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Conserved domains on  [gi|184193521|gb|ACC71486|]
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transferase hexapeptide repeat containing protein [Paraburkholderia phymatum STM815]

Protein Classification

acetyltransferase( domain architecture ID 10129737)

acetyltransferase similar to Escherichia coli GDP-perosamine N-acetyltransferase that catalyzes the transfer of an acetyl residue from acetyl-CoA onto GDP-perosamine to form GDP-N-acetyl-perosamine; belongs to the transferase hexapeptide repeat family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 9-207 6.25e-66

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: 201.94  E-value: 6.25e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521   9 ILGDSAFAEVAYECFTHDSDYEVVGFSVDSAYLGRDQLFGLPVvPFEEIERFFDPAEVEFYAALVYsqlNRLRTRFFGLA 88
Cdd:cd03360    1 IIGAGGHARVVADILEADSGYEVVGFLDDDPELKGTEGLGLPV-GLDELLLLYPPPDDEFVVAIGD---NKLRRKLAEKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  89 KDKGYRPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGAN 168
Cdd:cd03360   77 LAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 184193521 169 TFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKG 207
Cdd:cd03360  157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVG 195
 
Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 9-207 6.25e-66

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: 201.94  E-value: 6.25e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521   9 ILGDSAFAEVAYECFTHDSDYEVVGFSVDSAYLGRDQLFGLPVvPFEEIERFFDPAEVEFYAALVYsqlNRLRTRFFGLA 88
Cdd:cd03360    1 IIGAGGHARVVADILEADSGYEVVGFLDDDPELKGTEGLGLPV-GLDELLLLYPPPDDEFVVAIGD---NKLRRKLAEKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  89 KDKGYRPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGAN 168
Cdd:cd03360   77 LAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 184193521 169 TFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKG 207
Cdd:cd03360  157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVG 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 6-207 3.80e-53

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: 169.60  E-value: 3.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521    6 KLVILGDSAFAEVAYECFtHDSDYEVVGFSVDSAYLGRDQLFGLPVVPFEEIERFFDPAEVEFYAALVYsqlNRLRTRFF 85
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADIL-ERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGD---NKLRRRLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521   86 GLAKDKGYRPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTI 165
Cdd:TIGR03570  77 EKLKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 184193521  166 GANTFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKG 207
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 102-193 6.68e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 66.97  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 102 RAFVWPNAV---------IGEHCFIfEDNTV------QPfVKIGNNVvlwsgnHIGHHS-----TIEDNCFISSHAVISG 161
Cdd:COG0663   34 DVSVWPGAVlrgdvgpirIGEGSNI-QDGVVlhvdpgYP-LTIGDDV------TIGHGAilhgcTIGDNVLIGMGAIVLD 105

                         90       100       110
                 ....*....|....*....|....*....|..
gi 184193521 162 FCTIGANTFIGVNSAIANNVVIgADNWLGVGV 193
Cdd:COG0663  106 GAVIGDGSIVGAGALVTEGKVV-PPGSLVVGS 136
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-186 7.43e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 66.32  E-value: 7.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  87 LAKDKGYRPASYVSSRAFVWPNAVIGEHCfifednTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIG 166
Cdd:PRK00892  91 FDPPATPSPAAGIHPSAVIDPSAKIGEGV------SIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIY 164

                         90       100
                 ....*....|....*....|
gi 184193521 167 ANTFIGVNSAIANNVVIGAD 186
Cdd:PRK00892 165 HAVRIGNRVIIHSGAVIGSD 184
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
144-172 2.85e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 2.85e-04
                          10        20
                  ....*....|....*....|....*....
gi 184193521  144 HSTIEDNCFISSHAVISGFCTIGANTFIG 172
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 9-207 6.25e-66

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: 201.94  E-value: 6.25e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521   9 ILGDSAFAEVAYECFTHDSDYEVVGFSVDSAYLGRDQLFGLPVvPFEEIERFFDPAEVEFYAALVYsqlNRLRTRFFGLA 88
Cdd:cd03360    1 IIGAGGHARVVADILEADSGYEVVGFLDDDPELKGTEGLGLPV-GLDELLLLYPPPDDEFVVAIGD---NKLRRKLAEKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  89 KDKGYRPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGAN 168
Cdd:cd03360   77 LAAGYRFATLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 184193521 169 TFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKG 207
Cdd:cd03360  157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVG 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 6-207 3.80e-53

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: 169.60  E-value: 3.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521    6 KLVILGDSAFAEVAYECFtHDSDYEVVGFSVDSAYLGRDQLFGLPVVPFEEIERFFDPAEVEFYAALVYsqlNRLRTRFF 85
Cdd:TIGR03570   1 KLVIIGAGGHGRVVADIL-ERSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGD---NKLRRRLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521   86 GLAKDKGYRPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTI 165
Cdd:TIGR03570  77 EKLKAKGYRFATLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 184193521  166 GANTFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKG 207
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 102-193 6.68e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 66.97  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 102 RAFVWPNAV---------IGEHCFIfEDNTV------QPfVKIGNNVvlwsgnHIGHHS-----TIEDNCFISSHAVISG 161
Cdd:COG0663   34 DVSVWPGAVlrgdvgpirIGEGSNI-QDGVVlhvdpgYP-LTIGDDV------TIGHGAilhgcTIGDNVLIGMGAIVLD 105

                         90       100       110
                 ....*....|....*....|....*....|..
gi 184193521 162 FCTIGANTFIGVNSAIANNVVIgADNWLGVGV 193
Cdd:COG0663  106 GAVIGDGSIVGAGALVTEGKVV-PPGSLVVGS 136
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 90-186 9.26e-14

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: 68.89  E-value: 9.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  90 DKGYRPASYVSSRAFVWPNAVIGEHCfifednTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANT 169
Cdd:COG1044   90 YPPPAPAPGIHPSAVIDPSAKIGEGV------SIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC 163

                         90
                 ....*....|....*..
gi 184193521 170 FIGVNSAIANNVVIGAD 186
Cdd:COG1044  164 VIGDRVIIHSGAVIGAD 180
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-186 7.43e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 66.32  E-value: 7.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  87 LAKDKGYRPASYVSSRAFVWPNAVIGEHCfifednTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIG 166
Cdd:PRK00892  91 FDPPATPSPAAGIHPSAVIDPSAKIGEGV------SIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIY 164

                         90       100
                 ....*....|....*....|
gi 184193521 167 ANTFIGVNSAIANNVVIGAD 186
Cdd:PRK00892 165 HAVRIGNRVIIHSGAVIGSD 184
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 97-178 2.06e-12

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: 60.73  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  97 SYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNvvlwSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSA 176
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAA----TGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76


                 ..
gi 184193521 177 IA 178
Cdd:cd00208   77 VT 78
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
102-186 1.14e-11

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 60.27  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 102 RAFVWPNAVIGEHCFIFEDNTVQPF-VKIGNNVVLWSGNHI--GHHSTIEDNCFISSHAVI----------------SGF 162
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGP 81

                         90       100
                 ....*....|....*....|....
gi 184193521 163 CTIGANTFIGVNSAIANNVVIGAD 186
Cdd:COG0110   82 VTIGDDVWIGAGATILPGVTIGDG 105
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 108-186 1.34e-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: 61.27  E-value: 1.34e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 184193521 108 NAVIGEHCFIfedntvQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGAD 186
Cdd:cd03352    1 SAKIGENVSI------GPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSD 73
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 111-185 4.73e-11

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: 57.90  E-value: 4.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 111 IGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAV---------------------ISGFCTIGANT 169
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVftndlyprskiyrkwelkgttVKRGASIGANA 80

                         90
                 ....*....|....*.
gi 184193521 170 FIGVNSAIANNVVIGA 185
Cdd:cd03358   81 TILPGVTIGEYALVGA 96
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 106-185 1.35e-10

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: 56.29  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 106 WPNAVIGEHCFIFEDNTV--QPFVKIGNNVVLWSGNHIGH--------HSTIEDNCFISSHAVISGFCTIGANTFIGVNS 175
Cdd:cd03354    6 HPGAKIGPGLFIDHGTGIviGETAVIGDNCTIYQGVTLGGkgkgggkrHPTIGDNVVIGAGAKILGNITIGDNVKIGANA 85

                         90
                 ....*....|....*
gi 184193521 176 AI-----ANNVVIGA 185
Cdd:cd03354   86 VVtkdvpANSTVVGV 100
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 102-193 1.94e-10

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 57.04  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 102 RAFVWPNAV---------IGEHCFIfEDNTV------QPfVKIGNNVVlwsgnhIGHHS-----TIEDNCFISSHAVISG 161
Cdd:cd04645   23 GSSVWFGAVlrgdvnpirIGERTNI-QDGSVlhvdpgYP-TIIGDNVT------VGHGAvlhgcTIGDNCLIGMGAIILD 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 184193521 162 FCTIGANTFIGVNSAIANNVVIgADNWLGVGV 193
Cdd:cd04645   95 GAVIGKGSIVAAGSLVPPGKVI-PPGSLVAGS 125
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 97-207 1.53e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 55.49  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  97 SYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGN------------------------------------- 139
Cdd:cd03352   26 VVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAvigsdgfgfapdgggwvkipqlggviigddveigant 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 140 ----------------------HIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILG 197
Cdd:cd03352  106 tidrgalgdtvigdgtkidnlvQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTS 185

                        170
                 ....*....|
gi 184193521 198 NTEPDCIFKG 207
Cdd:cd03352  186 IVPPGEYVSG 195
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 110-184 2.23e-09

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 55.73  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  110 VIGEHCFIFEDNTVQP-------FVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVV 182
Cdd:TIGR01852  78 IIGDNNTIREFVTINRgtasgggVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVR 157


                  ..
gi 184193521  183 IG 184
Cdd:TIGR01852 158 IG 159
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 98-185 2.56e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 56.30  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  98 YVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVI--SGF------------- 162
Cdd:PRK00892 120 SIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsDGFgfandrggwvkip 199

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 184193521 163 ----------CTIGAN----------TFIGVNS------AIANNVVIGA 185
Cdd:PRK00892 200 qlgrviigddVEIGANttidrgalddTVIGEGVkidnlvQIAHNVVIGR 248
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-207 3.04e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 54.72  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  95 PASYVSSRAFVWPNAVIGEHCFIFEDntvqpfVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVI--SGF---------- 162
Cdd:cd03352   12 PNAVIGEGVVIGDGVVIGPGVVIGDG------VVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsDGFgfapdgggwv 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 163 -------------CTIGANTFI--GVNSA--------------IANNVVIGADNWLGVGVNILGNT--EPDCIFKG 207
Cdd:cd03352   86 kipqlggviigddVEIGANTTIdrGALGDtvigdgtkidnlvqIAHNVRIGENCLIAAQVGIAGSTtiGDNVIIGG 161
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
97-181 4.84e-09

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 52.95  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  97 SYVSSRAFVWP-NAVIGEHCFIFEDNTVQPF--VKIGNNVVLWSGNHIGHHS----------------TIEDNCFISSHA 157
Cdd:COG0110   15 VVIGPGVRIYGgNITIGDNVYIGPGVTIDDPggITIGDNVLIGPGVTILTGNhpiddpatfplrtgpvTIGDDVWIGAGA 94

                         90       100
                 ....*....|....*....|....
gi 184193521 158 VISGFCTIGANTFIGVNSAIANNV 181
Cdd:COG0110   95 TILPGVTIGDGAVVGAGSVVTKDV 118
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 110-197 9.08e-09

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: 53.87  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 110 VIGEHCFIFEDNTVQP-------FVKIGNNVVLWSGNHIGHHSTIEDNCFIS------------SHAVISG------FCT 164
Cdd:COG1043   81 EIGDNNTIREFVTIHRgtvqgggVTRIGDDNLLMAYVHVAHDCVVGNNVILAnnatlaghvevgDHAIIGGlsavhqFVR 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 184193521 165 IGANTFIGVNSAIANNV---VIGADNWLGV-GVNILG 197
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVppyVLAAGNPARLrGLNLVG 197
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 99-190 9.33e-09

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: 52.76  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  99 VSSRAFVWPNAV------IGEHCFI---------FEDNTVQPFVKIGNNVVLWSGNhiGHHSTIEDNCFISSHAVISGfC 163
Cdd:cd04745    3 VDPSSFVHPTAVligdviIGKNCYIgphaslrgdFGRIVIRDGANVQDNCVIHGFP--GQDTVLEENGHIGHGAILHG-C 79

                         90       100
                 ....*....|....*....|....*..
gi 184193521 164 TIGANTFIGVNSAIANNVVIGADNWLG 190
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVG 106
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 103-186 1.04e-08

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: 54.25  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 103 AFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSG-------------------------------------------- 138
Cdd:COG1044  139 VVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGavigadgfgfapdedggwvkipqlgrvvigddveiganttidrg 218

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521 139 --------------N--HIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGAD 186
Cdd:COG1044  219 algdtvigdgtkidNlvQIAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDG 282
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 110-181 1.23e-08

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 53.59  E-value: 1.23e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 184193521 110 VIGEHCFIFE------DntvqpfVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNV 181
Cdd:cd03351  104 RIGNNNLLMAyvhvahD------CVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDV 175
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 99-187 2.15e-08

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 53.10  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  99 VSSRAFVWPNAVIGEHCfifednTVQPFVKIGNNVVlwsgnhighhstIEDNCFISSHAVISGFCTIGANTFIGVNSAIA 178
Cdd:COG1043    4 IHPTAIVDPGAKLGENV------EIGPFCVIGPDVE------------IGDGTVIGSHVVIEGPTTIGKNNRIFPFASIG 65

                         90       100
                 ....*....|....*....|.
gi 184193521 179 NN------------VVIGADN 187
Cdd:COG1043   66 EEpqdlkykgeptrLEIGDNN 86
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 140-204 2.21e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.22  E-value: 2.21e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 140 HIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNI-----LGNtepDCI 204
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIyhavrIGN---RVI 174
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 99-187 2.62e-08

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 52.82  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  99 VSSRAFVWPNAVIGEhcfifeDNTVQPFVKIGNNVVlwsgnhighhstIEDNCFISSHAVISGFCTIGANTFIGVNSAIA 178
Cdd:cd03351    2 IHPTAIVDPGAKIGE------NVEIGPFCVIGPNVE------------IGDGTVIGSHVVIDGPTTIGKNNRIFPFASIG 63

                         90       100
                 ....*....|....*....|.
gi 184193521 179 NN------------VVIGADN 187
Cdd:cd03351   64 EApqdlkykgeptrLEIGDNN 84
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 110-197 4.43e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 51.95  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 110 VIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNV----VIGA 185
Cdd:PRK12461 103 RIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVppycMMAG 182

                         90
                 ....*....|..
gi 184193521 186 DNWLGVGVNILG 197
Cdd:PRK12461 183 HPTNVHGLNAVG 194
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
103-205 8.28e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 51.25  E-value: 8.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 103 AFVWPNAVIGEhcfifeDNTVQPFVKIGNNVVLWSGNHIGHHSTIE------DNCFISSHAVISG------------FCT 164
Cdd:PRK05289   9 AIVEPGAKIGE------NVEIGPFCVIGPNVVIGDGTVIGSHVVIDghttigKNNRIFPFASIGEdpqdlkykgeptRLV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 184193521 165 IGANTFI--GVN----SAIANNV-VIGADNWLGVGVNI-----LGNtepDCIF 205
Cdd:PRK05289  83 IGDNNTIreFVTinrgTVQGGGVtRIGDNNLLMAYVHVahdcvVGN---HVIL 132
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 107-184 1.44e-07

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 47.57  E-value: 1.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 184193521 107 PNAVIGEHCFIfEDNTVQPFVKIGNNVVLwSGNHIGHHSTIEDNCFISsHAVISGFCTIGANTFIGVNSAIANNVVIG 184
Cdd:cd05787    4 RGTSIGEGTTI-KNSVIGRNCKIGKNVVI-DNSYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGVVIG 78
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
110-185 1.87e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 50.10  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 110 VIGEHCFIFEDNTVQP-------FVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVV 182
Cdd:PRK05289  82 VIGDNNTIREFVTINRgtvqgggVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVR 161


                 ...
gi 184193521 183 IGA 185
Cdd:PRK05289 162 IGA 164
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 146-204 2.70e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.33  E-value: 2.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 184193521 146 TIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE--PDCI 204
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIigDRVI 63
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 126-199 4.42e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.56  E-value: 4.42e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521 126 FVKIGNNVvlwsgnHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNT 199
Cdd:cd03352    1 SAKIGENV------SIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGA 68
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 125-184 1.14e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 47.41  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 184193521 125 PFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGfCTIGANTFIGVNSAI-----ANNVVIG 184
Cdd:cd03353   14 GDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKASSVIegaviGNGATVG 77
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 108-184 2.01e-06

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: 45.14  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 108 NAVIGEHCFIFEDNTVQPF--------VKIGNNVVLWSGNH----------IGHHS---TIEDNCFISSHAVISGFCTIG 166
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGggitigdnVLIGPNVTIYDHNHdiddperpieQGVTSapiVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|..
gi 184193521 167 ANTFIG----VNSAIANNVVIG 184
Cdd:cd04647   81 DGAVVGagsvVTKDVPPNSIVA 102
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 103-184 2.31e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.44  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 103 AFVWPNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSG-------------------------------------------- 138
Cdd:PRK00892 143 AVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGavigsdgfgfandrggwvkipqlgrviigddveiganttidrga 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 184193521 139 -------------N--HIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIG 184
Cdd:PRK00892 223 lddtvigegvkidNlvQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIG 283
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 107-184 4.42e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.49  E-value: 4.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 184193521 107 PNAVIGEHCFIFEDNTVQPFVKIGNNVVLwSGNHIGHHSTIEDNCFISShAVISGFCTIGANTFIGVNSAIANNVVIG 184
Cdd:cd03353   20 VDVVIDPGVILEGKTVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVIEG-AVIGNGATVGPFAHLRPGTVLGEGVHIG 95
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 110-207 5.59e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.78  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 110 VIGEHCFIFEDNTV------QPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVI 183
Cdd:PRK12461  79 EIGDRNVIREGVTIhrgtkgGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRI 158

                         90       100
                 ....*....|....*....|....
gi 184193521 184 GADNWLGVGVNILGNTEPDCIFKG 207
Cdd:PRK12461 159 GALAMMAGGSRISKDVPPYCMMAG 182
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 94-184 9.36e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 45.63  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  94 RPASYVSSRAFVwPNAVIGEHCFIfeDNTVQpfvkignNVVLWSGNHIGHHSTIEDnCFISSHAVISGFCTIgANTFIGV 173
Cdd:PRK05293 280 LPPQYIAENAKV-KNSLVVEGCVV--YGTVE-------HSVLFQGVQVGEGSVVKD-SVIMPGAKIGENVVI-ERAIIGE 347

                         90
                 ....*....|.
gi 184193521 174 NSAIANNVVIG 184
Cdd:PRK05293 348 NAVIGDGVIIG 358
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-225 1.61e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.85  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 103 AFVWPNAVIG-----------------EHCFIFEDNTVQPF------------VKIGN-----NVVLWSGNHIGHHSTIE 148
Cdd:PRK14353 275 VVIEPNVVFGpgvtvasgavihafshlEGAHVGEGAEVGPYarlrpgaelgegAKVGNfvevkNAKLGEGAKVNHLTYIG 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 149 DnCFISSHAVISG---FC----------TIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTEPDCIFKGEQPQAAKV 215
Cdd:PRK14353 355 D-ATIGAGANIGAgtiTCnydgfnkhrtEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433

                        170
                 ....*....|.
gi 184193521 216 S-ARRFFKVKA 225
Cdd:PRK14353 434 GwAKKLRERLR 444
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 97-205 1.78e-05

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: 43.77  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  97 SYVSSRAFVWPNAV------IGEHCFIFEDNTVQ-----PFVkIGNNVVLWSGNHIghHS------TIEDNCFISSHAVI 159
Cdd:cd00710    3 PVIDPSAYVHPTAVvigdviIGDNVFVGPGASIRadegtPII-IGANVNIQDGVVI--HAlegysvWIGKNVSIAHGAIV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 184193521 160 SGFCTIGANTFIGVNSaIANNVVIGADNWLGVGVNILGNTEPDCIF 205
Cdd:cd00710   80 HGPAYIGDNCFIGFRS-VVFNAKVGDNCVIGHNAVVDGVEIPPGRY 124
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 123-184 3.88e-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: 43.86  E-value: 3.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 123 VQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGfCTIGANTFI----GVNSAIANNVVIG 184
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVIkysvIEDAVVGAGATVG 327
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 111-187 5.31e-05

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: 42.20  E-value: 5.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 184193521 111 IGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISShAVISGFCTIGANTFIGVNSAIANNVVIgADN 187
Cdd:cd03359   45 IGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNA-AQIGSYVHIGKNCVIGRRCIIKDCVKI-LDG 119
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 147-193 5.75e-05

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: 41.33  E-value: 5.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 184193521 147 IEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGV 193
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNV 47
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 95-205 7.96e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.32  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  95 PASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFV------KIGNNVVLWSGNHIGH------------HSTIEDNCFISSH 156
Cdd:PRK12461  10 PSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAvilgptRIGKNNKIHQGAVVGDepqdftykgeesRLEIGDRNVIREG 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 157 AVIS------GFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE-PDCIF 205
Cdd:PRK12461  90 VTIHrgtkggGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTvGDRAI 145
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 94-159 9.29e-05

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: 41.43  E-value: 9.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521  94 RPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPfVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVI 159
Cdd:cd03359   58 RPPFKKFSKGVAFFPLHIGDYVFIGENCVVNA-AQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVV 122
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-184 1.25e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.13  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521 116 FIFEDNT-VQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGfCTIGANTFI----GVNSAIANNVVIG 184
Cdd:PRK14354 254 IIDPESTyIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVD-STIGDGVTItnsvIEESKVGDNVTVG 326
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 153-211 1.39e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 41.54  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 153 ISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE--PDC-IFK----GEQPQ 211
Cdd:COG1043    4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTigKNNrIFPfasiGEEPQ 69
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 153-211 1.81e-04

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: 41.26  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 153 ISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE--PDC-IFK----GEQPQ 211
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTigKNNrIFPfasiGEAPQ 67
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 127-199 2.39e-04

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: 38.38  E-value: 2.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 184193521 127 VKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISG--FCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNT 199
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGA 75
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
153-211 2.58e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.85  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 153 ISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE--PDC-IFK----GEQPQ 211
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTigKNNrIFPfasiGEDPQ 70
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 153-211 2.63e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.78  E-value: 2.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 153 ISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNT---EPDCIFK----GEQPQ 211
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTrigKNNKIHQgavvGDEPQ 67
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
144-172 2.85e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 2.85e-04
                          10        20
                  ....*....|....*....|....*....
gi 184193521  144 HSTIEDNCFISSHAVISGFCTIGANTFIG 172
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 107-184 4.02e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 107 PNAVIGEHCFIFEDNTVQPFVKIGNNVVLWSGNHIgHHSTIEDNCFISS----HAVISGFCTIGANTFIGVNSAIANNVV 182
Cdd:PRK14354 264 ADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-VDSTIGDGVTITNsvieESKVGDNVTVGPFAHLRPGSVIGEEVK 342


                 ..
gi 184193521 183 IG 184
Cdd:PRK14354 343 IG 344
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
127-155 4.32e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 4.32e-04
                          10        20
                  ....*....|....*....|....*....
gi 184193521  127 VKIGNNVVLWSGNHIGHHSTIEDNCFISS 155
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 147-195 4.78e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 4.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 184193521 147 IEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNI 195
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKI 151
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 123-186 5.03e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.01  E-value: 5.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521 123 VQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGfctigaNTFIGVNSAIANNVVIGAD 186
Cdd:PRK12461   8 IDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILG------PTRIGKNNKIHQGAVVGDE 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 108-197 5.98e-04

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: 40.40  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 108 NAVIGEHCfifednTVQPF------------VKIGN-----NVVLWSG---NH--------------IG----------- 142
Cdd:COG1207  317 DAVVGAGA------TVGPFarlrpgtvlgegVKIGNfvevkNSTIGEGskvNHlsyigdaeigegvnIGagtitcnydgv 390

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 184193521 143 --HHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNVvigADNWLGVG----VNILG 197
Cdd:COG1207  391 nkHRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDV---PAGALAIArarqRNIEG 448
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 141-185 8.28e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.22  E-value: 8.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 184193521 141 IGHHSTIEDNCFISsHAVISGFCTIGANTFIgVNSAIANNVVIGA 185
Cdd:cd03356    2 IGESTVIGENAIIK-NSVIGDNVRIGDGVTI-TNSILMDNVTIGA 44
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 105-168 8.85e-04

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 37.17  E-value: 8.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521 105 VWPNAVIGEHC-----FIFEDNTVQPFVKIgNNVVLWSGNHIGHHSTIEdNCFISSHAVISG-----FCTIGAN 168
Cdd:cd04652    2 VGENTQVGEKTsikrsVIGANCKIGKRVKI-TNCVIMDNVTIEDGCTLE-NCIIGNGAVIGEkcklkDCLVGSG 73
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 119-198 1.11e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 38.34  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 119 EDNTVQPFVKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGFCTIGANTFIGV-----NSAIANNVVIGADNWlgVGV 193
Cdd:cd05636   10 EGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNsvevkNSIIMDGTKVPHLNY--VGD 87


                 ....*
gi 184193521 194 NILGN 198
Cdd:cd05636   88 SVLGE 92
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 127-184 1.12e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 1.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 184193521 127 VKIGNNVVLWSGNHIGHHSTIEDNCFISSHAVISGfCTIGANTFIGV-----NSAIANNVVIG 184
Cdd:PRK14355 269 VVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAgsvleDSVVGDDVAIG 330
PRK10502 PRK10502
putative acyl transferase; Provisional
 77-181 1.41e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.39  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  77 LNRLRT---RFFGLAKDKGY--RPASYVssrAFVWpNAVIGEHCFIFED----NTVQpfVKIGNNVV------LWSGNH- 140
Cdd:PRK10502  39 LYRWRAfllRLFGAKIGKGVviRPSVRI---TYPW-KLTIGDYAWIGDDvwlyNLGE--ITIGAHCVisqksyLCTGSHd 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 184193521 141 --------IGHHSTIEDNCFISSHAVISGFCTIGANTFIGVNSAIANNV 181
Cdd:PRK10502 113 ysdphfdlNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSL 161
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
108-137 1.50e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 184193521  108 NAVIGEHCFIFEDNTVQPFVKIGNNVVLWS 137
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 94-195 1.58e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 37.95  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  94 RPASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIGN-----NVVLWSGNHIGHHSTIED-----NCFISSHAVISGF- 162
Cdd:cd05636   27 RSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNsvevkNSIIMDGTKVPHLNYVGDsvlgeNVNLGAGTITANLr 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 184193521 163 -----------------------CTIGANTFIGVNSAIANNVVIGADNWLGVGVNI 195
Cdd:cd05636  107 fddkpvkvrlkgervdtgrrklgAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 126-197 1.82e-03

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: 37.79  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 126 FVKIGNNVVLWSGNHI--GHHSTIEDNCFISSHAVISGFC--TIGANTFIGVNSAI------------------ANNVVI 183
Cdd:cd03357   42 FGSVGENVYIEPPFHCdyGYNIHIGDNFYANFNCTILDVApvTIGDNVLIGPNVQIytaghpldpeernrgleyAKPITI 121

                         90
                 ....*....|....
gi 184193521 184 GADNWLGVGVNILG 197
Cdd:cd03357  122 GDNVWIGGGVIILP 135
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 95-180 1.98e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.49  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  95 PASYVSSRAFVWPNAVIGEHCFIFEDNTVQPFVKIG---NNVVLWSGNHIGHHStiedncFIsSHAVISGFCTIGANTfi 171
Cdd:cd05635   22 PFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGgevEDSIIEGYSNKQHDG------FL-GHSYLGSWCNLGAGT-- 92


                 ....*....
gi 184193521 172 gVNSAIANN 180
Cdd:cd05635   93 -NNSDLKNN 100
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 107-185 2.00e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.07  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 107 PNAVIGEHCFIFedNTV-QPFVKIGNNVVLwSGNHIGHHSTIEDNCFISsHAVISGFCTIGANTFIGVNSAIANNVVIGA 185
Cdd:cd03356    4 ESTVIGENAIIK--NSViGDNVRIGDGVTI-TNSILMDNVTIGANSVIV-DSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 141-186 2.13e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.02  E-value: 2.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 184193521 141 IGHHSTIEDNCFISsHAVISGFCTIGANTFIgVNSAIANNVVIGAD 186
Cdd:cd05787    2 IGRGTSIGEGTTIK-NSVIGRNCKIGKNVVI-DNSYIWDDVTIEDG 45
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 107-187 2.25e-03

Dynactin 6 (or subunit p27): 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 p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the 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: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 37.30  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 107 PNAVIGEHCfIFEDNTVQPFVKIGNNvvlwsgNHIGHHSTIEDNCFISSHavisgfCTIGANTFIGVNSAIANNVVI-GA 185
Cdd:cd04646   65 KPMIIGSNN-VFEVGCKCEALKIGNN------NVFESKSFVGKNVIITDG------CIIGAGCKLPSSEILPENTVIyGA 131


                 ..
gi 184193521 186 DN 187
Cdd:cd04646  132 DC 133
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 111-181 2.39e-03

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: 36.43  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 111 IGEHCFIFED----NTVQpfVKIGNNVVLWSGNHI--GHHS-------------TIEDNCFISSHAVISGFCTIGANTFI 171
Cdd:cd05825    6 IGDNSWIGEGvwiyNLAP--VTIGSDACISQGAYLctGSHDyrspafplitapiVIGDGAWVAAEAFVGPGVTIGEGAVV 83

                         90
                 ....*....|
gi 184193521 172 GVNSAIANNV 181
Cdd:cd05825   84 GARSVVVRDL 93
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 95-218 2.86e-03

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: 36.97  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  95 PASYVSSRAFVWPNAV------------IGEHCFIFEDNTVQPFVKIGNNVvlwsgnHIGHHST--------------IE 148
Cdd:cd03350    6 PGAIIRDGAFIGPGAVlmmpsyvnigayVDEGTMVDSWATVGSCAQIGKNV------HLSAGAViggvleplqatpviIE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 149 DNCFisshavISGFCTIGANTFIGVNSAIANNVVIGADnwlgvgvNILGNTEPDCIFKGEQPQAAKVSAR 218
Cdd:cd03350   80 DDVF------IGANCEVVEGVIVGKGAVLAAGVVLTQS-------TPIYDRETGEIYYGRVPPGSVVVAG 136
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 153-200 2.92e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 2.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 184193521 153 ISSHAVISGFCTIGANTFIGVNSAIANNVVIGADNWLGVGVNILGNTE 200
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVK 150
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 104-153 5.62e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.15  E-value: 5.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 184193521 104 FVWPNAVIGEHCFIfEDNTVQPFVKIGNNVVLWSGNH----IGHHSTIEDNCFI 153
Cdd:PRK05293 327 VIMPGAKIGENVVI-ERAIIGENAVIGDGVIIGGGKEvitvIGENEVIGVGTVI 379
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 108-202 6.21e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 35.13  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 108 NAVIGEHCFIfEDNTVQpfvkignNVVLWSGNHIGHHSTIEDncfisshAVISGFCTIGANTFIgVNSAIANNVVIGAdn 187
Cdd:cd04651   12 NSLVSEGCII-SGGTVE-------NSVLFRGVRVGSGSVVED-------SVIMPNVGIGRNAVI-RRAIIDKNVVIPD-- 73

                         90
                 ....*....|....*
gi 184193521 188 wlgvGVNILGNTEPD 202
Cdd:cd04651   74 ----GVVIGGDPEED 84
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 55-198 6.40e-03

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: 36.21  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521  55 EEIERFF--DPA-----EV-----EFYAALVYsqlnRLRTRFFglaKDKGYRPASYVSSRAFVW------PNAVIGEHCF 116
Cdd:COG1045    7 EDIQAVFerDPAarsllEVllcypGFHALALH----RLAHWLW---KRGLPLLARLLSERARFLtgidihPGATIGRGFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 117 IfeDNtvqpfvkiGNNVVlwsgnhIGHHSTIEDNCFISsHAVisgfcTIGANTFIGVNSA--IANNVVIGAdnwlgvGVN 194
Cdd:COG1045   80 I--DH--------GTGVV------IGETAVIGDNVTIY-QGV-----TLGGTGKEKGKRHptIGDNVVIGA------GAK 131


                 ....
gi 184193521 195 ILGN 198
Cdd:COG1045  132 ILGP 135
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 6-68 6.61e-03

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: 34.46  E-value: 6.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 184193521    6 KLVILGDSAFAEVAYECFTHDSDYEVVGFsVDSAYlgRDQLFGLPVVP-FEEIERFFDPAEVEF 68
Cdd:pfam17836   1 KLIIIGAGGHGKVVADIIEAMGEYEIIGF-LDDNK--KTEVNGYPVLGgDIDLLASLSPDEYDV 61
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 107-185 7.80e-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: 36.24  E-value: 7.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184193521 107 PNAVIGEHcfifedntvqpfVKIGN-----NVVLWSG---NH--------------IG-------------HHSTIEDNC 151
Cdd:cd03353   84 PGTVLGEG------------VHIGNfveikKSTIGEGskaNHlsylgdaeigegvnIGagtitcnydgvnkHRTVIGDNV 151

                         90       100       110
                 ....*....|....*....|....*....|....
gi 184193521 152 FISSHAVISGFCTIGANTFIGVNSAIANNVVIGA 185
Cdd:cd03353  152 FIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGA 185
 
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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