NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|511755534|ref|WP_016388981|]
View 

sugar O-acetyltransferase [Lacticaseibacillus paracasei]

Protein Classification

sugar O-acetyltransferase( domain architecture ID 10129706)

sugar O-acetyltransferase similar to maltose O-acetyltransferase and galactoside O-acetyltransferase, which catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016407
PubMed:  11747907

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 15-181 2.84e-90

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: 261.59  E-value: 2.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  15 PYDDMDPLLLAVRDEATAKTDALNN--EHDPAKRNALFRELVGQTGVKPFVNPNFHCEFGRNIRVGDHFYANYDCTILDG 92
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQtpPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  93 APVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVI 172
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 511755534 173 AAGNPCEVL 181
Cdd:cd03357  161 AAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 15-181 2.84e-90

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: 261.59  E-value: 2.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  15 PYDDMDPLLLAVRDEATAKTDALNN--EHDPAKRNALFRELVGQTGVKPFVNPNFHCEFGRNIRVGDHFYANYDCTILDG 92
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQtpPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  93 APVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVI 172
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 511755534 173 AAGNPCEVL 181
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
58-189 8.39e-51

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 160.42  E-value: 8.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  58 GVKPFVNPNFHCeFGRNIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERqlGGCIAKPIVVGDGC 137
Cdd:COG0110   12 GDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDV 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511755534 138 WLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLREITAADK 189
Cdd:COG0110   89 WIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-189 4.05e-45

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 148.23  E-value: 4.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   1 MNLEEKfafMATGKPYDDMDPLLLAVRDEATAKTDALNNEH--DPAKRNALFRELVGQTGVKPFVNPNFHCEFGRNIRVG 78
Cdd:PRK09527   3 MSMTER---IKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHpsEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  79 DHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIG 158
Cdd:PRK09527  80 RNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIG 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511755534 159 AGSVVTHDIPARVIAAGNPCEVLREITAADK 189
Cdd:PRK09527 160 AGSVVTKDIPPNVVAAGVPCRVIREINDRDK 190
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 74-177 4.92e-20

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 83.31  E-value: 4.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   74 NIRVGDHFYANYDCTIldGAPVTIGDHVLFGPKVGLytsnhlfdllerqLGGCiakpiVVGDGCWLAANVTVLPGVTIGA 153
Cdd:TIGR03570 117 DVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL-------------SGGV-----VIGEGVFIGAGATIIQGVTIGA 176

                          90       100
                  ....*....|....*....|....
gi 511755534  154 GTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 10-58 7.34e-10

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


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 52.49  E-value: 7.34e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 511755534   10 MATGKPYDDMDPLLLAVRDEATAKTDALNN--EHDPAKRNALFRELVGQTG 58
Cdd:pfam12464   2 MLAGELYDASDPELVAERLRARRLLRRYNNtpPEDAEEREELLKELFGSVG 52
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 15-181 2.84e-90

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: 261.59  E-value: 2.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  15 PYDDMDPLLLAVRDEATAKTDALNN--EHDPAKRNALFRELVGQTGVKPFVNPNFHCEFGRNIRVGDHFYANYDCTILDG 92
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQtpPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  93 APVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVI 172
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 511755534 173 AAGNPCEVL 181
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
58-189 8.39e-51

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 160.42  E-value: 8.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  58 GVKPFVNPNFHCeFGRNIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERqlGGCIAKPIVVGDGC 137
Cdd:COG0110   12 GDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDV 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511755534 138 WLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLREITAADK 189
Cdd:COG0110   89 WIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-189 4.05e-45

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 148.23  E-value: 4.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   1 MNLEEKfafMATGKPYDDMDPLLLAVRDEATAKTDALNNEH--DPAKRNALFRELVGQTGVKPFVNPNFHCEFGRNIRVG 78
Cdd:PRK09527   3 MSMTER---IKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHpsEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  79 DHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIG 158
Cdd:PRK09527  80 RNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIG 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511755534 159 AGSVVTHDIPARVIAAGNPCEVLREITAADK 189
Cdd:PRK09527 160 AGSVVTKDIPPNVVAAGVPCRVIREINDRDK 190
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 10-184 5.49e-45

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 147.27  E-value: 5.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  10 MATGKPYDDMDPLLLAVRDEATAKTDALNNE--HDPAKRNALFRELVGQTGvKPFVNPNFHCEFGRNIRVGDHFYANYDC 87
Cdd:PRK10092   8 MIAGELYRSADETLSRDRLRARQLIHRYNHSlpDEHTLRQQILADLFGQVT-EAYIEPTFRCDYGYNIFLGNNFYANFDC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  88 TILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDI 167
Cdd:PRK10092  87 VMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDV 166

                        170
                 ....*....|....*..
gi 511755534 168 PARVIAAGNPCEVLREI 184
Cdd:PRK10092 167 PDNVVVGGNPARIIKKL 183
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 74-181 7.82e-45

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: 144.14  E-value: 7.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  74 NIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLER-QLGGCIAKPIVVGDGCWLAANVTVLPGVTIG 152
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERpIEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 511755534 153 AGTIIGAGSVVTHDIPARVIAAGNPCEVL 181
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10502 PRK10502
putative acyl transferase; Provisional
 74-183 3.18e-31

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 111.96  E-value: 3.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  74 NIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNH-----LFDLlerqlggcIAKPIVVGDGCWLAANVTVLPG 148
Cdd:PRK10502  71 KLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHdysdpHFDL--------NTAPIVIGEGCWLAADVFVAPG 142

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 511755534 149 VTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLRE 183
Cdd:PRK10502 143 VTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 73-181 1.25e-30

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: 108.08  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  73 RNIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVGLYTSNHLFDLLERQLggcIAKPIVVGDGCWLAANVTVLPGVTIG 152
Cdd:cd05825    2 WNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPL---ITAPIVIGDGAWVAAEAFVGPGVTIG 78

                         90       100
                 ....*....|....*....|....*....
gi 511755534 153 AGTIIGAGSVVTHDIPARVIAAGNPCEVL 181
Cdd:cd05825   79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 74-182 2.27e-26

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: 98.39  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  74 NIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKV--GL-------YTSNHLFDLLERQLGGCIA-------KPIVVGDGC 137
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVkiGLggnhptdWVSTYPFYIFGGEWEDDAKfddwpskGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 511755534 138 WLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLR 182
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 74-177 1.61e-22

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: 89.85  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  74 NIRVGDHFYANYDCTIldGAPVTIGDHVLFGPKVGLytsnhlfdllerqLGGCiakpiVVGDGCWLAANVTVLPGVTIGA 153
Cdd:cd03360  114 DARIGDNVIINTGAVI--GHDCVIGDFVHIAPGVVL-------------SGGV-----TIGEGAFIGAGATIIQGVTIGA 173

                         90       100
                 ....*....|....*....|....
gi 511755534 154 GTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:cd03360  174 GAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 72-182 4.08e-21

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: 84.09  E-value: 4.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  72 GRNIRVGDHFYANYDCTILDG----------APVTIGDHVLFGPKVglYTSNHLFDLLERQLGGCIaKPIVVGDGCWLAA 141
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNvkiqsnvsiyEGVTIEDDVFIGPNV--VFTNDLYPRSKIYRKWEL-KGTTVKRGASIGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 511755534 142 NVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLR 182
Cdd:cd03358   79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 70-182 1.78e-20

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 84.54  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  70 EFGRNIRVGDHFYanydctILDGAPVTIGDHVLFGPKVGLYTSNH-LFDLLERQLGGCI--------AKPIVVGDGCWLA 140
Cdd:PRK09677  67 FFGDNVQVNDYVH------IACIESITIGRDTLIASKVFITDHNHgSFKHSDDFSSPNLppdmrtleSSAVVIGQRVWIG 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 511755534 141 ANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLR 182
Cdd:PRK09677 141 ENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 74-177 4.92e-20

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 83.31  E-value: 4.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   74 NIRVGDHFYANYDCTIldGAPVTIGDHVLFGPKVGLytsnhlfdllerqLGGCiakpiVVGDGCWLAANVTVLPGVTIGA 153
Cdd:TIGR03570 117 DVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL-------------SGGV-----VIGEGVFIGAGATIIQGVTIGA 176

                          90       100
                  ....*....|....*....|....
gi 511755534  154 GTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVVGVP 200
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 75-195 1.46e-17

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 75.83  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  75 IRVGDhfYAN-YDCTIL---DGAPVTIGDHVLFGPKVGLytsnHlfdllerqlgGCiakpiVVGDGCWLAANVTVLPGVT 150
Cdd:COG0663   50 IRIGE--GSNiQDGVVLhvdPGYPLTIGDDVTIGHGAIL----H----------GC-----TIGDNVLIGMGAIVLDGAV 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 511755534 151 IGAGTIIGAGSVVTHD--IPARVIAAGNPCEVLREITAADKTGFAGH 195
Cdd:COG0663  109 IGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEEEIAFLRES 155
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 75-189 4.37e-16

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: 71.67  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  75 IRVGDHFyaNY-DCTIL---DGAPVTIGDHVLFGPKVglytsnhlfdllerQLGGCiakpiVVGDGCWLAANVTVLPGVT 150
Cdd:cd04645   39 IRIGERT--NIqDGSVLhvdPGYPTIIGDNVTVGHGA--------------VLHGC-----TIGDNCLIGMGAIILDGAV 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 511755534 151 IGAGTIIGAGSVVTHD--IPARVIAAGNPCEVLREITAADK 189
Cdd:cd04645   98 IGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDEEI 138
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 67-177 7.56e-14

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: 64.38  E-value: 7.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  67 FHCEFGRNIRVGDHFYANYDCTILDGAPVTIGDHVLFGPKVglytsnhlfdLLERQLGGCIAKPIVVGDGCWLAANVTVL 146
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGV----------TLGGKGKGGGKRHPTIGDNVVIGAGAKIL 70

                         90       100       110
                 ....*....|....*....|....*....|.
gi 511755534 147 PGVTIGAGTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:cd03354   71 GNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 132-183 6.16e-13

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: 63.95  E-value: 6.16e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLRE 183
Cdd:COG1045  119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 75-164 7.64e-13

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: 61.11  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  75 IRVGDHFYANYDCTILDgaPVTIGDHVLFGPKVGLYTsnhlfdllerQLGGCIAKPIVVGDGCWLAANVTVLPGVTIGAG 154
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGA----------ATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                         90
                 ....*....|
gi 511755534 155 TIIGAGSVVT 164
Cdd:cd00208   69 AVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-177 4.58e-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: 59.34  E-value: 4.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  95 VTIGDHVLFGPKVGlytsnhlfdllerqlggcIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAA 174
Cdd:cd03352  133 VRIGENCLIAAQVG------------------IAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVS 194


                 ...
gi 511755534 175 GNP 177
Cdd:cd03352  195 GTP 197
PLN02739 PLN02739
serine acetyltransferase
 133-196 6.61e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 60.43  E-value: 6.61e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511755534 133 VGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLREITAADKTGFAGHD 196
Cdd:PLN02739 260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYD 323
PLN02694 PLN02694
serine O-acetyltransferase
 133-181 2.25e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 58.50  E-value: 2.25e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 511755534 133 VGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVL 181
Cdd:PLN02694 215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 10-58 7.34e-10

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


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 52.49  E-value: 7.34e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 511755534   10 MATGKPYDDMDPLLLAVRDEATAKTDALNN--EHDPAKRNALFRELVGQTG 58
Cdd:pfam12464   2 MLAGELYDASDPELVAERLRARRLLRRYNNtpPEDAEEREELLKELFGSVG 52
PLN02357 PLN02357
serine acetyltransferase
 133-181 6.78e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.50  E-value: 6.78e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 511755534 133 VGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVL 181
Cdd:PLN02357 281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 76-180 2.31e-08

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: 52.33  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  76 RVGDhfyanyDCTILDGAPV----TIGDHVLFGPKVglytsnhlfdllerQLGGciakPIVVGDGCWLAANVTVLPGVTI 151
Cdd:COG1043  106 RIGD------DNLLMAYVHVahdcVVGNNVILANNA--------------TLAG----HVEVGDHAIIGGLSAVHQFVRI 161

                         90       100
                 ....*....|....*....|....*....
gi 511755534 152 GAGTIIGAGSVVTHDIPARVIAAGNPCEV 180
Cdd:COG1043  162 GAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 76-180 2.77e-08

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: 52.05  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  76 RVGDH--FYAN----YDCTIldgapvtiGDHVLFgpkvglytSNHLfdllerQLGGCIakpiVVGDGCWLAANVTVLPGV 149
Cdd:cd03351  104 RIGNNnlLMAYvhvaHDCVI--------GNNVIL--------ANNA------TLAGHV----EIGDYAIIGGLSAVHQFC 157

                         90       100       110
                 ....*....|....*....|....*....|.
gi 511755534 150 TIGAGTIIGAGSVVTHDIPARVIAAGNPCEV 180
Cdd:cd03351  158 RIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 49-177 4.33e-08

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 52.45  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   49 LFRELVGqTGVKPFVNPNFHCEFGRNIRVGDHFYANYDCtildgapVTIGDHVLFGPKVGLYTsnHLFDllERQLGgciA 128
Cdd:TIGR02353 579 FLRPFRG-TPFLPAILRLLGVKIGRGVYIDGTDLTERDL-------VTIGDDSTLNEGSVIQT--HLFE--DRVMK---S 643

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 511755534  129 KPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVT--HDIPARVIAAGNP 177
Cdd:TIGR02353 644 DTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMkgEEVPAHTRWRGNP 694
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 132-172 1.10e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 50.79  E-value: 1.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD--IPARVI 172
Cdd:COG1044  128 VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERcvIGDRVI 170
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 92-163 4.47e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.17  E-value: 4.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511755534  92 GAPVTIGDHVLFGPkvglytsnhlfdllerqlGGCIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:cd03352   17 GEGVVIGDGVVIGP------------------GVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 47-163 7.87e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.09  E-value: 7.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  47 NALFRELVGQTGVKP--FVNPNfhCEFGRNIRVGDHfyanydCTIldGAPVTIGDHVLFGPkvglytsnhlfdllerqlg 124
Cdd:COG1044   87 QLFYPPPAPAPGIHPsaVIDPS--AKIGEGVSIGPF------AVI--GAGVVIGDGVVIGP------------------- 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 511755534 125 GC-IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:COG1044  138 GVvIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 132-169 1.28e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 46.64  E-value: 1.28e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPA 169
Cdd:cd03353  146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPP 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-172 1.61e-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: 46.63  E-value: 1.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 511755534 126 CIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD--IPARVI 172
Cdd:cd03352   15 VIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGciIGDRVI 63
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 133-185 2.74e-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: 2.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 511755534 133 VGDGCWLAANVTVLPGVTIGAGTIIGAGSVVT--HDIPARVIAAGNPCEVLREIT 185
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKagTVIPPRSLIAGSPAKVIRELS 135
PRK10191 PRK10191
putative acyl transferase; Provisional
 69-180 3.71e-06

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 44.88  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  69 CEFGRNIR----VGDHFyanydcTILDGAPVTIGDHVLFGPKvglYTSNHLFDLLERQlGGCIAKPiVVGDGCWLAANVT 144
Cdd:PRK10191  38 CFFGYEIQaaatIGRRF------TIHHGYAVVINKNVVAGDD---FTIRHGVTIGNRG-ADNMACP-HIGNGVELGANVI 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511755534 145 VLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEV 180
Cdd:PRK10191 107 ILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 130-191 3.73e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 46.29  E-value: 3.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511755534 130 PIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLREITAADKTG 191
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLKKRK 444
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 132-169 4.77e-06

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: 46.17  E-value: 4.77e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 511755534 132 VVGDGCWLAANVT-VLPgVTIGAGTIIGAGSVVTHDIPA 169
Cdd:COG1207  396 VIGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPA 433
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-173 5.34e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.87  E-value: 5.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIA 173
Cdd:PRK14356 400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLA 441
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 126-172 6.04e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.52  E-value: 6.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 511755534 126 CIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD--IPARVI 172
Cdd:PRK00892 126 VIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAvrIGNRVI 174
PLN02296 PLN02296
carbonate dehydratase
 93-190 7.98e-06

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 45.12  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  93 APVTIGDHVLFGPKVGLYtsnhlfdllerqlgGCiakpiVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD--IPAR 170
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLH--------------GC-----TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSG 178

                         90       100
                 ....*....|....*....|
gi 511755534 171 VIAAGNPCEVLREITAADKT 190
Cdd:PLN02296 179 EVWAGNPAKFLRKLTEEEIA 198
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-163 8.22e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 8.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511755534  86 DCTIldGAPVTIGDHVLFGPKVGLYTsnhlfdllerqlgGC-IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:PRK00892 118 GVSI--GPNAVIGAGVVIGDGVVIGA-------------GAvIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
130-159 8.92e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.17  E-value: 8.92e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 511755534  130 PIVVGDGCWLAANVTVLPGVTIGAGTIIGA 159
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-183 1.07e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.85  E-value: 1.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLRE 183
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 127-163 1.36e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 1.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI 145
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 132-177 2.25e-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: 43.85  E-value: 2.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
88-180 3.43e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  88 TILDGAPVTIGDHVLFgpkvglytsnhlfdllerqLGGC-IAKPIVVGDGCWLAANVT-----------VLPG------- 148
Cdd:PRK05289  99 TVQGGGVTRIGDNNLL-------------------MAYVhVAHDCVVGNHVILANNATlaghvevgdyaIIGGltavhqf 159

                         90       100       110
                 ....*....|....*....|....*....|..
gi 511755534 149 VTIGAGTIIGAGSVVTHDIPARVIAAGNPCEV 180
Cdd:PRK05289 160 VRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 74-185 3.86e-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: 42.17  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  74 NIRVGDHFYANYDCTILD--GAPVTIGDHVLFGPKVGLYtsnhlfdllerqlGGCIAKPIVVGDGCWLaanvtvLPGVTI 151
Cdd:cd04650   39 SIYIGKYSNVQENVSIHTdhGYPTEIGDYVTIGHNAVVH-------------GAKVGNYVIVGMGAIL------LNGAKI 99

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511755534 152 GAGTIIGAGSVVTH--DIPARVIAAGNPCEVLREIT 185
Cdd:cd04650  100 GDHVIIGAGAVVTPgkEIPDYSLVLGVPAKVVRKLT 135
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 122-168 5.09e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 41.60  E-value: 5.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 511755534 122 QLGGCI----AKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIP 168
Cdd:cd03350   63 VIGGVLeplqATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-173 7.02e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.51  E-value: 7.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIA 173
Cdd:PRK14354 395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-169 1.30e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  86 DCTILD-----GAPVTIGDHVLFGPKVGlytsnhlfdllerqlggcIAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAG 160
Cdd:PRK00892 230 EGVKIDnlvqiAHNVVIGRHTAIAAQVG------------------IAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAM 291


                 ....*....
gi 511755534 161 SVVTHDIPA 169
Cdd:PRK00892 292 SGVTKSIPE 300
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 127-163 1.49e-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: 41.16  E-value: 1.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:COG1043   28 IGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-183 1.51e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.65  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEVLRE 183
Cdd:PRK14355 399 VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKE 450
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 72-164 2.03e-04

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: 40.26  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  72 GRNIRVGdHFYANYDCTILDGAPVT----IGDHVLfGPKV----GLYTSNHLFDLLE--------------RQLGGciak 129
Cdd:cd05636   57 GDGCVVG-NSVEVKNSIIMDGTKVPhlnyVGDSVL-GENVnlgaGTITANLRFDDKPvkvrlkgervdtgrRKLGA---- 130

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 511755534 130 piVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVT 164
Cdd:cd05636  131 --IIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 73-178 2.05e-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: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  73 RNIRVGDHFYANYDCTI----------LDGAPVTIGDHVLFGP-------KVGLYTsnHLFDllerqlgGC-IAKPIVVG 134
Cdd:cd03359   41 ATVSIGRYCILSEGCVIrppfkkfskgVAFFPLHIGDYVFIGEncvvnaaQIGSYV--HIGK-------NCvIGRRCIIK 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 511755534 135 DGCWLAANvTVLPgvtigAGTIIGAGSVVThDIPARVIAAGNPC 178
Cdd:cd03359  112 DCVKILDG-TVVP-----PDTVIPPYSVVS-GRPARFIGELPEC 148
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 96-173 2.93e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.68  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534  96 TIGDHVLFGpkVGLYTSNhlFDllerqlgGCIAKPIVVGDGCWLAAN-VTVLPgVTIGAGTIIGAGSVVTHDIP--ARVI 172
Cdd:PRK14360 367 TLGEQVNIG--AGTITAN--YD-------GVKKHRTVIGDRSKTGANsVLVAP-ITLGEDVTVAAGSTITKDVPdnSLAI 434


                 .
gi 511755534 173 A 173
Cdd:PRK14360 435 A 435
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 132-166 5.26e-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: 39.31  E-value: 5.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 511755534 132 VVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD 166
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDG 37
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 127-166 5.63e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.62  E-value: 5.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD 166
Cdd:PRK12461  26 IGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE 65
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 127-163 8.07e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 8.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVI 139
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 127-166 1.04e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 38.57  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVTHD 166
Cdd:cd03351   26 IGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEA 65
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 128-164 1.11e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 38.56  E-value: 1.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 511755534 128 AKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVVT 164
Cdd:COG2171  168 AAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLT 204
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
127-163 1.29e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.54  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 511755534 127 IAKPIVVGDGCWLAANVTVLPGVTIGAGTIIGAGSVV 163
Cdd:PRK05289  29 IGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
cysE PRK11132
serine acetyltransferase; Provisional
 135-180 2.00e-03

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 38.14  E-value: 2.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 511755534 135 DGCWLAANVTVLPGVTIGAGTIIGAGSVVTHDIPARVIAAGNPCEV 180
Cdd:PRK11132 198 EGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 76-177 4.43e-03

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: 36.85  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511755534   76 RVGDHfyanydCTILDGAPV----TIGDHVLFgpkvglytSNHLfdllerQLGGciakPIVVGDGCWLAANVTVLPGVTI 151
Cdd:TIGR01852 103 RIGNN------NLLMAYSHIahdcVVGNHVIL--------ANNA------TLAG----HVEVGDYAIIGGLVAVHQFVRI 158

                          90       100
                  ....*....|....*....|....*.
gi 511755534  152 GAGTIIGAGSVVTHDIPARVIAAGNP 177
Cdd:TIGR01852 159 GRYAMIGGLSAVSKDVPPYCLAEGNR 184
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
131-164 4.67e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.57  E-value: 4.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 511755534  131 IVVGDGCWLAANVTVlpGVTIGAGTIIGAGSVVT 164
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVIT 32
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH