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Conserved domains on  [gi|751567988|ref|WP_041036886|]
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MULTISPECIES: maltose O-acetyltransferase [Serratia]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 3-185 2.28e-134

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.


The actual alignment was detected with superfamily member PRK10092:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 183  Bit Score: 372.99  E-value: 2.28e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   3 ISEEKRKMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGYQGGTIEPTFRCDYGYNIYLGKNF 82
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  83 YANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGA 162
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 751567988 163 VVTKDVPANCVVGGNPARIIKQL 185
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 3-185 2.28e-134

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 372.99  E-value: 2.28e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   3 ISEEKRKMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGYQGGTIEPTFRCDYGYNIYLGKNF 82
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  83 YANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGA 162
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 751567988 163 VVTKDVPANCVVGGNPARIIKQL 185
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 15-182 7.81e-103

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: 292.79  E-value: 7.81e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  15 LYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGYQGG-TIEPTFRCDYGYNIYLGKNFYANFDCVILDV 93
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENvYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  94 CEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCV 173
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 751567988 174 VGGNPARII 182
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
64-185 8.47e-56

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 172.75  E-value: 8.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  64 IEPTFRCdYGYNIYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRvgGAEFGKPVRIGDNVWIGGR 143
Cdd:COG0110   17 IGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWIGAG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751567988 144 AVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIKQL 185
Cdd:COG0110   94 ATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 78-179 1.15e-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: 84.47  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   78 LGKNFYANFDCVIldVCEVHIGDNCLLAPGVHIytathpldaetrvGGAefgkpVRIGDNVWIGGRAVINPGVTIGDNAV 157
Cdd:TIGR03570 120 IGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 751567988  158 VASGAVVTKDVPANCVVGGNPA 179
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 9-57 3.98e-19

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: 76.38  E-value: 3.98e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 751567988    9 KMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLG 57
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFG 49
 
Name Accession Description Interval E-value
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 3-185 2.28e-134

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 372.99  E-value: 2.28e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   3 ISEEKRKMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGYQGGTIEPTFRCDYGYNIYLGKNF 82
Cdd:PRK10092   1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  83 YANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGA 162
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 751567988 163 VVTKDVPANCVVGGNPARIIKQL 185
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 15-182 7.81e-103

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: 292.79  E-value: 7.81e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  15 LYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGYQGG-TIEPTFRCDYGYNIYLGKNFYANFDCVILDV 93
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENvYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  94 CEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCV 173
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 751567988 174 VGGNPARII 182
Cdd:cd03357  161 AAGNPARVI 169
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 7-185 2.11e-57

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 179.04  E-value: 2.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   7 KRKMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLGGY-QGGTIEPTFRCDYGYNIYLGKNFYAN 85
Cdd:PRK09527   6 TERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVgENAWVEPPVYFSYGSNIHIGRNFYAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  86 FDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:PRK09527  86 FNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVT 165

                        170       180
                 ....*....|....*....|
gi 751567988 166 KDVPANCVVGGNPARIIKQL 185
Cdd:PRK09527 166 KDIPPNVVAAGVPCRVIREI 185
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
64-185 8.47e-56

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 172.75  E-value: 8.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  64 IEPTFRCdYGYNIYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRvgGAEFGKPVRIGDNVWIGGR 143
Cdd:COG0110   17 IGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLRTGPVTIGDDVWIGAG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751567988 144 AVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIKQL 185
Cdd:COG0110   94 ATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 75-182 5.50e-48

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: 151.84  E-value: 5.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  75 NIYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHIYTATHPLDAETRVGGAEF-GKPVRIGDNVWIGGRAVINPGVTIG 153
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVtSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 751567988 154 DNAVVASGAVVTKDVPANCVVGGNPARII 182
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 75-184 7.69e-33

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: 114.56  E-value: 7.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  75 NIYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHI---------YTATHPLDAETRVGGAEFG-------KPVRIGDNV 138
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIglggnhptdWVSTYPFYIFGGEWEDDAKfddwpskGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751567988 139 WIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIKQ 184
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
PRK10502 PRK10502
putative acyl transferase; Provisional
 39-184 3.18e-27

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 101.18  E-value: 3.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  39 HSSPEEGELRKQWLGELLGGY--QGGTIEPTFRCDYGYNIYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHIYTATHP 116
Cdd:PRK10502  33 AWSPQPLYRWRAFLLRLFGAKigKGVVIRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751567988 117 LDAETrvggaeFG---KPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIKQ 184
Cdd:PRK10502 113 YSDPH------FDlntAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 87-182 5.50e-26

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: 95.75  E-value: 5.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  87 DCVILDVCEVHIGDNCLLAPGVHIYTATH-------PLDAetrvggaefgKPVRIGDNVWIGGRAVINPGVTIGDNAVVA 159
Cdd:cd05825   15 GVWIYNLAPVTIGSDACISQGAYLCTGSHdyrspafPLIT----------APIVIGDGAWVAAEAFVGPGVTIGEGAVVG 84

                         90       100
                 ....*....|....*....|...
gi 751567988 160 SGAVVTKDVPANCVVGGNPARII 182
Cdd:cd05825   85 ARSVVVRDLPAWTVYAGNPAVPV 107
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 73-183 1.50e-23

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 89.87  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  73 GYNIYLGKNFYANFDCVILDVCEVH----------IGDNCLLAPGVHIYTATHPLDAETRvgGAEFgKPVRIGDNVWIGG 142
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNVKIQsnvsiyegvtIEDDVFIGPNVVFTNDLYPRSKIYR--KWEL-KGTTVKRGASIGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751567988 143 RAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIK 183
Cdd:cd03358   79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 73-178 4.36e-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: 88.31  E-value: 4.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  73 GYNIYLGKNFYANFDCVIldVCEVHIGDNCLLAPGVHIytathpldaetrvGGAefgkpVRIGDNVWIGGRAVINPGVTI 152
Cdd:cd03360  112 NPDARIGDNVIINTGAVI--GHDCVIGDFVHIAPGVVL-------------SGG-----VTIGEGAFIGAGATIIQGVTI 171

                         90       100
                 ....*....|....*....|....*.
gi 751567988 153 GDNAVVASGAVVTKDVPANCVVGGNP 178
Cdd:cd03360  172 GAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 98-184 2.31e-21

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 85.52  E-value: 2.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  98 IGDNCLLAPGVHIytathpldaetrvGGAEFGK----PVrIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCV 173
Cdd:COG1045   94 IGDNVTIYQGVTL-------------GGTGKEKgkrhPT-IGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                         90
                 ....*....|.
gi 751567988 174 VGGNPARIIKQ 184
Cdd:COG1045  160 VVGVPARIVKR 170
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 78-179 1.15e-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: 84.47  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   78 LGKNFYANFDCVIldVCEVHIGDNCLLAPGVHIytathpldaetrvGGAefgkpVRIGDNVWIGGRAVINPGVTIGDNAV 157
Cdd:TIGR03570 120 IGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 751567988  158 VASGAVVTKDVPANCVVGGNPA 179
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 9-57 3.98e-19

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: 76.38  E-value: 3.98e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 751567988    9 KMIAGELYDAGDDLLRSERRRARQLTHRYNHSSPEEGELRKQWLGELLG 57
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFG 49
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 96-178 1.69e-18

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: 76.32  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvGGAEFGKPVR---IGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANC 172
Cdd:cd03354   29 AVIGDNCTIYQGVTL-------------GGKGKGGGKRhptIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANS 95


                 ....*.
gi 751567988 173 VVGGNP 178
Cdd:cd03354   96 TVVGVP 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 76-165 2.34e-17

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: 72.67  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  76 IYLGKNFYANFDCVILDvcEVHIGDNCLLAPGVHIYTATHPldaetrvggaEFGKPVRIGDNVWIGGRAVINPGVTIGDN 155
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                         90
                 ....*....|
gi 751567988 156 AVVASGAVVT 165
Cdd:cd00208   69 AVIGAGAVVT 78
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 76-183 4.47e-17

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 74.91  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  76 IYLGKNFYANFDCVILDVCEVHIGDNCLLAPGVHIYTATH-PLDAETRVGGAEF--------GKPVRIGDNVWIGGRAVI 146
Cdd:PRK09677  66 LFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgSFKHSDDFSSPNLppdmrtleSSAVVIGQRVWIGENVTI 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751567988 147 NPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIK 183
Cdd:PRK09677 146 LPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 96-184 1.61e-16

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: 73.60  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLApgvhiytathpldAETRVGGAefgkpVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVG 175
Cdd:cd03352  133 VRIGENCLIA-------------AQVGIAGS-----TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVS 194


                 ....*....
gi 751567988 176 GNPARIIKQ 184
Cdd:cd03352  195 GTPAQPHRE 203
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 88-185 3.44e-15

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 69.29  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  88 CVI--LDVCEVHIGDNCLLAPGVHIYTAThpldaetrvggaefgkpvrIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:COG0663   62 VVLhvDPGYPLTIGDDVTIGHGAILHGCT-------------------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVT 122

                         90       100
                 ....*....|....*....|..
gi 751567988 166 --KDVPANCVVGGNPARIIKQL 185
Cdd:COG0663  123 egKVVPPGSLVVGSPAKVVREL 144
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 97-181 1.09e-13

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: 67.07  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  97 HIGDNCLLAPGVHIytaTHpldaETRVG-------GAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVP 169
Cdd:cd03351  104 RIGNNNLLMAYVHV---AH----DCVIGnnvilanNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVP 176

                         90
                 ....*....|..
gi 751567988 170 ANCVVGGNPARI 181
Cdd:cd03351  177 PYVIAAGNRARL 188
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 69-185 1.16e-13

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: 65.13  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  69 RCDYGYnIYLGKNfyanfdCVILDVCEVH--------IGDNCLLAPGVHIYTAThpldaetrvggaefgkpvrIGDNVWI 140
Cdd:cd04645   33 RGDVNP-IRIGER------TNIQDGSVLHvdpgyptiIGDNVTVGHGAVLHGCT-------------------IGDNCLI 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751567988 141 GGRAVINPGVTIGDNAVVASGAVVT--KDVPANCVVGGNPARIIKQL 185
Cdd:cd04645   87 GMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 96-184 2.25e-13

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: 66.96  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLApgvhiytathpldAETRVGGAefgkpVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVG 175
Cdd:COG1044  241 VRIGEHTAIA-------------AQVGIAGS-----TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYS 302


                 ....*....
gi 751567988 176 GNPARIIKQ 184
Cdd:COG1044  303 GSPAQPHRE 311
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 98-181 8.52e-12

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: 61.57  E-value: 8.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  98 IGDNCLLAPGVHIytAtHplDAetRVG-------GAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPA 170
Cdd:COG1043  107 IGDDNLLMAYVHV--A-H--DC--VVGnnvilanNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPP 179

                         90
                 ....*....|.
gi 751567988 171 NCVVGGNPARI 181
Cdd:COG1043  180 YVLAAGNPARL 190
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-184 1.67e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.69  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrVGGAefgkpvRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCV-V 174
Cdd:PRK00892 244 VVIGRHTAIAAQVGI------------AGST------KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEyS 305

                         90
                 ....*....|
gi 751567988 175 GGNPARIIKQ 184
Cdd:PRK00892 306 SGIPAQPNKE 315
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 75-185 5.33e-11

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 57.99  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  75 NIYLGKNFYANFDCVIL-DVCEVHIGDNCLLAPGVHIytaTHPLDAETrvGGAEFGkPVRIGDNVWI------------- 140
Cdd:cd03359   21 NIVLNGKTIIQSDVIIRgDLATVSIGRYCILSEGCVI---RPPFKKFS--KGVAFF-PLHIGDYVFIgencvvnaaqigs 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 751567988 141 ----GGRAVINPGVTIGDNAVVASGAVVTKD--VPANCVVGGNPARIIKQL 185
Cdd:cd03359   95 yvhiGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGEL 145
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 96-182 1.14e-09

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 55.73  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   96 VHIGDNCLLAPGVHIytaTHPLDAETRV---GGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANC 172
Cdd:TIGR01852 102 TRIGNNNLLMAYSHI---AHDCVVGNHVilaNNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYC 178

                          90
                  ....*....|
gi 751567988  173 VVGGNPARII 182
Cdd:TIGR01852 179 LAEGNRARLR 188
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
98-181 1.22e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 55.87  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  98 IGDNCLLAPGVHIytaTHplDAetRVG-------GAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPA 170
Cdd:PRK05289 108 IGDNNLLMAYVHV---AH--DC--VVGnhvilanNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPP 180

                         90
                 ....*....|.
gi 751567988 171 NCVVGGNPARI 181
Cdd:PRK05289 181 YVLAEGNPARL 191
PLN02357 PLN02357
serine acetyltransferase
 133-182 6.06e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.12  E-value: 6.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARII 182
Cdd:PLN02357 280 KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 96-164 6.20e-09

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: 53.87  E-value: 6.20e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVV 164
Cdd:COG1044  127 VVIGDGVVIGPGVVI------------------GDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-164 7.64e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 7.64e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVV 164
Cdd:PRK00892 131 VVIGDGVVIGAGAVI------------------GDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
PLN02296 PLN02296
carbonate dehydratase
 88-185 8.89e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 53.21  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  88 CVIL-DVCEVHIG------DNCLlapgVHIytathpldAETRVGGAEFgkPVRIGDNVWIGGRAVINP------------ 148
Cdd:PLN02296  83 CVLRgDVNSISVGsgtniqDNSL----VHV--------AKTNLSGKVL--PTIIGDNVTIGHSAVLHGctvedeafvgmg 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751567988 149 -----GVTIGDNAVVASGAVVTKD--VPANCVVGGNPARIIKQL 185
Cdd:PLN02296 149 atlldGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
PLN02739 PLN02739
serine acetyltransferase
 96-183 1.69e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 52.73  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpLDAETRVG-GAEFG-KPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCV 173
Cdd:PLN02739 226 VVIGETAVIGDRVSI------LHGVTLGGtGKETGdRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSM 299

                         90
                 ....*....|
gi 751567988 174 VGGNPARIIK 183
Cdd:PLN02739 300 VAGNPAKLIG 309
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 97-181 2.25e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 51.95  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  97 HIGDNCLLAPGVHIYTATHPLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGG 176
Cdd:PRK12461 103 RIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAG 182


                 ....*
gi 751567988 177 NPARI 181
Cdd:PRK12461 183 HPTNV 187
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 96-174 2.56e-08

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 50.46  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIYTATHPLDAetrvggaefgKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTK--------- 166
Cdd:cd03350   50 AQIGKNVHLSAGAVIGGVLEPLQA----------TPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydret 119

                         90
                 ....*....|....
gi 751567988 167 ------DVPANCVV 174
Cdd:cd03350  120 geiyygRVPPGSVV 133
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 133-185 3.22e-08

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 50.65  E-value: 3.22e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT--KDVPANCVVGGNPARIIKQL 185
Cdd:cd04650   80 KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
PLN02694 PLN02694
serine O-acetyltransferase
 133-182 9.75e-08

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 50.41  E-value: 9.75e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARII 182
Cdd:PLN02694 214 KIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 96-176 1.10e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.71  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVP------ 169
Cdd:cd03352    2 AKIGENVSIGPNAVI------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIigdrvi 63


                 ....*....
gi 751567988 170 --ANCVVGG 176
Cdd:cd03352   64 ihSGAVIGS 72
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 134-174 1.20e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 49.34  E-value: 1.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 751567988 134 IGDNVWIG-GRAVINPgVTIGDNAVVASGAVVTKDVPANCVV 174
Cdd:cd03353  147 IGDNVFIGsNSQLVAP-VTIGDGATIAAGSTITKDVPPGALA 187
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 96-175 1.87e-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: 49.63  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTkdvpANCVVG 175
Cdd:COG1044  109 AKIGEGVSIGPFAVI------------------GAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIY----ERCVIG 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-174 1.95e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVP--ANCV 173
Cdd:PRK00892 113 AKIGEGVSIGPNAVI------------------GAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRigNRVI 174


                 .
gi 751567988 174 V 174
Cdd:PRK00892 175 I 175
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 133-171 2.01e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 49.86  E-value: 2.01e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPAN 171
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDD 420
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 134-183 2.38e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 49.64  E-value: 2.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 751567988 134 IGDNVWIGGRAV-INPgVTIGDNAVVASGAVVTKDVPANC-VVGGNPARIIK 183
Cdd:COG1207  397 IGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPAGAlAIARARQRNIE 447
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 96-184 2.61e-07

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: 48.96  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLLAPGVHIYTATHPLDAEtrvggaefgkPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTK--------- 166
Cdd:COG2171  145 AQIGKNVHLSGGAGIGGVLEPLQAA----------PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvt 214

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751567988 167 ------DVPANCVV------------GGNPARIIKQ 184
Cdd:COG2171  215 gevyygRVPAGSVVvpgslpgkdgdyGLYCAVIVKR 250
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
132-166 3.93e-07

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 44.74  E-value: 3.93e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 751567988  132 VRIGDNVWIGGRAVInpGVTIGDNAVVASGAVVTK 166
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 96-185 5.02e-07

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: 47.36  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGDNCLL--APGVHIYtathpLDAETRVGGAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTK--DVPAN 171
Cdd:cd04745   46 ANVQDNCVIhgFPGQDTV-----LEENGHIGHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPR 120

                         90
                 ....*....|....
gi 751567988 172 CVVGGNPARIIKQL 185
Cdd:cd04745  121 SLIAGSPAKVIREL 134
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 132-177 5.71e-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: 48.48  E-value: 5.71e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 751567988 132 VRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVP--ANCVVGGN 177
Cdd:COG1044  109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVigDDCVLHPN 156
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
131-160 6.91e-07

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.86  E-value: 6.91e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 751567988  131 PVRIGDNVWIGGRAVINPGVTIGDNAVVAS 160
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 96-179 7.60e-07

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.21  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   96 VHIGDNCLLAPGVHIytATHPLdaETRVGGAEFgkpVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTK--DVPANCV 173
Cdd:TIGR02353 617 VTIGDDSTLNEGSVI--QTHLF--EDRVMKSDT---VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTR 689


                  ....*.
gi 751567988  174 VGGNPA 179
Cdd:TIGR02353 690 WRGNPA 695
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-183 7.84e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 48.00  E-value: 7.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  95 EVHIGDNCLLAPGVHIYTAThpLDAETRV------GGAEFGKPV-------------------RIGDNVWIGGRAVINPG 149
Cdd:PRK14360 331 EAQIGSNCRIGNFVEIKKSQ--LGEGSKVnhlsyiGDATLGEQVnigagtitanydgvkkhrtVIGDRSKTGANSVLVAP 408

                         90       100       110
                 ....*....|....*....|....*....|....
gi 751567988 150 VTIGDNAVVASGAVVTKDVPANCVVGGNPARIIK 183
Cdd:PRK14360 409 ITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 132-177 9.81e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.83  E-value: 9.81e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 751567988 132 VRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVP--ANCVVGGN 177
Cdd:PRK00892 113 AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKigADCRLHAN 160
PRK10191 PRK10191
putative acyl transferase; Provisional
 54-181 1.20e-06

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 46.04  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  54 ELLGGYQ---GGTIEPTFRCDYGYNIYLGKNFYAnfdcvildvcevhiGDNCLLAPGVHIytathpldaeTRVGGAEFGK 130
Cdd:PRK10191  37 ECFFGYEiqaAATIGRRFTIHHGYAVVINKNVVA--------------GDDFTIRHGVTI----------GNRGADNMAC 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 751567988 131 PVrIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARI 181
Cdd:PRK10191  93 PH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 98-174 3.81e-06

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 45.57  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  98 IGDNCLLAPGVHIYTATHPLDAetrvggaefgKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTK----------- 166
Cdd:PRK11830 153 IGKNVHLSGGVGIGGVLEPLQA----------NPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretge 222

                         90
                 ....*....|..
gi 751567988 167 ----DVPANCVV 174
Cdd:PRK11830 223 vhygRVPAGSVV 234
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-171 4.85e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.59  E-value: 4.85e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 751567988 134 IGDNVWIGGRA-VINPgVTIGDNAVVASGAVVTKDVPAN 171
Cdd:PRK14354 396 IGDNAFIGCNSnLVAP-VTVGDNAYIAAGSTITKDVPED 433
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-171 6.27e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.49  E-value: 6.27e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 751567988 134 IGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPAN 171
Cdd:PRK14356 401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDG 438
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 129-164 6.48e-06

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: 45.01  E-value: 6.48e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 751567988 129 GKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVV 164
Cdd:COG1043   29 GPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
98-164 8.67e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.70  E-value: 8.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751567988  98 IGDNCLLAPGVHIytathpldaetrvggaefGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVV 164
Cdd:PRK05289  17 IGENVEIGPFCVI------------------GPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-184 1.24e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 44.75  E-value: 1.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 751567988 131 PVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVVGGNPARIIKQ 184
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 129-164 6.01e-05

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: 42.03  E-value: 6.01e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 751567988 129 GKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVV 164
Cdd:cd03351   27 GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-182 6.54e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.62  E-value: 6.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 751567988 134 IGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANC-VVGGNPARII 182
Cdd:PRK14352 402 IGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGAlAVSEGPQRNI 451
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-171 8.44e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 8.44e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 751567988 134 IGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPAN 171
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPD 437
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 96-179 1.09e-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: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988   96 VHIGDNCLLAPGVHIytATHPLDAE-TRVGgaefgkPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKD--VPANC 172
Cdd:TIGR02353 132 LTIGAGTIVRKEVML--LGYRAERGrLHTG------PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGE 203


                  ....*..
gi 751567988  173 VVGGNPA 179
Cdd:TIGR02353 204 RWHGSPA 210
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-174 1.43e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.55  E-value: 1.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751567988  98 IGDNCLLAPGvhiyTATHPLDaetrvgGAEFGKPVrIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDVPANCVV 174
Cdd:PRK09451 372 IGDNVNIGAG----TITCNYD------GANKFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 117-182 2.73e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.39  E-value: 2.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751567988 117 LDAETRVG-GAEFGKPVRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVTKDvPANCVVGGNPARII 182
Cdd:PRK12461  14 LGSGVEIGpFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE-PQDFTYKGEESRLE 79
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 69-171 3.52e-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: 39.15  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  69 RCDYGYNIYLGKNfyANF-DCVI---LDVCEVHIGDNCLLAPGVHIY-TAThpLDAETRVGgaeFGKPV---RIGDNVWI 140
Cdd:cd00710   36 RADEGTPIIIGAN--VNIqDGVVihaLEGYSVWIGKNVSIAHGAIVHgPAY--IGDNCFIG---FRSVVfnaKVGDNCVI 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 751567988 141 GGRAVINpGVTIGDNAVVASGAVVTKDVPAN 171
Cdd:cd00710  109 GHNAVVD-GVEIPPGRYVPAGAVITSQTQAD 138
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 88-168 4.83e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.22  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  88 CVILDVCEVH---IGDNCLLAPGVHIytathpldAETRVGGAefgkpVRIGDNVWIGGrAVINPGVTIGDNAVVASGAVV 164
Cdd:cd03356    6 TVIGENAIIKnsvIGDNVRIGDGVTI--------TNSILMDN-----VTIGANSVIVD-SIIGDNAVIGENVRVVNLCII 71


                 ....
gi 751567988 165 TKDV 168
Cdd:cd03356   72 GDDV 75
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-169 6.05e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.59  E-value: 6.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 751567988 134 IGDNVWIGGRA-VINPgVTIGDNAVVASGAVVTKDVP 169
Cdd:PRK14359 370 IGKNVFIGSDTqLVAP-VNIEDNVLIAAGSTVTKDVP 405
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
133-165 6.10e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 6.10e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVID 48
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 95-177 9.53e-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: 37.99  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  95 EVHIGDNCLLAPGVHIYtathpldaetrvggAEFGKPVRIGDN----------------VWIGGRAVINPG------VTI 152
Cdd:cd00710   20 DVIIGDNVFVGPGASIR--------------ADEGTPIIIGANvniqdgvvihalegysVWIGKNVSIAHGaivhgpAYI 85

                         90       100
                 ....*....|....*....|....*.
gi 751567988 153 GDNAVVASGAVVTK-DVPANCVVGGN 177
Cdd:cd00710   86 GDNCFIGFRSVVFNaKVGDNCVIGHN 111
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 133-165 1.23e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 38.46  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 751567988 133 RIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:COG1043   15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIE 47
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 132-165 1.46e-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: 38.18  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 751567988 132 VRIGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:cd03351   12 AKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVID 45
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 117-177 1.71e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 35.68  E-value: 1.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751567988 117 LDAETRVGGAEFGKPVRIGDNVWIGGRAVIN-----PGVTIGDNAVVaSGAVVTKdvpaNCVVGGN 177
Cdd:cd03356    2 IGESTVIGENAIIKNSVIGDNVRIGDGVTITnsilmDNVTIGANSVI-VDSIIGD----NAVIGEN 62
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 96-169 2.99e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.65  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  96 VHIGD-----NCLLAPGV---HI-YTATHPLDAETRVGG----AEFG----KPVRIGDNVWIGGRAVINPGVTIGDNAVV 158
Cdd:PRK14358 347 VHIGNfvetkNARLDAGVkagHLaYLGDVTIGAETNVGAgtivANFDgvnkHQSKVGAGVFIGSNTTLIAPRVVGDAAFI 426

                         90
                 ....*....|.
gi 751567988 159 ASGAVVTKDVP 169
Cdd:PRK14358 427 AAGSAVHDDVP 437
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 95-175 4.78e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 36.93  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751567988  95 EVHIGDNCLLAPGVHIYtathpldaetrvggaefGKpVRIGDNVWIGGRAVINpGVTIGDNAVV----ASGAVVTkdvpA 170
Cdd:COG1207  266 DVEIGRDVVIDPNVILE-----------------GK-TVIGEGVVIGPNCTLK-DSTIGDGVVIkysvIEDAVVG----A 322


                 ....*
gi 751567988 171 NCVVG 175
Cdd:COG1207  323 GATVG 327
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 134-165 6.79e-03

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 35.64  E-value: 6.79e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 751567988 134 IGDNVWIGGRAVINPGVTIGDNAVVASGAVVT 165
Cdd:cd05636  132 IGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
 
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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