPVNPTDfekhvthhyeflGDKLIIGKFCSIASGIefIMNGANHVMKGISTYPFnilggdwqqy 103
Cdd:COG0110  22 RIYGGNITIGDNVYIGPGVTIDD------------PGGITIGDNVLIGPGV--TILTGNHPIDDPATFPL---------- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476 104 tpeltdlpLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPE 173
Cdd:COG0110  78 --------RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 29-166 6.21e-27

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: 99.07  E-value: 6.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  29 NIEIGDYTYYDDPVNPTDfekhvthhyeflGDKLIIGKFCSIASGIEFImnGANHVMKGISTYPFNIlggdwqqytpelt 108
Cdd:cd04647   1 NISIGDNVYIGPGCVISA------------GGGITIGDNVLIGPNVTIY--DHNHDIDDPERPIEQG------------- 53

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15266476 109 dlPLKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:cd04647  54 --VTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 117-162 3.93e-23

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: 90.94  E-value: 3.93e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNP 162
Cdd:cd03357 120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNP 165
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 117-169 5.15e-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: 72.42  E-value: 5.15e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPS 169
Cdd:COG1045 119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 61-162 1.16e-15

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: 69.94  E-value: 1.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  61 KLIIGKFCSIASGIEF-----IMNGANHVmkgISTYPFnILGG--DWQQYTPELTDLPLkgdtVVGNDVWFGQNVTVLPG 133
Cdd:cd05825   3 NLTIGDNSWIGEGVWIynlapVTIGSDAC---ISQGAY-LCTGshDYRSPAFPLITAPI----VIGDGAWVAAEAFVGPG 74

                        90       100
                ....*....|....*....|....*....
gi 15266476 134 VKIGDGAIIGANSVVTKDVAPYTIVGGNP 162
Cdd:cd05825  75 VTIGEGAVVGARSVVVRDLPAWTVYAGNP 103
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 57-166 2.80e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 71.06  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476   57 FLGDKLIIGKFCSIASgIEFIMNGANhVMKGISTYPFNILGGDWQQYTPELT------DLPLKGDTVV-GNDVWFGQNVT 129
Cdd:PRK09677  67 FFGDNVQVNDYVHIAC-IESITIGRD-TLIASKVFITDHNHGSFKHSDDFSSpnlppdMRTLESSAVViGQRVWIGENVT 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15266476  130 VLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK09677 145 ILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 117-162 8.52e-15

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: 67.47  E-value: 8.52e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNP 162
Cdd:cd03354  56 TIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 114-162 9.97e-15

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: 69.44  E-value: 9.97e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15266476 114 GDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNP 162
Cdd:cd03360 149 GGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 116-167 1.24e-14

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: 67.53  E-value: 1.24e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15266476 116 TVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIG 167
Cdd:cd03358  68 TTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10502 PRK10502
putative acyl transferase; Provisional
 117-173 2.88e-14

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 68.05  E-value: 2.88e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15266476  117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEPE 173
Cdd:PRK10502 126 VIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRVETE 182
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 112-162 1.08e-13

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 66.75  E-value: 1.08e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15266476   112 LKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNP 162
Cdd:TIGR03570 150 LSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 118-166 6.38e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 64.45  E-value: 6.38e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15266476  118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK10092 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 118-166 2.78e-12

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 63.10  E-value: 2.78e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15266476  118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK09527 134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 114-164 1.80e-11

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: 60.88  E-value: 1.80e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15266476 114 GDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQ 164
Cdd:cd03352 149 GSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 112-178 2.99e-11

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: 60.91  E-value: 2.99e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15266476 112 LKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPS--------FEPEVIQAL 178
Cdd:cd03351 135 LAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNlvglkrrgFSREEIRAL 209
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 115-178 3.68e-11

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: 60.80  E-value: 3.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476 115 DTVVGNDVWFGQNVT-----------VLPG-------VKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGP-------- 168
Cdd:COG1043 122 DCVVGNNVILANNATlaghvevgdhaIIGGlsavhqfVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLnlvglkrr 201

                        90
                ....*....|
gi 15266476 169 SFEPEVIQAL 178
Cdd:COG1043 202 GFSREQIRAL 211
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
115-180 1.90e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 55.87  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  115 DTVVGNDVWFGQNVT-----------VLPG-------VKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPS------- 169
Cdd:PRK05289 123 DCVVGNHVILANNATlaghvevgdyaIIGGltavhqfVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNlvglkrr 202

                         90
                 ....*....|..
gi 15266476  170 -FEPEVIQALEN 180
Cdd:PRK05289 203 gFSREEIHALRR 214
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 58-180 2.03e-09

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: 55.73  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476    58 LGDKLIIGKFCSIASGIEfIMNG---ANHV-MKGIST-------YPFNILGGDWQ--QYTPELTDLPL------------ 112
Cdd:TIGR01852  13 IGENVEIGPFCIVGPGVK-IGDGvelKSHVvILGHTTigegtriFPGAVIGGVPQdlKYKGEKTRLIIgdnntirefvti 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476   113 -------KGDTVVGNDVWF------------GQNVTV-----LPG-VKIGDGAIIGAN------------------SVVT 149
Cdd:TIGR01852  92 nrgtasgGGVTRIGNNNLLmayshiahdcvvGNHVILannatLAGhVEVGDYAIIGGLvavhqfvrigryamigglSAVS 171

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 15266476   150 KDVAPYTIVGGNPIQLIG--------PSFEPEVIQALEN 180
Cdd:TIGR01852 172 KDVPPYCLAEGNRARLRGlnivglrrRGFSREEITAIKR 210
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 118-182 3.95e-09

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: 53.57  E-value: 3.95e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15266476 118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVT--KDVAPYTIVGGNPIQLIGPsFEPEVIQALENLA 182
Cdd:cd04645  80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE-LTDEEIAELRESA 145
PLN02357 PLN02357
serine acetyltransferase
 118-172 5.27e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.89  E-value: 5.27e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15266476  118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEP 172
Cdd:PLN02357 281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKENP 335
PLN02694 PLN02694
serine O-acetyltransferase
 118-172 6.12e-09

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 54.65  E-value: 6.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15266476  118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIGPSFEP 172
Cdd:PLN02694 215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKP 269
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 118-168 8.04e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 52.72  E-value: 8.04e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15266476 118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVT--KDVAPYTIVGGNPIQLIGP 168
Cdd:COG0663  91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRE 143
PLN02739 PLN02739
serine acetyltransferase
 118-167 4.30e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 52.35  E-value: 4.30e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15266476  118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLIG 167
Cdd:PLN02739 260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 116-154 3.05e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.03  E-value: 3.05e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15266476 116 TVVGNDVWFGQNVT-VLPgVKIGDGAIIGANSVVTKDVAP 154
Cdd:COG1207 395 TVIGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPA 433
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 113-149 4.55e-07

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: 46.09  E-value: 4.55e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15266476 113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVT 149
Cdd:cd00208  42 KNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 113-154 5.06e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.19  E-value: 5.06e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15266476 113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAP 154
Cdd:cd03353 142 KHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPP 183
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-154 8.14e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 48.70  E-value: 8.14e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15266476  113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAP 154
Cdd:PRK14353 378 KHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPD 419
cysE PRK11132
serine acetyltransferase; Provisional
 114-171 1.50e-06

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 47.38  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476  114 GDT-VVGNDVWFGQNVT--------------------------VLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK11132 165 GETaVIENDVSILQSVTlggtgktsgdrhpkiregvmigagakILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244

                         90
                 ....*....|.
gi 15266476  167 G------PSFE 171
Cdd:PRK11132 245 GkpesdkPSMD 255
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 114-164 2.49e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.93  E-value: 2.49e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15266476 114 GDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQ 164
Cdd:COG1044 257 GSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-153 2.59e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 47.33  E-value: 2.59e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15266476  113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVA 153
Cdd:PRK09451 392 KFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVA 432
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-152 4.38e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.64  E-value: 4.38e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15266476  113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:PRK14356 396 KHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDV 435
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
115-144 5.67e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.55  E-value: 5.67e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 15266476   115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGA 144
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-166 8.33e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.52  E-value: 8.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15266476  113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNPIQLI 166
Cdd:PRK14357 381 KNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 112-180 8.52e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 8.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15266476  112 LKGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGGNP-----IQLIG---PSFEPEVIQALEN 180
Cdd:PRK12461 134 LAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPtnvhgLNAVGlrrRGFSSRAIRALKR 210
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-157 1.85e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.44  E-value: 1.85e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15266476  116 TVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTI 157
Cdd:PRK14354 394 TIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 118-180 2.75e-05

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: 42.94  E-value: 2.75e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15266476 118 VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVT--KDVAPYTIVGGNPIQLIGPSFEPEVIQALEN 180
Cdd:cd04650  81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKN 145
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 114-164 4.48e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.20  E-value: 4.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15266476  114 GDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV-APYTIVGGNPIQ 164
Cdd:PRK00892 260 GSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQ 311
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 115-152 7.44e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.70  E-value: 7.44e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15266476 115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:COG1044 108 SAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-154 1.48e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 1.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15266476  113 KGDTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAP 154
Cdd:PRK14355 395 KHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPP 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 112-163 1.78e-04

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: 41.66  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15266476   112 LKGDTV-VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTK--DVAPYTIVGGNPI 163
Cdd:TIGR02353 641 MKSDTVtIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 102-176 1.95e-04

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: 40.28  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15266476 102 QYTPELTDLPLK-GDTV------------VGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKD--VAPYTIVGGNPIQLI 166
Cdd:cd03359  63 KFSKGVAFFPLHiGDYVfigencvvnaaqIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFI 142

                        90
                ....*....|
gi 15266476 167 GPsfEPEVIQ 176
Cdd:cd03359 143 GE--LPECTQ 150
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 115-155 1.97e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.39  E-value: 1.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15266476  115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANS-----VVTKD--VAPY 155
Cdd:PRK14353 268 DTVIGRDVVIEPNVVFGPGVTVASGAVIHAFShlegaHVGEGaeVGPY 315
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-154 2.33e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 2.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15266476  113 KGDTVVGNDVWFGQ-NVTVLPgVKIGDGAIIGANSVVTKDVAP 154
Cdd:PRK14352 397 KHRTTIGSHVRTGSdTMFVAP-VTVGDGAYTGAGTVIREDVPP 438
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 115-152 2.87e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 2.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15266476  115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-159 4.18e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 40.39  E-value: 4.18e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15266476 116 TVVGNDVWFGQNVTVLPGVKIGDGAIIGANSV----VTkdVAPYTIVG 159
Cdd:COG1044 121 AVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVlhpnVT--IYERCVIG 166
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 115-148 4.61e-04

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: 39.70  E-value: 4.61e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 15266476 115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVV 148
Cdd:cd03352  37 GVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 117-152 9.17e-04

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: 38.93  E-value: 9.17e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:cd03352   3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
PRK10191 PRK10191
putative acyl transferase; Provisional
 117-160 1.04e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 37.95  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15266476  117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDVAPYTIVGG 160
Cdd:PRK10191  94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVG 137
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 112-159 1.38e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.17  E-value: 1.38e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15266476 112 LKGDTVVGNDVWFGQNvTVLPGVKIGDGAIIGANSVVT-KDVAPYTIVG 159
Cdd:cd03353  30 LEGKTVIGEDCVIGPN-CVIKDSTIGDGVVIKASSVIEgAVIGNGATVG 77
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 115-148 1.67e-03

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: 38.46  E-value: 1.67e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 15266476 115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVV 148
Cdd:COG1044 144 GVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
116-150 1.69e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.72  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15266476   116 TVVGNDVWFGQNVTVlpGVKIGDGAIIGANSVVTK 150
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 117-161 1.90e-03

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: 38.46  E-value: 1.90e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVvtkdVAPYTIVGGN 161
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVV----IGPGVVIGDG 144
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 115-152 2.77e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.39  E-value: 2.77e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15266476 115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:cd03352  19 GVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 117-148 3.68e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.43  E-value: 3.68e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15266476  117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVV 148
Cdd:PRK00892 126 VIGAGVVIGDGVVIGAGAVIGDGVKIGADCRL 157
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 117-148 4.63e-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: 36.62  E-value: 4.63e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVV 148
Cdd:cd03352  15 VIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 117-161 5.92e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 5.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15266476  117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVvtkdVAPYTIVGGN 161
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVV----IGAGAVIGDG 148
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 117-149 6.38e-03

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 36.03  E-value: 6.38e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 15266476 117 VVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVT 149
Cdd:cd05636 131 IIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 115-148 6.61e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 6.61e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15266476  115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVV 148
Cdd:PRK00892 148 GVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 116-149 8.83e-03

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: 36.54  E-value: 8.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15266476 116 TVVGNDVWFGQNVTVLPGV------KIGDGAIIGANSVVT 149
Cdd:COG1207 261 TYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLK 300
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 115-152 9.09e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.27  E-value: 9.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15266476  115 DTVVGNDVWFGQNVTVLPGVKIGDGAIIGANSVVTKDV 152
Cdd:PRK00892 130 GVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 112-159 9.49e-03

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: 36.54  E-value: 9.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15266476 112 LKGDTVVGNDVWFGQNvTVLPGVKIGDGAIIgANSVVTK-DVAPYTIVG 159
Cdd:COG1207 281 LEGKTVIGEGVVIGPN-CTLKDSTIGDGVVI-KYSVIEDaVVGAGATVG 327
 
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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