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Conserved domains on  [gi|1172340666|ref|WP_080723940|]
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MULTISPECIES: serine acetyltransferase [Hafnia]

Protein Classification

serine acetyltransferase( domain architecture ID 10129656)

serine acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 100-195 3.31e-35

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: 119.85  E-value: 3.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVK 179
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90
                  ....*....|....*.
gi 1172340666 180 VGAMSFVNKDIPANGV 195
Cdd:cd03354    81 IGANAVVTKDVPANST 96
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 100-195 3.31e-35

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: 119.85  E-value: 3.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVK 179
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90
                  ....*....|....*.
gi 1172340666 180 VGAMSFVNKDIPANGV 195
Cdd:cd03354    81 IGANAVVTKDVPANST 96
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 68-193 1.71e-25

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: 97.08  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  68 LFWWRLASEMDKHGSKRhqkIASRICDKLKTRYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQD 147
Cdd:COG1045    35 LALHRLAHWLWKRGLPL---LARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGK 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1172340666 148 MPPNSIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPAN 193
Cdd:COG1045   112 EKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPG 157
PLN02357 PLN02357
serine acetyltransferase
 72-206 6.84e-18

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 80.70  E-value: 6.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  72 RLASEMDKHGSKrhqKIASRICDKLKTRYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPN 151
Cdd:PLN02357  200 RIAHKLWTQGRK---ILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGD 276

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1172340666 152 SIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPAngvyitRKTSVFTP 206
Cdd:PLN02357  277 RHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPP------RTTAVGNP 325
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 108-197 6.46e-14

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: 67.52  E-value: 6.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 108 AVIGPGLHMphHAGIVISKHARIGSNFIIRQNTTIG---AVQD---MPPNSII----KIGNNVDIGANCCLIGPITIGDN 177
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIVEhdcVIGDfvhIAPGVTLsggvVIGEGVFIGAGATIIQGVTIGAG 177

                          90       100
                  ....*....|....*....|
gi 1172340666 178 VKVGAMSFVNKDIPANGVYI 197
Cdd:TIGR03570 178 AIVGAGAVVTKDIPDGGVVV 197
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
154-199 1.54e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 37.80  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1172340666 154 IKIGNNVDIGANCCLigPITIGDNVKVGAmsfvnkdipanGVYITR 199
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGA-----------GVVITA 33
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 100-195 3.31e-35

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: 119.85  E-value: 3.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVK 179
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90
                  ....*....|....*.
gi 1172340666 180 VGAMSFVNKDIPANGV 195
Cdd:cd03354    81 IGANAVVTKDVPANST 96
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 68-193 1.71e-25

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: 97.08  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  68 LFWWRLASEMDKHGSKRhqkIASRICDKLKTRYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQD 147
Cdd:COG1045    35 LALHRLAHWLWKRGLPL---LARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGK 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1172340666 148 MPPNSIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPAN 193
Cdd:COG1045   112 EKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPG 157
PLN02357 PLN02357
serine acetyltransferase
 72-206 6.84e-18

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 80.70  E-value: 6.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  72 RLASEMDKHGSKrhqKIASRICDKLKTRYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPN 151
Cdd:PLN02357  200 RIAHKLWTQGRK---ILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGD 276

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1172340666 152 SIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPAngvyitRKTSVFTP 206
Cdd:PLN02357  277 RHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPP------RTTAVGNP 325
PRK10191 PRK10191
putative acyl transferase; Provisional
 100-203 1.03e-15

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 71.07  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGavqDMPPNSII--KIGNNVDIGANCCLIGPITIGDN 177
Cdd:PRK10191   40 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIG---NRGADNMAcpHIGNGVELGANVIILGDITIGNN 116

                          90       100
                  ....*....|....*....|....*.
gi 1172340666 178 VKVGAMSFVNKDIPANGVYITRKTSV 203
Cdd:PRK10191  117 VTVGAGSVVLDSVPDNALVVGEKARV 142
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
100-196 1.36e-15

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 70.28  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGA--VIGPGLHMPHHAGIVISKHARIGSNFIIRQNT--TIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIG 175
Cdd:COG0110    24 YGGNITIGDnvYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIG 103

                          90       100
                  ....*....|....*....|.
gi 1172340666 176 DNVKVGAMSFVNKDIPANGVY 196
Cdd:COG0110   104 DGAVVGAGSVVTKDVPPYAIV 124
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 109-196 6.65e-15

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: 67.87  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 109 VIGPGLHMPHHAGIVISKHARIGSNFII-----RQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVKVGAM 183
Cdd:cd04647     9 YIGPGCVISAGGGITIGDNVLIGPNVTIydhnhDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAG 88

                          90
                  ....*....|...
gi 1172340666 184 SFVNKDIPANGVY 196
Cdd:cd04647    89 SVVTKDVPPNSIV 101
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 108-197 3.64e-14

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: 67.89  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 108 AVIGPGLHMphHAGIVISKHARIGSNFIIRQNTTIG-----------AvqdmpPNSII----KIGNNVDIGANCCLIGPI 172
Cdd:cd03360    97 AVIGEGCVI--MAGAVINPDARIGDNVIINTGAVIGhdcvigdfvhiA-----PGVVLsggvTIGEGAFIGAGATIIQGV 169

                          90       100
                  ....*....|....*....|....*
gi 1172340666 173 TIGDNVKVGAMSFVNKDIPANGVYI 197
Cdd:cd03360   170 TIGAGAIIGAGAVVTKDVPDGSVVV 194
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 108-197 6.46e-14

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: 67.52  E-value: 6.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 108 AVIGPGLHMphHAGIVISKHARIGSNFIIRQNTTIG---AVQD---MPPNSII----KIGNNVDIGANCCLIGPITIGDN 177
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIVEhdcVIGDfvhIAPGVTLsggvVIGEGVFIGAGATIIQGVTIGAG 177

                          90       100
                  ....*....|....*....|
gi 1172340666 178 VKVGAMSFVNKDIPANGVYI 197
Cdd:TIGR03570 178 AIVGAGAVVTKDIPDGGVVV 197
PLN02694 PLN02694
serine O-acetyltransferase
 90-206 8.74e-14

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 68.52  E-value: 8.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  90 SRICDKlktrYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLI 169
Cdd:PLN02694  153 SRISDV----FAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATIL 228

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1172340666 170 GPITIGDNVKVGAMSFVNKDIPAngvyitRKTSVFTP 206
Cdd:PLN02694  229 GNVKIGEGAKIGAGSVVLIDVPP------RTTAVGNP 259
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 107-196 2.79e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.39  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 107 GAVIG---------PGLH--MPHHAGIVISKHARIGSNfiirqnTTI--GAVQDmppnSIIK----------IGNNVDIG 163
Cdd:PRK00892  178 GAVIGsdgfgfandRGGWvkIPQLGRVIIGDDVEIGAN------TTIdrGALDD----TVIGegvkidnlvqIAHNVVIG 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1172340666 164 ANC-----------------CLIGP-------ITIGDNVKVGAMSFVNKDIPANGVY 196
Cdd:PRK00892  248 RHTaiaaqvgiagstkigryCMIGGqvgiaghLEIGDGVTITAMSGVTKSIPEPGEY 304
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 102-196 3.33e-12

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: 64.27  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 102 ADVELGA--VIGPGLH-MPH---------HAGIVISKHARIGSNFIIRQNTTIGA-----VQDmPPNSIIK--------I 156
Cdd:COG1044   125 AGVVIGDgvVIGPGVViGDGvvigddcvlHPNVTIYERCVIGDRVIIHSGAVIGAdgfgfAPD-EDGGWVKipqlgrvvI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 157 GNNVDIGANCC----------------------------------------------------------LIGPITIGDNV 178
Cdd:COG1044   204 GDDVEIGANTTidrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgiagstkigdnvviggqvgIAGHLTIGDGV 283

                         170
                  ....*....|....*...
gi 1172340666 179 KVGAMSFVNKDIPANGVY 196
Cdd:COG1044   284 IIGAQSGVTKSIPEGGVY 301
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 101-199 2.83e-11

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: 60.13  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 101 AADVELGAVIGPGLHMPHHAgiVISKHARIGsNFI-----------------------IRQNTTIGAvqdmppNSII--- 154
Cdd:cd03353    67 GAVIGNGATVGPFAHLRPGT--VLGEGVHIG-NFVeikkstigegskanhlsylgdaeIGEGVNIGA------GTITcny 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1172340666 155 --------KIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:cd03353   138 dgvnkhrtVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIAR 190
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 108-187 3.18e-11

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: 57.26  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 108 AVIGPGLHMPHHAgiVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVN 187
Cdd:cd00208     1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 154-195 3.56e-11

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: 59.36  E-value: 3.56e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1172340666 154 IKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGV 195
Cdd:cd03357   119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 102-196 7.64e-11

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 58.96  E-value: 7.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 102 ADVELG--AVIGPGLHMPH----------HAGIVISKHARIGSNFIIRQNTTIGA-----------VQDMPPNSIIKIGN 158
Cdd:cd03352    18 EGVVIGdgVVIGPGVVIGDgvvigddcviHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgfapdgggWVKIPQLGGVIIGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 159 NVDIGANCC----------------------------------------------------------LIGPITIGDNVKV 180
Cdd:cd03352    98 DVEIGANTTidrgalgdtvigdgtkidnlvqiahnvrigencliaaqvgiagsttigdnviiggqvgIAGHLTIGDGVVI 177

                         170
                  ....*....|....*.
gi 1172340666 181 GAMSFVNKDIPANGVY 196
Cdd:cd03352   178 GAGSGVTSIVPPGEYV 193
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-199 2.61e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 58.79  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAgiVISKHARIGsNFIIRQNTTIGAVQDMPPNSII------------------------- 154
Cdd:PRK14360  312 SDSQIGDGVKIGPYAHLRPEA--QIGSNCRIG-NFVEIKKSQLGEGSKVNHLSYIgdatlgeqvnigagtitanydgvkk 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1172340666 155 ---KIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14360  389 hrtVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIAR 436
PLN02739 PLN02739
serine acetyltransferase
 71-195 5.69e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 57.74  E-value: 5.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  71 WRLASEMDKHGSKRhqkIASRICDKLKTRYAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQDMPP 150
Cdd:PLN02739  178 YRVAHKLWKQGRKL---LALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETG 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1172340666 151 NSIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGV 195
Cdd:PLN02739  255 DRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSM 299
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 155-199 1.01e-08

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: 54.26  E-value: 1.01e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1172340666 155 KIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:COG1207   396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIAR 440
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 155-199 3.25e-08

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 52.69  E-value: 3.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1172340666 155 KIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14359  369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISR 413
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 110-195 1.41e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 50.00  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 110 IGPGLHMPHHAGIVISKHARIGSNFIIRQNTTI--------------GAVQDMPpnsiIKIGNNVDIGANCCLIGPITIG 175
Cdd:PRK09527   78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLsvtghpvhhelrknGEMYSFP----ITIGNNVWIGSHVVINPGVTIG 153

                          90       100
                  ....*....|....*....|
gi 1172340666 176 DNVKVGAMSFVNKDIPANGV 195
Cdd:PRK09527  154 DNSVIGAGSVVTKDIPPNVV 173
cysE PRK11132
serine acetyltransferase; Provisional
 100-192 3.75e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 49.31  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVIGPGLHMPHHAGIVISKHARIGSNFIIRQNTTIGAVQ----DMPPnsiiKIGNNVDIGANCCLIGPITIG 175
Cdd:PRK11132  140 FQVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGTGktsgDRHP----KIREGVMIGAGAKILGNIEVG 215

                          90
                  ....*....|....*..
gi 1172340666 176 DNVKVGAMSFVNKDIPA 192
Cdd:PRK11132  216 RGAKIGAGSVVLQPVPP 232
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-199 4.35e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 49.34  E-value: 4.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1172340666 156 IGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIAR 444
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-180 5.46e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.98  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  88 IASRICDKLKTR-YAADVELGAVIGPGLHMPHHAGI----VISKHARIGSNFIIRQNTTIGavqdmpPNSiiKIGNNVDI 162
Cdd:PRK00892   86 RLAQLFDPPATPsPAAGIHPSAVIDPSAKIGEGVSIgpnaVIGAGVVIGDGVVIGAGAVIG------DGV--KIGADCRL 157

                          90
                  ....*....|....*...
gi 1172340666 163 GANCCLIGPITIGDNVKV 180
Cdd:PRK00892  158 HANVTIYHAVRIGNRVII 175
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 110-197 6.88e-07

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 46.34  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 110 IGPGLHMPHhaGIVISKHARIGSNFIIRQNTTIG--------AV--QDMPPNSII---------KIGNNVDIGANCCLIG 170
Cdd:cd03358     7 IGTNVFIEN--DVKIGDNVKIQSNVSIYEGVTIEddvfigpnVVftNDLYPRSKIyrkwelkgtTVKRGASIGANATILP 84

                          90       100
                  ....*....|....*....|....*..
gi 1172340666 171 PITIGDNVKVGAMSFVNKDIPANGVYI 197
Cdd:cd03358    85 GVTIGEYALVGAGAVVTKDVPPYALVV 111
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-200 2.51e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 47.33  E-value: 2.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1172340666 156 IGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITRK 200
Cdd:PRK09451  397 IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRV 441
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-199 3.12e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.75  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 102 ADVELGAVIGPGLHM-PhhaGIVISKHARIGsNFIIRQNTTIGAVQDMPPNSII-------------------------- 154
Cdd:PRK14354  317 SKVGDNVTVGPFAHLrP---GSVIGEEVKIG-NFVEIKKSTIGEGTKVSHLTYIgdaevgenvnigcgtitvnydgknkf 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1172340666 155 --KIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14354  393 ktIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIAR 439
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 130-197 7.23e-06

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: 43.36  E-value: 7.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172340666 130 IGSNFIIRQNTTIGA------VQDMP-PNSIIKIGNNVDIGANCcLIGP-ITIGDNVKVGAMSFVNKDIPANGVYI 197
Cdd:cd05825    26 IGSDACISQGAYLCTgshdyrSPAFPlITAPIVIGDGAWVAAEA-FVGPgVTIGEGAVVGARSVVVRDLPAWTVYA 100
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 104-204 1.13e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 43.52  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 104 VELGAVIGPGLHMPHHAgiVISKHARIGSNFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCcligpiTIGDNVKVGAM 183
Cdd:cd03350    28 VNIGAYVDEGTMVDSWA--TVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANC------EVVEGVIVGKG 99

                          90       100
                  ....*....|....*....|.
gi 1172340666 184 SFVnkdipANGVYITRKTSVF 204
Cdd:cd03350   100 AVL-----AAGVVLTQSTPIY 115
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 154-195 1.45e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 44.03  E-value: 1.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1172340666 154 IKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGV 195
Cdd:PRK10092  130 VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-199 3.43e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.70  E-value: 3.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1172340666 156 IGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14353  383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGR 426
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 119-182 4.29e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.20  E-value: 4.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172340666 119 HAGIVISKHARIGSNFIIRQNTTIGAvqdmppNSIIkiGNNVDIGANCcligpiTIGDNVKVGA 182
Cdd:PRK00892  104 HPSAVIDPSAKIGEGVSIGPNAVIGA------GVVI--GDGVVIGAGA------VIGDGVKIGA 153
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 154-209 4.66e-05

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 42.56  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1172340666 154 IKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITRKTSVFTPYDV 209
Cdd:PRK09677  131 VVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNH 186
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 107-199 5.30e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.43  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 107 GAVIGPGLHMphhAGIVISKHARIGS-----NFIIRQNTTIGAVQDMPPNSII-----------KIGNNVDIGANCCLIG 170
Cdd:PRK14358  340 GTVLGEGVHI---GNFVETKNARLDAgvkagHLAYLGDVTIGAETNVGAGTIVanfdgvnkhqsKVGAGVFIGSNTTLIA 416

                          90       100
                  ....*....|....*....|....*....
gi 1172340666 171 PITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14358  417 PRVVGDAAFIAAGSAVHDDVPEGAMAVAR 445
PRK10502 PRK10502
putative acyl transferase; Provisional
 154-197 7.28e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.86  E-value: 7.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1172340666 154 IKIGNNVDIGANCcLIGP-ITIGDNVKVGAMSFVNKDIPANGVYI 197
Cdd:PRK10502  125 IVIGEGCWLAADV-FVAPgVTIGSGAVVGARSSVFKSLPANTICR 168
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-203 7.95e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.81  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 108 AVIGPGLHMphHAGIVISKHARIGsNFIIRQNTTIGAVQDMPPNSII---KIGNNVDIG--------------------- 163
Cdd:PRK14355  327 VAIGPMAHL--RPGTELSAHVKIG-NFVETKKIVMGEGSKASHLTYLgdaTIGRNVNIGcgtitcnydgvkkhrtviedd 403

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1172340666 164 ----ANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITRKTSV 203
Cdd:PRK14355  404 vfvgSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQV 447
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 133-192 8.53e-05

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: 40.99  E-value: 8.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 133 NFIIRQNTTIGAVQDMPPNSIIKIGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPA 192
Cdd:cd03349    53 YIFGGEWEDDAKFDDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPP 112
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
154-199 1.54e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 37.80  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1172340666 154 IKIGNNVDIGANCCLigPITIGDNVKVGAmsfvnkdipanGVYITR 199
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGA-----------GVVITA 33
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 132-197 1.81e-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: 40.87  E-value: 1.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172340666 132 SNFIIRQNTTIGavQDM--PPNSIIK----IGNNVDIGANCcLIGPITIGDNVKVGAMSFVNKDIPANGVYI 197
Cdd:cd03353     8 ETTYIDGDVEIG--VDVviDPGVILEgktvIGEDCVIGPNC-VIKDSTIGDGVVIKASSVIEGAVIGNGATV 76
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 108-182 2.04e-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: 38.76  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172340666 108 AVIGPGLHmphhagivISKHARIgSNFIIRQNTTIGAvqdmppNSIIK---IGNNVDIGANCCLIGPITIGDNVKVGA 182
Cdd:cd03356    17 SVIGDNVR--------IGDGVTI-TNSILMDNVTIGA------NSVIVdsiIGDNAVIGENVRVVNLCIIGDDVVVED 79
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 154-181 2.13e-04

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: 40.48  E-value: 2.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1172340666 154 IKIGNNVDIGANCCL--IGPITIGDNVKVG 181
Cdd:cd03357    63 IHIGDNFYANFNCTIldVAPVTIGDNVLIG 92
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
154-182 2.38e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*....
gi 1172340666 154 IKIGNNVDIGANCCLIGPITIGDNVKVGA 182
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 119-186 2.82e-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: 39.92  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172340666 119 HAGIVISKHARI----GSNFIIRQNTTI--GAVQDMPPNSIIKIGNNVDIgANCCLI-GPITIGDNVKVGAMSFV 186
Cdd:cd00710    24 GDNVFVGPGASIradeGTPIIIGANVNIqdGVVIHALEGYSVWIGKNVSI-AHGAIVhGPAYIGDNCFIGFRSVV 97
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 101-209 3.07e-04

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: 40.49  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 101 AADVELGAVIGPG-LHMPhhaGIV-ISkhARIGSNFIIRQNTTIGA-VQdmppnsiikIGNNVDIGANCcLIG------- 170
Cdd:COG2171   103 GARVRLGAYLAPGvVLMP---SFVnIG--AYVDEGTMVDTWATVGScAQ---------IGKNVHLSGGA-GIGgvleplq 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1172340666 171 --PITIGDNVKVGAMS------FVNKD--IPAnGVYITRKTSVftpYDV 209
Cdd:COG2171   168 aaPVIIEDNCFIGARSgvvegvIVGEGavLGA-GVYLTASTKI---YDR 212
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-199 3.13e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.90  E-value: 3.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1172340666 156 IGNNVDIGANCCLIGPITIGDNVKVGAMSFVNKDIPANGVYITR 199
Cdd:PRK14357  386 IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGR 429
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-192 4.25e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.31  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666  98 TRYAADVELG-------AVIGPGLHMPH--HAG-IVISKHARIGSnfiirqnTTIGAVQDMPPNSIIKIGNNVDIGANCC 167
Cdd:PRK14352  341 TVLGEEGKLGafvetknATIGRGTKVPHltYVGdADIGEHSNIGA-------SSVFVNYDGVNKHRTTIGSHVRTGSDTM 413

                          90       100
                  ....*....|....*....|....*
gi 1172340666 168 LIGPITIGDNVKVGAMSFVNKDIPA 192
Cdd:PRK14352  414 FVAPVTVGDGAYTGAGTVIREDVPP 438
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 122-196 6.76e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.85  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 122 IVISKHARIGSNFIIR---QNTTIGA---VQDmppNSII--------KIGNNVDIGANC----------CLIGP--I--- 172
Cdd:COG0663    29 VTIGEDVSVWPGAVLRgdvGPIRIGEgsnIQD---GVVLhvdpgyplTIGDDVTIGHGAilhgctigdnVLIGMgaIvld 105

                          90       100
                  ....*....|....*....|....*...
gi 1172340666 173 --TIGDNVKVGAMSFV--NKDIPANGVY 196
Cdd:COG0663   106 gaVIGDGSIVGAGALVteGKVVPPGSLV 133
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-186 1.73e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 102 ADVELGA--VIGPGLHMPHHAGI----VISKHAR-----IGSNFIIRQ----------NTTIGAVQDMPPNSiiKIGNNV 160
Cdd:PRK14354  264 ADVEIGSdtVIEPGVVIKGNTVIgedcVIGPGSRivdstIGDGVTITNsvieeskvgdNVTVGPFAHLRPGS--VIGEEV 341

                          90       100
                  ....*....|....*....|....*.
gi 1172340666 161 DIGaNCCLIGPITIGDNVKVGAMSFV 186
Cdd:PRK14354  342 KIG-NFVEIKKSTIGEGTKVSHLTYI 366
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 123-181 1.74e-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: 38.08  E-value: 1.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172340666 123 VISKHARIGSNfiirqnTTIGavqdmpPNSII----KIGNNVDIGANCCLIGPITIGDNVKVG 181
Cdd:COG1043     9 IVDPGAKLGEN------VEIG------PFCVIgpdvEIGDGTVIGSHVVIEGPTTIGKNNRIF 59
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 129-197 1.95e-03

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: 37.39  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 129 RIGSNFIIRQNTTIGAVQDMPpnsiIKIGNNVDIGANC----------CLIGP-------ITIGDNVKVGAMSFV--NKD 189
Cdd:cd04645    40 RIGERTNIQDGSVLHVDPGYP----TIIGDNVTVGHGAvlhgctigdnCLIGMgaiildgAVIGKGSIVAAGSLVppGKV 115


                  ....*...
gi 1172340666 190 IPANGVYI 197
Cdd:cd04645   116 IPPGSLVA 123
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 100-186 2.98e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 100 YAADVELGAVI-GPGL--HMPHHAGIVISKH-----ARIGSNFIirQNTTIGAVQDMPPNSII----KIGNNVDIGANCC 167
Cdd:PRK00892   49 QLATTKAGAVIvSPDDaeFVPAGNALLVVKNpylafARLAQLFD--PPATPSPAAGIHPSAVIdpsaKIGEGVSIGPNAV 126

                          90       100
                  ....*....|....*....|
gi 1172340666 168 lIGP-ITIGDNVKVGAMSFV 186
Cdd:PRK00892  127 -IGAgVVIGDGVVIGAGAVI 145
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 122-195 4.44e-03

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: 36.39  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 122 IVISKHARIGSNFIIRQN----TTIGAVQDMPPNSII---KIGNNVDIGANCCLIGPITIGDNVKVGAMSFV--NKDIPA 192
Cdd:cd04650    40 IYIGKYSNVQENVSIHTDhgypTEIGDYVTIGHNAVVhgaKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVtpGKEIPD 119


                  ...
gi 1172340666 193 NGV 195
Cdd:cd04650   120 YSL 122
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
123-180 5.97e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.61  E-value: 5.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172340666 123 VISKHARIGSNFIIRQNTTIGavqdmpPNsiIKIGNNVDIGANCCLIGPITIGDNVKV 180
Cdd:PRK05289   10 IVEPGAKIGENVEIGPFCVIG------PN--VVIGDGTVIGSHVVIDGHTTIGKNNRI 59
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 129-180 6.37e-03

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: 36.04  E-value: 6.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1172340666 129 RIGSNFIIRQNTTIGAVQdmppnsiikIGNNVDIGANCCLIGPITIGDNVKV 180
Cdd:cd03359    74 HIGDYVFIGENCVVNAAQ---------IGSYVHIGKNCVIGRRCIIKDCVKI 116
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 129-191 6.77e-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: 36.64  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 129 RIGSNFIIRQNTTI--GAVQDmppNSIIKIGNNVDIGANC-----CLIGP-------------ITIGDNVK--------- 179
Cdd:cd03351    79 EIGDNNTIREFVTIhrGTAQG---GGVTRIGNNNLLMAYVhvahdCVIGNnvilannatlaghVEIGDYAIigglsavhq 155

                          90       100
                  ....*....|....*....|.
gi 1172340666 180 ---------VGAMSFVNKDIP 191
Cdd:cd03351   156 fcrigrhamVGGGSGVVQDVP 176
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 102-191 6.78e-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: 36.53  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172340666 102 ADVELGA--VIGPglhmphHAgiVISKHARIGSNFIIRQNTTIGAV-QDM-----PP------NSII------------- 154
Cdd:COG1043    30 PDVEIGDgtVIGS------HV--VIEGPTTIGKNNRIFPFASIGEEpQDLkykgePTrleigdNNTIrefvtihrgtvqg 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172340666 155 ----------------------KIGNNVDIGANCCLIGPITIGDN------------VKVGAMSF------VNKDIP 191
Cdd:COG1043   102 ggvtrigddnllmayvhvahdcVVGNNVILANNATLAGHVEVGDHaiigglsavhqfVRIGAHAMvgggsgVVKDVP 178
 
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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