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Conserved domains on  [gi|2486546494|ref|WP_279187284|]
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MULTISPECIES: acyltransferase [Bacteroides]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
41-161 3.58e-25

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 96.48  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFSPETLKIdvtrpslvtihGGGTFLHTNFTILTHDYAtlnfLNKYKEFVPNSGRVVIGNNVWFGQNVTV 120
Cdd:COG0110    32 DNVYIGPGVTIDDPGGITI-----------GDNVLIGPGVTILTGNHP----IDDPATFPLRTGPVTIGDDVWIGAGATI 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTLDE 161
Cdd:COG0110    97 LPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
41-161 3.58e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 96.48  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFSPETLKIdvtrpslvtihGGGTFLHTNFTILTHDYAtlnfLNKYKEFVPNSGRVVIGNNVWFGQNVTV 120
Cdd:COG0110    32 DNVYIGPGVTIDDPGGITI-----------GDNVLIGPGVTILTGNHP----IDDPATFPLRTGPVTIGDDVWIGAGATI 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTLDE 161
Cdd:COG0110    97 LPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 41-156 4.69e-25

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: 95.22  E-value: 4.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFSPETLKIDvtrpSLVTIhGGGTFLHTNftilTHDYATLNFLNKYKefvPNSGRVVIGNNVWFGQNVTV 120
Cdd:cd04647     6 DNVYIGPGCVISAGGGITIG----DNVLI-GPNVTIYDH----NHDIDDPERPIEQG---VTSAPIVIGDDVWIGANVVI 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:cd04647    74 LPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 43-156 5.07e-18

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.15  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  43 VQIDDDVFLFSPETLKI--DVTRPSLVTI--HGGGTFLHTNftilthDYATLNFlnKYKEFVPNSGRVVIGNNVWFGQNV 118
Cdd:PRK09677   72 VQVNDYVHIACIESITIgrDTLIASKVFItdHNHGSFKHSD------DFSSPNL--PPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2486546494 119 TVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 67-152 8.60e-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: 65.21  E-value: 8.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  67 VTIhGGGTFLHTNfTILTHDyatlNFLNKYKEFVPN---SGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIP 143
Cdd:TIGR03570 118 VRI-GDNVIINTG-AIVEHD----CVIGDFVHIAPGvtlSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIP 191


                  ....*....
gi 2486546494 144 ANSVAAGCP 152
Cdd:TIGR03570 192 DGGVVVGVP 200
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
106-133 3.76e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 42.32  E-value: 3.76e-06
                          10        20
                  ....*....|....*....|....*...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIG 133
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
41-161 3.58e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 96.48  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFSPETLKIdvtrpslvtihGGGTFLHTNFTILTHDYAtlnfLNKYKEFVPNSGRVVIGNNVWFGQNVTV 120
Cdd:COG0110    32 DNVYIGPGVTIDDPGGITI-----------GDNVLIGPGVTILTGNHP----IDDPATFPLRTGPVTIGDDVWIGAGATI 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTLDE 161
Cdd:COG0110    97 LPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 41-156 4.69e-25

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: 95.22  E-value: 4.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFSPETLKIDvtrpSLVTIhGGGTFLHTNftilTHDYATLNFLNKYKefvPNSGRVVIGNNVWFGQNVTV 120
Cdd:cd04647     6 DNVYIGPGCVISAGGGITIG----DNVLI-GPNVTIYDH----NHDIDDPERPIEQG---VTSAPIVIGDDVWIGANVVI 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:cd04647    74 LPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 106-156 5.98e-22

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: 89.02  E-value: 5.98e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:cd03357   119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 43-156 5.07e-18

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.15  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  43 VQIDDDVFLFSPETLKI--DVTRPSLVTI--HGGGTFLHTNftilthDYATLNFlnKYKEFVPNSGRVVIGNNVWFGQNV 118
Cdd:PRK09677   72 VQVNDYVHIACIESITIgrDTLIASKVFItdHNHGSFKHSD------DFSSPNL--PPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2486546494 119 TVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 67-156 7.75e-17

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: 74.50  E-value: 7.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  67 VTIHGGGTflHTNFTILTHDYATLNFLNKYKEFV---PNSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIP 143
Cdd:cd03349    34 VKIGLGGN--HPTDWVSTYPFYIFGGEWEDDAKFddwPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVP 111

                          90
                  ....*....|...
gi 2486546494 144 ANSVAAGCPCKVI 156
Cdd:cd03349   112 PYAIVGGNPAKVI 124
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 67-156 5.68e-15

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 71.19  E-value: 5.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  67 VTIhGGGTFLHTNFTILTHDYATLNFLNKYKEFVpnSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANS 146
Cdd:PRK09527   96 VTI-GDNVLIAPNVTLSVTGHPVHHELRKNGEMY--SFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNV 172

                          90
                  ....*....|
gi 2486546494 147 VAAGCPCKVI 156
Cdd:PRK09527  173 VAAGVPCRVI 182
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 67-152 3.81e-13

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 65.97  E-value: 3.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  67 VTIhGGGTFLHTNfTILTHDyatlNFLNKYKEFVPN---SGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIP 143
Cdd:cd03360   115 ARI-GDNVIINTG-AVIGHD----CVIGDFVHIAPGvvlSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVP 188


                  ....*....
gi 2486546494 144 ANSVAAGCP 152
Cdd:cd03360   189 DGSVVVGNP 197
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 64-152 5.19e-13

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: 63.23  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  64 PSLVTIHGGGTFLH------TNFTILtHDyATLNflnkYKEFVPNSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSV 137
Cdd:cd03354    13 PGLFIDHGTGIVIGetavigDNCTIY-QG-VTLG----GKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAV 86

                          90
                  ....*....|....*
gi 2486546494 138 VMGKIPANSVAAGCP 152
Cdd:cd03354    87 VTKDVPANSTVVGVP 101
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 67-152 8.60e-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: 65.21  E-value: 8.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  67 VTIhGGGTFLHTNfTILTHDyatlNFLNKYKEFVPN---SGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIP 143
Cdd:TIGR03570 118 VRI-GDNVIINTG-AIVEHD----CVIGDFVHIAPGvtlSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIP 191


                  ....*....
gi 2486546494 144 ANSVAAGCP 152
Cdd:TIGR03570 192 DGGVVVGVP 200
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 84-156 6.63e-12

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: 60.31  E-value: 6.63e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486546494  84 THDYATLNFlnkykEFVpnSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:cd05825    42 SHDYRSPAF-----PLI--TAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 102-159 3.05e-11

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 60.60  E-value: 3.05e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486546494 102 NSGR-----VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTL 159
Cdd:PRK10092  121 NSGAelgkpVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 108-161 1.01e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 58.50  E-value: 1.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMG--KIPANSVAAGCPCKVICTLDE 161
Cdd:COG0663    91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPGSLVVGSPAKVVRELTE 146
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 108-161 1.38e-10

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: 57.81  E-value: 1.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMG--KIPANSVAAGCPCKVICTLDE 161
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPgkVIPPGSLVAGSPAKVVRELTD 135
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 107-156 1.18e-09

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: 55.86  E-value: 1.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2486546494 107 VIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:COG1045   119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIV 168
PRK10502 PRK10502
putative acyl transferase; Provisional
 85-156 5.16e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 54.19  E-value: 5.16e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486546494  85 HDYATlnflnkyKEFVPNSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:PRK10502  111 HDYSD-------PHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 108-161 6.36e-09

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: 53.34  E-value: 6.36e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVM-GK-IPANSVAAGCPCKVICTLDE 161
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpGKeIPDYSLVLGVPAKVVRKLTE 136
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 103-152 7.57e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 53.95  E-value: 7.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2486546494 103 SGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCP 152
Cdd:cd03352   148 AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 41-157 3.36e-07

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: 47.88  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  41 KGVQIDDDVFLFspetlkidvtrPSLVTihgggtflhtnftilTHDYATLNFLNKYKEFVPnsgrVVIGNNVWFGQNVTV 120
Cdd:cd03358    33 EGVTIEDDVFIG-----------PNVVF---------------TNDLYPRSKIYRKWELKG----TTVKRGASIGANATI 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2486546494 121 LRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVIC 157
Cdd:cd03358    83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10191 PRK10191
putative acyl transferase; Provisional
 107-155 5.54e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 47.96  E-value: 5.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2486546494 107 VIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKV 155
Cdd:PRK10191   94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 108-165 1.84e-06

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: 46.44  E-value: 1.84e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVV---MgKIPANSVAAGCPCKVICTLDEYFEK 165
Cdd:cd03359    92 IGSYVHIGKNCVIGRRCIIKDCVKILDGTVVppdT-VIPPYSVVSGRPARFIGELPECTQE 151
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
106-133 3.76e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 42.32  E-value: 3.76e-06
                          10        20
                  ....*....|....*....|....*...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIG 133
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 108-161 4.17e-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: 45.44  E-value: 4.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGK--IPANSVAAGCPCKVICTLDE 161
Cdd:cd04745    81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSD 136
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 106-138 5.64e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.86  E-value: 5.64e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVV 138
Cdd:cd03352    38 VVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 38-152 8.15e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 46.28  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  38 LREKGVQIDDDVFLFSpetlkIDVTRPSLVTIhGGGTFLHTNFTILTHdyatlnflnKYKEFVPNSGRVVIGNNVWFGQN 117
Cdd:TIGR02353 593 LRLLGVKIGRGVYIDG-----TDLTERDLVTI-GDDSTLNEGSVIQTH---------LFEDRVMKSDTVTIGDGATLGPG 657

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2486546494 118 VTVLRGSDIGDNCIIGYGSVVMG--KIPANSVAAGCP 152
Cdd:TIGR02353 658 AIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNP 694
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 106-139 1.15e-05

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: 42.24  E-value: 1.15e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVM 139
Cdd:cd00208    45 TIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 103-150 3.78e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.18  E-value: 3.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2486546494 103 SGRVVIGNNVWFGQNvTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAG 150
Cdd:cd03353    31 EGKTVIGEDCVIGPN-CVIKDSTIGDGVVIKASSVIEGAVIGNGATVG 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 40-151 4.99e-05

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: 42.78  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  40 EKGVQIDDDVFLFSPETLKIDVTRPSLVTIHGGgtflhtnfTILTHD---YATLNflNKYKEfVPNSGRVVIGNNVWFGQ 116
Cdd:cd03352    35 GDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSG--------AVIGSDgfgFAPDG--GGWVK-IPQLGGVIIGDDVEIGA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2486546494 117 NVTVLRGS------------D----IGDNCIIGYGSVvmgkIPANSVAAGC 151
Cdd:cd03352   104 NTTIDRGAlgdtvigdgtkiDnlvqIAHNVRIGENCL----IAAQVGIAGS 150
PLN02739 PLN02739
serine acetyltransferase
 108-161 6.06e-05

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 43.49  E-value: 6.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTLDE 161
Cdd:PLN02739  260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 106-138 8.06e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.08  E-value: 8.06e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVV 138
Cdd:COG1044   145 VVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 99-155 1.84e-04

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 39.10  E-value: 1.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2486546494  99 FVPNSgrvVIGNNVWFGQNVtVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKV 155
Cdd:cd05787    13 TIKNS---VIGRNCKIGKNV-VIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTI 65
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 33-155 2.20e-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: 42.05  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  33 MLIRTLREKGVQIDDDVFLFSpetLKIDVTrpSLVTIhGGGTFLHTNFTILTH----DYATLnflnkykefvpnsGRVVI 108
Cdd:TIGR02353 103 LYSLYLRALGAKIGKGVDIGS---LPPVCT--DLLTI-GAGTIVRKEVMLLGYraerGRLHT-------------GPVTL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2486546494 109 GNNVWFGQNVTVLRGSDIGDNCIIGYGSVV-MGK-IPANSVAAGCP-CKV 155
Cdd:TIGR02353 164 GRDAFIGTRSTLDIDTSIGDGAQLGHGSALqGGQsIPDGERWHGSPaQKT 213
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 100-151 2.55e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 2.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486546494 100 VPNSGRVVIGNNVWFGQNVTVLRGS--D--IGDNCI------IGYGsVVMGKipaNSVAAGC 151
Cdd:PRK00892  198 IPQLGRVIIGDDVEIGANTTIDRGAldDtvIGEGVKidnlvqIAHN-VVIGR---HTAIAAQ 255
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 106-138 3.08e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 3.08e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVV 138
Cdd:PRK00892  149 VKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 100-150 6.19e-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: 6.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486546494 100 VPNSGRVVIGNNVWFGQNVTVLRGS------------D----IGDNCIIGY-----------GSVVMGKipaNSVAAG 150
Cdd:COG1044   195 IPQLGRVVIGDDVEIGANTTIDRGAlgdtvigdgtkiDnlvqIAHNVRIGEhtaiaaqvgiaGSTKIGD---NVVIGG 269
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
106-138 6.60e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 36.26  E-value: 6.60e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2486546494 106 VVIGNNVWFGQNVTVlrGSDIGDNCIIGYGSVV 138
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
PLN02357 PLN02357
serine acetyltransferase
 108-156 7.28e-04

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 40.25  E-value: 7.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVI 156
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 106-143 8.48e-04

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: 39.62  E-value: 8.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVmGKIP 143
Cdd:COG1043    32 VEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI-GEEP 68
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 105-139 8.51e-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: 40.00  E-value: 8.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2486546494 105 RVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVM 139
Cdd:COG1044   126 GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY 160
PLN02694 PLN02694
serine O-acetyltransferase
 108-183 8.87e-04

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 39.63  E-value: 8.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486546494 108 IGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKVICTLDEyfEKRKKCCVEEAFDYARSIQE 183
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEK--PAKHEECPGESMDHTSFISE 288
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 104-156 9.58e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 38.76  E-value: 9.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2486546494 104 GRVVIGNNVWFGQNVTVLRgSDIGDNCIIGYGSVVMG-KIPANS-VAAGcpcKVI 156
Cdd:cd00710    81 GPAYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVVDGvEIPPGRyVPAG---AVI 131
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-139 2.08e-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: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2486546494 105 RVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVM 139
Cdd:cd03352    19 GVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIY 53
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 16-133 2.79e-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: 38.47  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486546494  16 RLLQKQVAiesikqnpkmliRTLREKGVQIDDdvflfsPETLKIDVTrpslVTIhGGGTFLHTNfTILThdyatlnflnk 95
Cdd:COG1207   238 RILQRRIA------------ERLMRAGVTIID------PATTYIDGD----VEI-GRDVVIDPN-VILE----------- 282

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2486546494  96 ykefvpnsGRVVIGNNVWFGQNV---------------TVLRGSDIGDNCIIG 133
Cdd:COG1207   283 --------GKTVIGEGVVIGPNCtlkdstigdgvvikySVIEDAVVGAGATVG 327
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-148 3.76e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.17  E-value: 3.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2486546494 102 NSGRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVA 148
Cdd:PRK14356  395 NKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLA 441
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
106-143 3.81e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.77  E-value: 3.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVmGKIP 143
Cdd:PRK05289   33 VVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI-GEDP 69
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 104-155 4.30e-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: 37.41  E-value: 4.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2486546494 104 GRVVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVMGKIPANSVAAGCPCKV 155
Cdd:cd03351   137 GHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 103-152 5.26e-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: 37.30  E-value: 5.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2486546494 103 SGRVVIGNNVWFGQNVTVlrgSD---IGDNCIIGYGSVVMGKIPANSVAAGCP 152
Cdd:COG1044   256 AGSTKIGDNVVIGGQVGI---AGhltIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 104-133 5.65e-03

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: 35.94  E-value: 5.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2486546494 104 GRVVIGNNVWFGQNVTVLRGSDIGDNCIIG 133
Cdd:cd03358    15 NDVKIGDNVKIQSNVSIYEGVTIEDDVFIG 44
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-150 5.71e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 5.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2486546494 103 SGRVVIGNNVWFGQNVTVlRGSDIGDNCIIGYGSVVMGKIPANSVAAG 150
Cdd:PRK14355  284 SGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLEDSVVGDDVAIG 330
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 106-143 6.86e-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: 6.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIGYGSVVmGKIP 143
Cdd:cd03351    30 VEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI-GEAP 66
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 106-147 9.04e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 9.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2486546494 106 VVIGNNVWFGQNVTVLRGSDIGDNCIIG-----YGSVVMGK---IPANSV 147
Cdd:PRK00892  131 VVIGDGVVIGAGAVIGDGVKIGADCRLHanvtiYHAVRIGNrviIHSGAV 180
 
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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