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Conserved domains on  [gi|1468733855|gb|AXT49808|]
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sialic acid O-acetyltransferase [Aquimarina sp. BL5]

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 ...
 5-206 2.50e-49

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 TIGR03570:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 201  Bit Score: 159.58  E-value: 2.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855   5 VIIGAGTQGQVYASYLKEAGVNIIGFIDDNPDLIGKEVINIPVIGKYKDLflDEFKNKIHDVYCPIGVNAVRVEYLSTLK 84
Cdd:TIGR03570   3 VIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDL--LRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  85 KEGYGIPGFLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNA 164
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPA 206
Cdd:TIGR03570 161 FIGAGATIIQGVT-IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-206 2.50e-49

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: 159.58  E-value: 2.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855   5 VIIGAGTQGQVYASYLKEAGVNIIGFIDDNPDLIGKEVINIPVIGKYKDLflDEFKNKIHDVYCPIGVNAVRVEYLSTLK 84
Cdd:TIGR03570   3 VIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDL--LRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  85 KEGYGIPGFLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNA 164
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPA 206
Cdd:TIGR03570 161 FIGAGATIIQGVT-IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-205 1.95e-48

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: 156.88  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855   6 IIGAGTQGQVYASYLKEA-GVNIIGFIDDNPDLIGKEVINIPVIGkykDLFLDEFKNKIHDVYCPIGVNAVRVEYLSTLK 84
Cdd:cd03360     1 IIGAGGHARVVADILEADsGYEVVGFLDDDPELKGTEGLGLPVGL---DELLLLYPPPDDEFVVAIGDNKLRRKLAEKLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  85 KEGYGIPGFLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNA 164
Cdd:cd03360    78 AAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNP 205
Cdd:cd03360   158 FIGAGATIIQGVT-IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
93-214 2.62e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 85.69  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIvmphtTIGNYIMINMDSTI--AHHVTLEDGVFMSSGVNIGAL------------- 157
Cdd:COG0110     4 LLLFGARIGDGVVIGPGVRIYGGNI-----TIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpatfplr 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 158 ---INVRKNAYIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQP 214
Cdd:COG0110    79 tgpVTIGDDVWIGAGATILPGVT-IGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
PLN02694 PLN02694
serine O-acetyltransferase
 98-213 1.82e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 61.97  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  98 VSIAPDVTIGEAvymlagnIVMPHTT---IGNYIMINMDSTIAHHVTLeDGVFMSSG-----VNIGALInvrknayiGMG 169
Cdd:PLN02694  161 VDIHPAAKIGKG-------ILFDHATgvvIGETAVIGNNVSILHHVTL-GGTGKACGdrhpkIGDGVLI--------GAG 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1468733855 170 VTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQ 213
Cdd:PLN02694  225 ATILGNVK-IGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKE 267
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 3-76 7.93e-07

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 45.25  E-value: 7.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1468733855   3 NAVIIGAGTQGQVYASYLKEAGV-NIIGFIDDNPDligKEVINIPVIGKyKDLFLDEFKNKIHDVYCPIGVNAVR 76
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAMGEyEIIGFLDDNKK---TEVNGYPVLGG-DIDLLASLSPDEYDVVIAIGNNKVR 71
 
Name Accession Description Interval E-value
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-206 2.50e-49

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: 159.58  E-value: 2.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855   5 VIIGAGTQGQVYASYLKEAGVNIIGFIDDNPDLIGKEVINIPVIGKYKDLflDEFKNKIHDVYCPIGVNAVRVEYLSTLK 84
Cdd:TIGR03570   3 VIIGAGGHGRVVADILERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDL--LRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  85 KEGYGIPGFLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNA 164
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPA 206
Cdd:TIGR03570 161 FIGAGATIIQGVT-IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-205 1.95e-48

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: 156.88  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855   6 IIGAGTQGQVYASYLKEA-GVNIIGFIDDNPDLIGKEVINIPVIGkykDLFLDEFKNKIHDVYCPIGVNAVRVEYLSTLK 84
Cdd:cd03360     1 IIGAGGHARVVADILEADsGYEVVGFLDDDPELKGTEGLGLPVGL---DELLLLYPPPDDEFVVAIGDNKLRRKLAEKLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  85 KEGYGIPGFLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNA 164
Cdd:cd03360    78 AAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNP 205
Cdd:cd03360   158 FIGAGATIIQGVT-IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
93-214 2.62e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 85.69  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIvmphtTIGNYIMINMDSTI--AHHVTLEDGVFMSSGVNIGAL------------- 157
Cdd:COG0110     4 LLLFGARIGDGVVIGPGVRIYGGNI-----TIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpatfplr 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 158 ---INVRKNAYIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQP 214
Cdd:COG0110    79 tgpVTIGDDVWIGAGATILPGVT-IGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 100-210 1.09e-16

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: 72.92  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 100 IAPDVTIGEAVYmlagniVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGV------NIGALIN---------VRKNA 164
Cdd:cd03358     1 IGDNCIIGTNVF------IENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVvftndlYPRSKIYrkwelkgttVKRGA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1468733855 165 YIGMGVTAMTGIkEIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:cd03358    75 SIGANATILPGV-TIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 104-209 1.19e-14

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: 68.60  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 104 VTIGEAVYMLAGNIVMPHT--TIGNYIMI--NMD-STIAHHVTLEDgvfMSSGVNIGALINVRKNAYIGMGVTAMTGIKe 178
Cdd:cd03357    63 IHIGDNFYANFNCTILDVApvTIGDNVLIgpNVQiYTAGHPLDPEE---RNRGLEYAKPITIGDNVWIGGGVIILPGVT- 138

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1468733855 179 IGKETLIGAGTVIIKDVPEYTTVVGNPARVI 209
Cdd:cd03357   139 IGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 98-209 1.41e-13

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: 64.40  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  98 VSIAPDVTIGEAVYMLAGNIVmphtTIGNYIMINMDSTI-AHHVTLEDGVFMSSGVNIGALINVRKNAYIGMGVTAMTGI 176
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGI----TIGDNVLIGPNVTIyDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGV 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1468733855 177 KeIGKETLIGAGTVIIKDVPEYTTVVGNPARVI 209
Cdd:cd04647    78 T-IGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 120-212 1.17e-11

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: 60.87  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 120 PHTTIGNYIMInmdstiaHHVT---------LEDGVFMSSGVNIGALIN--------VRKNAYIGMGVTAMTGIkEIGKE 182
Cdd:COG1045    70 PGATIGRGFFI-------DHGTgvvigetavIGDNVTIYQGVTLGGTGKekgkrhptIGDNVVIGAGAKILGPI-TIGDN 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1468733855 183 TLIGAGTVIIKDVPEYTTVVGNPARVIKTK 212
Cdd:COG1045   142 AKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
PLN02694 PLN02694
serine O-acetyltransferase
 98-213 1.82e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 61.97  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  98 VSIAPDVTIGEAvymlagnIVMPHTT---IGNYIMINMDSTIAHHVTLeDGVFMSSG-----VNIGALInvrknayiGMG 169
Cdd:PLN02694  161 VDIHPAAKIGKG-------ILFDHATgvvIGETAVIGNNVSILHHVTL-GGTGKACGdrhpkIGDGVLI--------GAG 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1468733855 170 VTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQ 213
Cdd:PLN02694  225 ATILGNVK-IGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKE 267
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
 1-54 5.46e-11

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 57.63  E-value: 5.46e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468733855   1 MKNAVIIGAGTQGQVYASYLK---EAGVNIIGFIDDNPDLIGKEVINIPVIGKYKDL 54
Cdd:COG1086    21 KRRVLIVGAGEAGRQLARALRrnpDLGYRVVGFVDDDPDKRGRRIEGVPVLGTLDDL 77
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 93-211 2.53e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.96  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAG----------------NI---VMPHTTIGNYIMINMDSTIAHHVTLEdgvfmssGVN 153
Cdd:COG0663    18 FVAPTAVVIGDVTIGEDVSVWPGavlrgdvgpirigegsNIqdgVVLHVDPGYPLTIGDDVTIGHGAILH-------GCT 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 154 IGalinvrKNAYIGMGVTAMTGIKeIGKETLIGAGTVII--KDVPEYTTVVGNPARVIKT 211
Cdd:COG0663    91 IG------DNVLIGMGAIVLDGAV-IGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRE 143
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 122-208 5.63e-10

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: 57.34  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 122 TTIG--NYIMINmdSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmgvtAMTGIKE---IGKETLIGAGTVIIKDVP 196
Cdd:COG1043   105 TRIGddNLLMAY--VHVAHDCVVGNNVILANNATLAGHVEVGDHAIIG----GLSAVHQfvrIGAHAMVGGGSGVVKDVP 178

                          90
                  ....*....|..
gi 1468733855 197 EYTTVVGNPARV 208
Cdd:COG1043   179 PYVLAAGNPARL 190
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 166-210 5.99e-10

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: 55.63  E-value: 5.99e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1468733855 166 IGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:cd03349    82 IGHGATILPGVT-IGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 122-208 7.49e-10

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: 57.06  E-value: 7.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 122 TTIG--NYIMINmdSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmGVTAMTGIKEIGKETLIGAGTVIIKDVPEYT 199
Cdd:cd03351   103 TRIGnnNLLMAY--VHVAHDCVIGNNVILANNATLAGHVEIGDYAIIG-GLSAVHQFCRIGRHAMVGGGSGVVQDVPPYV 179


                  ....*....
gi 1468733855 200 TVVGNPARV 208
Cdd:cd03351   180 IAAGNRARL 188
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 121-209 1.61e-09

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: 53.38  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 121 HTTIGNYIMI-------NMDS-TIAHHVTLEDGVFMSSG---------------VNIGALINVRKNAYIGMGVTamtgik 177
Cdd:cd05825     3 NLTIGDNSWIgegvwiyNLAPvTIGSDACISQGAYLCTGshdyrspafplitapIVIGDGAWVAAEAFVGPGVT------ 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1468733855 178 eIGKETLIGAGTVIIKDVPEYTTVVGNPARVI 209
Cdd:cd05825    77 -IGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PLN02357 PLN02357
serine acetyltransferase
 98-213 1.67e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 56.43  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  98 VSIAPDVTIGEAvymlagnIVMPHTT---IGNYIMINMDSTIAHHVTLeDGVFMSSGvnigalinvRKNAYIGMGV---- 170
Cdd:PLN02357  227 VDIHPGAKIGQG-------ILLDHATgvvIGETAVVGNNVSILHNVTL-GGTGKQSG---------DRHPKIGDGVliga 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1468733855 171 -TAMTGIKEIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQ 213
Cdd:PLN02357  290 gTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKE 333
cysE PRK11132
serine acetyltransferase; Provisional
 93-209 2.06e-09

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 55.86  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGnIVMPHTT---IGNYIMINMDSTIAHHVTLeDGVFMSSGvniGALINVRKNAYIGMG 169
Cdd:PRK11132  131 YLQNQISVAFQVDIHPAAKIGRG-IMLDHATgivIGETAVIENDVSILQSVTL-GGTGKTSG---DRHPKIREGVMIGAG 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1468733855 170 VTAMTGIkEIGKETLIGAGTVIIKDVPEYTTVVGNPARVI 209
Cdd:PRK11132  206 AKILGNI-EVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
122-208 5.98e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 54.33  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 122 TTIG--NYIMINmdSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmgvtAMTGIKE---IGKETLIGAGTVIIKDVP 196
Cdd:PRK05289  106 TRIGdnNLLMAY--VHVAHDCVVGNHVILANNATLAGHVEVGDYAIIG----GLTAVHQfvrIGAHAMVGGMSGVSQDVP 179

                          90
                  ....*....|..
gi 1468733855 197 EYTTVVGNPARV 208
Cdd:PRK05289  180 PYVLAEGNPARL 191
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 120-205 1.56e-08

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: 50.52  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 120 PHTTIGNYIMIN--MDSTIAHHVTLEDGVFMSSGVNIGALIN--------VRKNAYIGMGVTAMTGIkEIGKETLIGAGT 189
Cdd:cd03354     7 PGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKgggkrhptIGDNVVIGAGAKILGNI-TIGDNVKIGANA 85

                          90
                  ....*....|....*.
gi 1468733855 190 VIIKDVPEYTTVVGNP 205
Cdd:cd03354    86 VVTKDVPANSTVVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 98-210 1.96e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 53.50  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  98 VSIAPDVTIGEAVYMLAGNIVMphttIGNYIMINMDSTIAHHVTLeDGVFMSSG---VNIGalinvrKNAYIGMGVTAMT 174
Cdd:PLN02739  206 IDIHPAARIGKGILLDHGTGVV----IGETAVIGDRVSILHGVTL-GGTGKETGdrhPKIG------DGALLGACVTILG 274

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1468733855 175 GIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:PLN02739  275 NIS-IGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 99-210 2.81e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 51.93  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  99 SIAPDVTIGEAVYM-LAGNIVMPHT-TIGNYIMINMDSTIA------HHVTLEDGVFMSSGVNIGalinvrKNAYIGMGV 170
Cdd:PRK09527   71 SYGSNIHIGRNFYAnFNLTIVDDYTvTIGDNVLIAPNVTLSvtghpvHHELRKNGEMYSFPITIG------NNVWIGSHV 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1468733855 171 TAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:PRK09527  145 VINPGVT-IGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 89-209 2.83e-08

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: 52.26  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  89 GIPGFLHHT-----VSIAPDVTIGEAVYMLAGNIVMPHTT-IGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRK 162
Cdd:TIGR01852  63 GVPQDLKYKgektrLIIGDNNTIREFVTINRGTASGGGVTrIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGD 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1468733855 163 NAYIGmGVTAMTGIKEIGKETLIGAGTVIIKDVPEYTTVVGNPARVI 209
Cdd:TIGR01852 143 YAIIG-GLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLR 188
PRK10502 PRK10502
putative acyl transferase; Provisional
 123-212 4.37e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 51.10  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 123 TIGNYIMI-------NMDS-TIAHHVTLEDGVFMSSGVN---------IGALINVRKNAYIGMGVTAMTGIKeIGKETLI 185
Cdd:PRK10502   73 TIGDYAWIgddvwlyNLGEiTIGAHCVISQKSYLCTGSHdysdphfdlNTAPIVIGEGCWLAADVFVAPGVT-IGSGAVV 151

                          90       100
                  ....*....|....*....|....*..
gi 1468733855 186 GAGTVIIKDVPEYTTVVGNPARVIKTK 212
Cdd:PRK10502  152 GARSSVFKSLPANTICRGNPAVPIRPR 178
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 144-211 3.86e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 48.27  E-value: 3.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468733855 144 DGVFMSSGVNIGALINVRKNAYIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKT 211
Cdd:PRK10092  116 DPVARNSGAELGKPVTIGNNVWIGGRAVINPGVT-IGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 3-76 7.93e-07

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 45.25  E-value: 7.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1468733855   3 NAVIIGAGTQGQVYASYLKEAGV-NIIGFIDDNPDligKEVINIPVIGKyKDLFLDEFKNKIHDVYCPIGVNAVR 76
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAMGEyEIIGFLDDNKK---TEVNGYPVLGG-DIDLLASLSPDEYDVVIAIGNNKVR 71
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-210 2.43e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 47.45  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 100 IAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINmDSTI-----AHHVTLEDGVFMSSGVNIGA------LINVRKN-AYIG 167
Cdd:PRK14357  309 IEDDVSVGPFSRLREGTVLKKSVKIGNFVEIK-KSTIgentkAQHLTYLGDATVGKNVNIGAgtitcnYDGKKKNpTFIE 387

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1468733855 168 MGV-----TAMTGIKEIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:PRK14357  388 DGAfigsnSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 149-210 3.44e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 46.02  E-value: 3.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468733855 149 SSGVNIGalinvrKNAYIGMGVTAMTGIKeIGKETLIGAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:PRK09677  128 SSAVVIG------QRVWIGENVTILPGVS-IGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 86-214 4.77e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.26  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  86 EGYGIPGFLH-HTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYImiNMDSTI------AHHVTLEDGVFMSSGVNIGA-- 156
Cdd:PRK14356  309 SGATIHSFSHlEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFV--EMKKAVlgkgakANHLTYLGDAEIGAGANIGAgt 386

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468733855 157 -----------LINVRKNAYIGMGvTAMTGIKEIGKETLIGAGTVIIKDVPEYTTVVGNPARVIKTKQP 214
Cdd:PRK14356  387 itcnydgvnkhRTVIGEGAFIGSN-TALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQKNLPRKK 454
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 93-211 8.18e-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: 44.28  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYmlagniVMPHTTI---GNYIMIN----------MDSTIAHHVTLEDGvfmsSGVNIGALI- 158
Cdd:cd04745     8 FVHPTAVLIGDVIIGKNCY------IGPHASLrgdFGRIVIRdganvqdncvIHGFPGQDTVLEEN----GHIGHGAILh 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468733855 159 --NVRKNAYIGMGVTAMTGIkEIGKETLIGAGTVIIK--DVPEYTTVVGNPARVIKT 211
Cdd:cd04745    78 gcTIGRNALVGMNAVVMDGA-VIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRE 133
CoA_binding_3 pfam13727
CoA-binding domain;
2-68 1.24e-05

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 44.18  E-value: 1.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468733855   2 KNAVIIGAGTQGQVYASYLK---EAGVNIIGFIDDNPDLIGKEVINIPVIGKYKDL--FLDEfkNKIHDVYC 68
Cdd:pfam13727  78 RNNRRVVAVGGGLELARQIRanpWLGFRVVGVFDDRDDDRVPEVAGVPVLGNLADLveYVRE--TRVDEVYL 147
PRK05472 PRK05472
redox-sensing transcriptional repressor Rex; Provisional
 3-75 2.67e-05

redox-sensing transcriptional repressor Rex; Provisional


Pssm-ID: 235486 [Multi-domain]  Cd Length: 213  Bit Score: 43.57  E-value: 2.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1468733855   3 NAVIIGAGTQGQVYASY--LKEAGVNIIGFIDDNPDLIGKEVINIPVIGkykdlfLDEFKNKIHDVYCPIGVNAV 75
Cdd:PRK05472   86 NVALVGAGNLGRALLNYngFEKRGFKIVAAFDVDPEKIGTKIGGIPVYH------IDELEEVVKENDIEIGILTV 154
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-191 3.62e-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: 43.47  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  95 HHTVSIAPDVTIGEAVYmlagniVMPHTTIGNyiminmDSTIAHHVTLEDGVFMSSGVNIGAlinvrkNAYIGMGVTAMT 174
Cdd:COG1044   100 HPSAVIDPSAKIGEGVS------IGPFAVIGA------GVVIGDGVVIGPGVVIGDGVVIGD------DCVLHPNVTIYE 161

                          90
                  ....*....|....*..
gi 1468733855 175 GIKeIGKETLIGAGTVI 191
Cdd:COG1044   162 RCV-IGDRVIIHSGAVI 177
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 103-210 3.93e-05

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.48  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 103 DVTIGEAVYMLAGNIVMphttigNYiminmDSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmgvtamtgikeigke 182
Cdd:COG1207   369 DAEIGEGVNIGAGTITC------NY-----DGVNKHRTVIGDGAFIGSNTNLVAPVTIGDGATIG--------------- 422

                          90       100
                  ....*....|....*....|....*...
gi 1468733855 183 tligAGTVIIKDVPEYTTVVGNPARVIK 210
Cdd:COG1207   423 ----AGSTITKDVPAGALAIARARQRNI 446
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 122-208 4.55e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.09  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 122 TTIG--NYIMINmdSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmGVTAMTGIKEIGKETLIGAGTVIIKDVPEYT 199
Cdd:PRK12461  102 TRIGndNLLMAY--SHVAHDCQIGNNVILVNGALLAGHVTVGDRAIIS-GNCLVHQFCRIGALAMMAGGSRISKDVPPYC 178


                  ....*....
gi 1468733855 200 TVVGNPARV 208
Cdd:PRK12461  179 MMAGHPTNV 187
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 93-210 4.83e-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: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIV---MPHTTIGNYIMINMDSTI--AHHVTLEDGVFMSSGVNigALIN---VRKNA 164
Cdd:cd04650     8 YVHPTSYVIGDVVIGELTSVWHYAVIrgdNDSIYIGKYSNVQENVSIhtDHGYPTEIGDYVTIGHN--AVVHgakVGNYV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1468733855 165 YIGMGVTAMTGIKeIGKETLIGAGTVII--KDVPEYTTVVGNPARVIK 210
Cdd:cd04650    86 IVGMGAILLNGAK-IGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVR 132
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 97-207 7.81e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 42.01  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  97 TVSIAPDVTIGeavymlAGNIV----MPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGMGVTA 172
Cdd:cd03352    92 GVIIGDDVEIG------ANTTIdrgaLGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGI 165

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1468733855 173 MTGIkEIGKETLIGAGTVIIKDVPEYTTVVGNPAR 207
Cdd:cd03352   166 AGHL-TIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 93-191 8.23e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.66  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINmDSTI-------AHHV----------------TLEDGVFMS 149
Cdd:PRK14358  266 LIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVT-DSVLhegavikPHSVlegaevgagsdvgpfaRLRPGTVLG 344

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1468733855 150 SGVNIGALINVrKNAYIGMGVT----AMTGIKEIGKETLIGAGTVI 191
Cdd:PRK14358  345 EGVHIGNFVET-KNARLDAGVKaghlAYLGDVTIGAETNVGAGTIV 389
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 104-206 2.03e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 41.66  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 104 VTIGEAVYMLAGNIvmPHT---TIGNYIMINMDSTIAHHVtLEDGVFMSSGVNIGalinvrKNAYIGMGVTAMTGIkEIG 180
Cdd:TIGR02353 598 VKIGRGVYIDGTDL--TERdlvTIGDDSTLNEGSVIQTHL-FEDRVMKSDTVTIG------DGATLGPGAIVLYGV-VMG 667

                          90       100
                  ....*....|....*....|....*...
gi 1468733855 181 KETLIGAGTVIIK--DVPEYTTVVGNPA 206
Cdd:TIGR02353 668 EGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 103-203 2.84e-04

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: 40.10  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 103 DVTIGEAVYMLAGNIVMphttigNYiminmDSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYIGmgvtamtgikeigke 182
Cdd:cd03353   119 DAEIGEGVNIGAGTITC------NY-----DGVNKHRTVIGDNVFIGSNSQLVAPVTIGDGATIA--------------- 172

                          90       100
                  ....*....|....*....|.
gi 1468733855 183 tligAGTVIIKDVPEYTTVVG 203
Cdd:cd03353   173 ----AGSTITKDVPPGALAIA 189
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 95-211 3.01e-04

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: 39.70  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  95 HHTVSIAPDVTIGEAVyMLAGnivmphTTIGNYIMINMDSTIAHHVtledgvfmssgvnigalinvrknayigmgvtamt 174
Cdd:cd04645    58 GYPTIIGDNVTVGHGA-VLHG------CTIGDNCLIGMGAIILDGA---------------------------------- 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1468733855 175 gikEIGKETLIGAGTVII--KDVPEYTTVVGNPARVIKT 211
Cdd:cd04645    97 ---VIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-196 3.09e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.88  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 100 IAPDVTIGEAVYMLAGNIVMPHTTIGNY-----IMINMDSTIAHHVTLEDGVfMSSGVNIGA------LINVRKN-AYIG 167
Cdd:PRK14355  323 VGDDVAIGPMAHLRPGTELSAHVKIGNFvetkkIVMGEGSKASHLTYLGDAT-IGRNVNIGCgtitcnYDGVKKHrTVIE 401

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1468733855 168 MGVTAMTGIK-----EIGKETLIGAGTVIIKDVP 196
Cdd:PRK14355  402 DDVFVGSDVQfvapvTVGRNSLIAAGTTVTKDVP 435
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 94-156 4.42e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 4.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468733855  94 LHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDS------TIAHHVTLEDGVFMSSGVNIGA 156
Cdd:PRK00892  115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCrlhanvTIYHAVRIGNRVIIHSGAVIGS 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 93-156 5.21e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.70  E-value: 5.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGA 156
Cdd:cd03352     9 SIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGS 72
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-198 5.33e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855 103 DVTIGEAVYMLAGNIVmphttignyimINMDSTIAHHVTLEDGVFMSSGVNIGALINVRKNAYigmgvtamtgikeigke 182
Cdd:PRK14354  368 DAEVGENVNIGCGTIT-----------VNYDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAY----------------- 419

                          90
                  ....*....|....*.
gi 1468733855 183 tlIGAGTVIIKDVPEY 198
Cdd:PRK14354  420 --IAAGSTITKDVPED 433
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-191 8.33e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  95 HHTVSIAPDVTIGEAVYmlagniVMPHTTIGNyiminmDSTIAHHVTLEDGVFMSSGVNIGAlinvrkNAYIGMGVTAMT 174
Cdd:PRK00892  104 HPSAVIDPSAKIGEGVS------IGPNAVIGA------GVVIGDGVVIGAGAVIGDGVKIGA------DCRLHANVTIYH 165

                          90
                  ....*....|....*..
gi 1468733855 175 GIKeIGKETLIGAGTVI 191
Cdd:PRK00892  166 AVR-IGNRVIIHSGAVI 181
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 93-190 1.38e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.17  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  93 FLHHTVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINmDSTIAHHVTLE-----DGVFMSSGVNIGALINVR------ 161
Cdd:cd03353    11 YIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKassviEGAVIGNGATVGPFAHLRpgtvlg 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1468733855 162 -----------KNAYIGMGVTA----MTGIKEIGKETLIGAGTV 190
Cdd:cd03353    90 egvhignfveiKKSTIGEGSKAnhlsYLGDAEIGEGVNIGAGTI 133
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 97-206 2.05e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.27  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468733855  97 TVSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINM-----DSTIAHHVTLEDGVFMSS----GVNIG--------ALI- 158
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPgsrivDSTIGDGVTITNSVIEESkvgdNVTVGpfahlrpgSVIg 338

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468733855 159 -NVR-------KNAYIGMG--VTAMT--GIKEIGKETLIGAGTVIIK--DVPEYTTVVGNPA 206
Cdd:PRK14354  339 eEVKignfveiKKSTIGEGtkVSHLTyiGDAEVGENVNIGCGTITVNydGKNKFKTIIGDNA 400
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 140-202 7.17e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 36.32  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468733855 140 VTLEDGVFMSSGVNIGALINVRKNAYIGMGVTAMTGIKEIGKETligaGTVIIKDVPEYTTVV 202
Cdd:PRK11830  177 VIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRET----GEVHYGRVPAGSVVV 235
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 98-156 7.94e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.53  E-value: 7.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1468733855  98 VSIAPDVTIGEAVYMLAGNIVMPHTTIGNYIMINMDSTIAHHVTLEDGVFMSSGVNIGA 156
Cdd:COG1044   121 AVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGA 179
 
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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