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Conserved domains on  [gi|2098067313|gb|UBD12678|]
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NeuD/PglB/VioB family sugar acetyltransferase [Bacteroides thetaiotaomicron]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 286-546 6.79e-92

Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.


:

Pssm-ID: 405145 [Multi-domain]  Cd Length: 278  Bit Score: 282.69  E-value: 6.79e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 286 SLRHELTRQVNDPCEALVLKDKVrfseVFEDILGRRVMTFDE--------IKRQMHDPYSISINE-VVIKPIKGQAGQGI 356
Cdd:pfam14397   1 RRNTRYIRKYNPRALYPLVDDKL----KFKQLALRAGLPVPKlygvisigHDISRLDAFVRSLPPgFVIKPAKGSGGKGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 357 IFPMQ-------NFTSLRQLHDYVI----STVKKPDEYLYEERIIQHSALNKLNPSSLNTLRIVTYYDEsiNKVDVWSVV 425
Cdd:pfam14397  77 LVITRrgdqdyfKSSGCRILLDELKrhvsSLGGKPDVALVEERIVQDPVFAKLSPESVNTIRVITFLLD--NGVPVMPAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 426 LRIGIKAR-TDNFATGGIAVLVD-HRGVVCQPAIIKHPSGERFHIHPVSGEKITGCIIPYYDQAIALAKQAAMRIPKVRS 503
Cdd:pfam14397 155 LRLGTGASlVDNLHQGGVGVGIDlATGVLFKPALQAVQYGEPIEHHPDTGVKFRGFQIPNWDQILELAAECAQTLPGLGY 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2098067313 504 IGWDVAITET-GPYMLEGNDNWCMTLFQLPGGEGLRHLANSVCN 546
Cdd:pfam14397 235 VGWDIVIDENgGPLLLELNARPGLGIFQIANGEGLLPRLQNVEK 278
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 1-202 1.67e-61

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: 201.18  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313   1 MVIIGSKGCAKEILTALKwDNVEETVSLFDNINTDISDAYYDFPIIKSWNELEQHLKTDSKVIIGVGGGQRREVLARKIA 80
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILE-RSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  81 CLGGVLTTFISQKALVGgYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDR 160
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVS-PSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2098067313 161 TEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPA 202
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 286-546 6.79e-92

Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.


Pssm-ID: 405145 [Multi-domain]  Cd Length: 278  Bit Score: 282.69  E-value: 6.79e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 286 SLRHELTRQVNDPCEALVLKDKVrfseVFEDILGRRVMTFDE--------IKRQMHDPYSISINE-VVIKPIKGQAGQGI 356
Cdd:pfam14397   1 RRNTRYIRKYNPRALYPLVDDKL----KFKQLALRAGLPVPKlygvisigHDISRLDAFVRSLPPgFVIKPAKGSGGKGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 357 IFPMQ-------NFTSLRQLHDYVI----STVKKPDEYLYEERIIQHSALNKLNPSSLNTLRIVTYYDEsiNKVDVWSVV 425
Cdd:pfam14397  77 LVITRrgdqdyfKSSGCRILLDELKrhvsSLGGKPDVALVEERIVQDPVFAKLSPESVNTIRVITFLLD--NGVPVMPAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 426 LRIGIKAR-TDNFATGGIAVLVD-HRGVVCQPAIIKHPSGERFHIHPVSGEKITGCIIPYYDQAIALAKQAAMRIPKVRS 503
Cdd:pfam14397 155 LRLGTGASlVDNLHQGGVGVGIDlATGVLFKPALQAVQYGEPIEHHPDTGVKFRGFQIPNWDQILELAAECAQTLPGLGY 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2098067313 504 IGWDVAITET-GPYMLEGNDNWCMTLFQLPGGEGLRHLANSVCN 546
Cdd:pfam14397 235 VGWDIVIDENgGPLLLELNARPGLGIFQIANGEGLLPRLQNVEK 278
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 1-202 1.67e-61

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: 201.18  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313   1 MVIIGSKGCAKEILTALKwDNVEETVSLFDNINTDISDAYYDFPIIKSWNELEQHLKTDSKVIIGVGGGQRREVLARKIA 80
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILE-RSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  81 CLGGVLTTFISQKALVGgYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDR 160
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVS-PSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2098067313 161 TEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPA 202
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 3-201 9.70e-55

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: 183.07  E-value: 9.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313   3 IIGSKGCAKEILTALKWDNVEETVSLFDNiNTDISDAYYDFPIIKSWNELEQHLKTDSKVIIGVGGGQRREVLARKIACL 82
Cdd:cd03360     1 IIGAGGHARVVADILEADSGYEVVGFLDD-DPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLRRKLAEKLLAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  83 GGVLTTFISQKALVGgYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTE 162
Cdd:cd03360    80 GYRFATLIHPSAVVS-PSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAF 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2098067313 163 IGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVP 201
Cdd:cd03360   159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
99-205 1.49e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 102.26  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  99 YDNTIEPGVVILSGATIT-CNVSIGQGTFINKSTVIS--HDVRIGRYCEVSPGAKVL----------------GRAIIGD 159
Cdd:COG0110     7 FGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILtgnhpiddpatfplrtGPVTIGD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2098067313 160 RTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:COG0110    87 DVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVI 132
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 102-199 1.57e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 72.09  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGA-----------------KV--LGRAIIGDRTE 162
Cdd:PRK00892  132 VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAvigsdgfgfandrggwvKIpqLGRVIIGDDVE 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2098067313 163 IGANAVI----LPDVIVGADCK------IGAGAVVTRN--IDSHTTVAG 199
Cdd:PRK00892  212 IGANTTIdrgaLDDTVIGEGVKidnlvqIAHNVVIGRHtaIAAQVGIAG 260
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
155-183 1.30e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 2098067313 155 AIIGDRTEIGANAVILPDVIVGADCKIGA 183
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 286-546 6.79e-92

Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.


Pssm-ID: 405145 [Multi-domain]  Cd Length: 278  Bit Score: 282.69  E-value: 6.79e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 286 SLRHELTRQVNDPCEALVLKDKVrfseVFEDILGRRVMTFDE--------IKRQMHDPYSISINE-VVIKPIKGQAGQGI 356
Cdd:pfam14397   1 RRNTRYIRKYNPRALYPLVDDKL----KFKQLALRAGLPVPKlygvisigHDISRLDAFVRSLPPgFVIKPAKGSGGKGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 357 IFPMQ-------NFTSLRQLHDYVI----STVKKPDEYLYEERIIQHSALNKLNPSSLNTLRIVTYYDEsiNKVDVWSVV 425
Cdd:pfam14397  77 LVITRrgdqdyfKSSGCRILLDELKrhvsSLGGKPDVALVEERIVQDPVFAKLSPESVNTIRVITFLLD--NGVPVMPAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 426 LRIGIKAR-TDNFATGGIAVLVD-HRGVVCQPAIIKHPSGERFHIHPVSGEKITGCIIPYYDQAIALAKQAAMRIPKVRS 503
Cdd:pfam14397 155 LRLGTGASlVDNLHQGGVGVGIDlATGVLFKPALQAVQYGEPIEHHPDTGVKFRGFQIPNWDQILELAAECAQTLPGLGY 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2098067313 504 IGWDVAITET-GPYMLEGNDNWCMTLFQLPGGEGLRHLANSVCN 546
Cdd:pfam14397 235 VGWDIVIDENgGPLLLELNARPGLGIFQIANGEGLLPRLQNVEK 278
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 1-202 1.67e-61

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: 201.18  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313   1 MVIIGSKGCAKEILTALKwDNVEETVSLFDNINTDISDAYYDFPIIKSWNELEQHLKTDSKVIIGVGGGQRREVLARKIA 80
Cdd:TIGR03570   2 LVIIGAGGHGRVVADILE-RSGWEVVGFLDDNPALQGTEVDGLPVLGGDEDLLRYPPDEVDLVVAIGDNKLRRRLVEKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  81 CLGGVLTTFISQKALVGgYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDR 160
Cdd:TIGR03570  81 AKGYRFATLIHPSAIVS-PSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2098067313 161 TEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPA 202
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 3-201 9.70e-55

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: 183.07  E-value: 9.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313   3 IIGSKGCAKEILTALKWDNVEETVSLFDNiNTDISDAYYDFPIIKSWNELEQHLKTDSKVIIGVGGGQRREVLARKIACL 82
Cdd:cd03360     1 IIGAGGHARVVADILEADSGYEVVGFLDD-DPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLRRKLAEKLLAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  83 GGVLTTFISQKALVGgYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTE 162
Cdd:cd03360    80 GYRFATLIHPSAVVS-PSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAF 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2098067313 163 IGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVP 201
Cdd:cd03360   159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
99-205 1.49e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 102.26  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  99 YDNTIEPGVVILSGATIT-CNVSIGQGTFINKSTVIS--HDVRIGRYCEVSPGAKVL----------------GRAIIGD 159
Cdd:COG0110     7 FGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILtgnhpiddpatfplrtGPVTIGD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2098067313 160 RTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:COG0110    87 DVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVI 132
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 103-205 2.95e-20

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: 86.40  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTfinkstVISHDVRIGRYC----EVSPGAKV-----LGRAIIGDRTEIGANAVILPDV 173
Cdd:cd03358    13 IENDVKIGDNVKIQSNVSIYEGV------TIEDDVFIGPNVvftnDLYPRSKIyrkweLKGTTVKRGASIGANATILPGV 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2098067313 174 IVGADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd03358    87 TIGEYALVGAGAVVTKDVPPYALVVGNPARII 118
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 117-205 3.28e-19

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: 85.17  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 117 CNVSIGQGTFINKSTVISHD--VRIGRYCEVSPGAKVL-----------------GRAI-IGDRTEIGANAVILPDVIVG 176
Cdd:cd03357    61 YNIHIGDNFYANFNCTILDVapVTIGDNVLIGPNVQIYtaghpldpeernrgleyAKPItIGDNVWIGGGVIILPGVTIG 140

                          90       100
                  ....*....|....*....|....*....
gi 2098067313 177 ADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd03357   141 DNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 118-205 4.29e-19

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: 82.50  E-value: 4.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 118 NVSIGQGTFINKSTVIS--HDVRIGRYCEVSPGAKVL-------------------GRAIIGDRTEIGANAVILPDVIVG 176
Cdd:cd04647     1 NISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYdhnhdiddperpieqgvtsAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 2098067313 177 ADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 112-201 9.03e-19

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: 81.33  E-value: 9.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 112 GATITCNVSIGQGTFINKST--VISHDVRIGRYCEVSPG--------AKVLGRAIIGDRTEIGANAVILPDVIVGADCKI 181
Cdd:cd03354     2 GIDIHPGAKIGPGLFIDHGTgiVIGETAVIGDNCTIYQGvtlggkgkGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                          90       100
                  ....*....|....*....|
gi 2098067313 182 GAGAVVTRNIDSHTTVAGVP 201
Cdd:cd03354    82 GANAVVTKDVPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 112-210 6.98e-17

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: 78.59  E-value: 6.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 112 GATITCNVSI--GQGTFINKSTVISHDVRIgrYCEVSPGAKVLGRA----IIGDRTEIGANAVILPDVIVGADCKIGAGA 185
Cdd:COG1045    71 GATIGRGFFIdhGTGVVIGETAVIGDNVTI--YQGVTLGGTGKEKGkrhpTIGDNVVIGAGAKILGPITIGDNAKIGANS 148

                          90       100
                  ....*....|....*....|....*
gi 2098067313 186 VVTRNIDSHTTVAGVPARSITKSSN 210
Cdd:COG1045   149 VVLKDVPPGSTVVGVPARIVKRKGS 173
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 118-205 3.51e-15

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 72.58  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 118 NVSIGQGTFINKS-TVISHD-VRIGRYCEVSPGAKVL----------------------------------GRAIIGDRT 161
Cdd:cd03349     1 NISVGDYSYGSGPdCDVGGDkLSIGKFCSIAPGVKIGlggnhptdwvstypfyifggeweddakfddwpskGDVIIGNDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2098067313 162 EIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd03349    81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 87-203 1.62e-14

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: 70.90  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGyDNTIEPGVVILSGATI---TCNVSIGQGTFINKSTVI----SHDVRIGRYCEVSPGAkVLGRAIIGD 159
Cdd:cd04645     5 SAFIAPNATVIG-DVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGA-VLHGCTIGD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2098067313 160 RTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTTVAGVPAR 203
Cdd:cd04645    83 NCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAK 128
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 102-181 4.44e-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: 73.51  E-value: 4.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGA------------------KV--LGRAIIGDRT 161
Cdd:COG1044   128 VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAvigadgfgfapdedggwvKIpqLGRVVIGDDV 207

                          90       100
                  ....*....|....*....|....
gi 2098067313 162 EIGANAVI----LPDVIVGADCKI 181
Cdd:COG1044   208 EIGANTTIdrgaLGDTVIGDGTKI 231
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 103-187 1.14e-13

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 72.36  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTfinkstVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIG 182
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFA------VIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIH 172


                  ....*
gi 2098067313 183 AGAVV 187
Cdd:COG1044   173 SGAVI 177
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 102-205 1.31e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 68.90  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATI---TCNVSIGQGTFINKSTVI----SHDVRIGRYCEVSPGAKVLGrAIIGDRTEIGANAVILPDVI 174
Cdd:COG0663    30 TIGEDVSVWPGAVLrgdVGPIRIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLDGAV 108

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2098067313 175 VGADCKIGAGAVVTRN--IDSHTTVAGVPARSI 205
Cdd:COG0663   109 IGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVV 141
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 102-199 1.57e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 72.09  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGA-----------------KV--LGRAIIGDRTE 162
Cdd:PRK00892  132 VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAvigsdgfgfandrggwvKIpqLGRVIIGDDVE 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2098067313 163 IGANAVI----LPDVIVGADCK------IGAGAVVTRN--IDSHTTVAG 199
Cdd:PRK00892  212 IGANTTIdrgaLDDTVIGEGVKidnlvqIAHNVVIGRHtaIAAQVGIAG 260
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 96-181 3.32e-13

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: 68.59  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  96 VGGYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKV-------------------LGRAI 156
Cdd:cd03352    15 VIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVI 94

                          90       100
                  ....*....|....*....|....*....
gi 2098067313 157 IGDRTEIGANAVI----LPDVIVGADCKI 181
Cdd:cd03352    95 IGDDVEIGANTTIdrgaLGDTVIGDGTKI 123
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 100-189 3.72e-13

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: 68.59  E-value: 3.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 100 DNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVI-------LPD 172
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfAPD 80

                          90       100
                  ....*....|....*....|....*....
gi 2098067313 173 ------------VIVGADCKIGAGAVVTR 189
Cdd:cd03352    81 gggwvkipqlggVIIGDDVEIGANTTIDR 109
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 78-205 1.06e-12

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: 67.05  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  78 KIACLGGVlttfisqkalvggydnTIEPGVVILSGATITC----NVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLG 153
Cdd:cd03352    86 KIPQLGGV----------------IIGDDVEIGANTTIDRgalgDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAG 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098067313 154 RAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd03352   150 STTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPH 201
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 103-205 1.22e-12

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: 64.16  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITC--NVSIGQGTFInksTVISHDVRigrycevSPGAKVLGRAI-IGDRTEIGANAVILPDVIVGADC 179
Cdd:cd05825    12 IGEGVWIYNLAPVTIgsDACISQGAYL---CTGSHDYR-------SPAFPLITAPIvIGDGAWVAAEAFVGPGVTIGEGA 81

                          90       100
                  ....*....|....*....|....*.
gi 2098067313 180 KIGAGAVVTRNIDSHTTVAGVPARSI 205
Cdd:cd05825    82 VVGARSVVVRDLPAWTVYAGNPAVPV 107
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 103-187 2.03e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 68.63  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTfinkstVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIG 182
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNA------VIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIH 176


                  ....*
gi 2098067313 183 AGAVV 187
Cdd:PRK00892  177 SGAVI 181
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 125-187 1.68e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.46  E-value: 1.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098067313 125 TFINKSTVISHDVRIGRYCEVSPGAkVLG-RAIIGDRTEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:PRK00892  101 AGIHPSAVIDPSAKIGEGVSIGPNA-VIGaGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
cysE PRK11132
serine acetyltransferase; Provisional
 106-209 1.75e-10

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 62.02  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 106 GVVILSGATITCNVSIGQGT--FINKSTVISHDVRI---------GRYCevspgakvlgraiiGDR-------TEIGANA 167
Cdd:PRK11132  141 QVDIHPAAKIGRGIMLDHATgiVIGETAVIENDVSIlqsvtlggtGKTS--------------GDRhpkiregVMIGAGA 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2098067313 168 VILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSITKSS 209
Cdd:PRK11132  207 KILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPE 248
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 103-205 4.59e-10

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: 57.78  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLG--------RAIIGDRTEIGANAVILPDVI 174
Cdd:cd03350    16 IGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGvleplqatPVIIEDDVFIGANCEVVEGVI 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2098067313 175 VGADCKIGAGAVV---TRNIDSHTTVAG---VPARSI 205
Cdd:cd03350    96 VGKGAVLAAGVVLtqsTPIYDRETGEIYygrVPPGSV 132
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 156-207 5.25e-10

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 59.12  E-value: 5.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098067313 156 IIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSITK 207
Cdd:PRK09677  132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 93-207 6.06e-10

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 58.67  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  93 KALVGGYDN-TIEPgvvilsgaTITC----NVSIGQGTFINKSTVISH--DVRIGRYCEVSPGAKV-------------- 151
Cdd:PRK10092   51 ADLFGQVTEaYIEP--------TFRCdygyNIFLGNNFYANFDCVMLDvcPIRIGDNCMLAPGVHIytathpldpvarns 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 152 ---LGRAI-IGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSITK 207
Cdd:PRK10092  123 gaeLGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 107-188 1.06e-09

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: 54.95  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 107 VVILSGATITCNVSIGQGTFINKSTVISHDVRIGryceVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAV 186
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIG----AATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76


                  ..
gi 2098067313 187 VT 188
Cdd:cd00208    77 VT 78
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 87-178 1.55e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 59.65  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGgyDN-TIEPGVVIlsGAtitcNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKvlgraiIGDRTEIGA 165
Cdd:COG1044   102 SAVIDPSAKIG--EGvSIGPFAVI--GA----GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT------IYERCVIGD 167

                          90
                  ....*....|...
gi 2098067313 166 NAVILPDVIVGAD 178
Cdd:COG1044   168 RVIIHSGAVIGAD 180
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-191 2.25e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 59.49  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  88 TFISQKALVG-----GYDNTIEPGVVI-----LSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEV-----SPGAKV- 151
Cdd:PRK14353  269 TVIGRDVVIEpnvvfGPGVTVASGAVIhafshLEGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVknaklGEGAKVn 348

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2098067313 152 ----LGRAIIGD-------------------RTEIGANAVILPD------VIVGADCKIGAGAVVTRNI 191
Cdd:PRK14353  349 hltyIGDATIGAganigagtitcnydgfnkhRTEIGAGAFIGSNsalvapVTIGDGAYIASGSVITEDV 417
PRK10191 PRK10191
putative acyl transferase; Provisional
 106-203 3.72e-09

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 55.67  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 106 GVVILSGATITCNVSI--GQGTFINKSTV------ISHDVRIGrycevSPGAKVLGRAIIGDRTEIGANAVILPDVIVGA 177
Cdd:PRK10191   41 GYEIQAAATIGRRFTIhhGYAVVINKNVVagddftIRHGVTIG-----NRGADNMACPHIGNGVELGANVIILGDITIGN 115

                          90       100
                  ....*....|....*....|....*.
gi 2098067313 178 DCKIGAGAVVTRNIDSHTTVAGVPAR 203
Cdd:PRK10191  116 NVTVGAGSVVLDSVPDNALVVGEKAR 141
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 87-182 8.56e-09

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: 55.50  E-value: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISqKALVGGYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHdVRIGRYCevspgakVLGRAIIGDRTEIGAN 166
Cdd:cd03353     9 TTYID-GDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDG-VVIKASS-------VIEGAVIGNGATVGPF 79

                          90
                  ....*....|....*.
gi 2098067313 167 AVILPDVIVGADCKIG 182
Cdd:cd03353    80 AHLRPGTVLGEGVHIG 95
PRK10502 PRK10502
putative acyl transferase; Provisional
 106-203 1.84e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 54.19  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 106 GVVILSGATIT--CNVSIGQGTFINKSTVISH--DVRIGRYCEVSPGA--------------KVLGRAI-IGDRTEIGAN 166
Cdd:PRK10502   57 GVVIRPSVRITypWKLTIGDYAWIGDDVWLYNlgEITIGAHCVISQKSylctgshdysdphfDLNTAPIvIGEGCWLAAD 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2098067313 167 AVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPAR 203
Cdd:PRK10502  137 VFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 98-207 2.01e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 54.62  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  98 GYDNTIEPGVVILSGAtitcNVSIGQGTFINKSTVISHD--VRIGRYCEVSPGA--KVLGRAI----------------I 157
Cdd:PRK09527   59 GENAWVEPPVYFSYGS----NIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVtlSVTGHPVhhelrkngemysfpitI 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2098067313 158 GDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPARSITK 207
Cdd:PRK09527  135 GNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 90-205 2.97e-08

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: 53.37  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  90 ISQKALVGGYDNTIEPG-VVILSGATI---TCNVSIGQGTFINKSTVI-----------SH-DVRIGRYCEVSPGAKVLG 153
Cdd:cd03359    10 VSRKSVICGSQNIVLNGkTIIQSDVIIrgdLATVSIGRYCILSEGCVIrppfkkfskgvAFfPLHIGDYVFIGENCVVNA 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2098067313 154 rAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTTVAGVPARSI 205
Cdd:cd03359    90 -AQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFI 142
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 144-200 9.08e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 9.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 144 EVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTTV-AGV 200
Cdd:PRK00892  102 GIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGvkIGADCRLhANV 161
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 136-190 9.08e-08

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: 52.80  E-value: 9.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2098067313 136 DVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRN 190
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEG 55
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 102-188 9.77e-08

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: 51.82  E-value: 9.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEV------------------------------------ 145
Cdd:cd05636    25 IVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVknsiimdgtkvphlnyvgdsvlgenvnlgagtitan 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 146 -----------------SPGAKVLGrAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVT 188
Cdd:cd05636   105 lrfddkpvkvrlkgervDTGRRKLG-AIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-182 9.91e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.45  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGyDNTIEPGVVILSGATITCNVSIGQGTFINKSTvishdvrIGRYCEVSpgAKVLGRAIIGDRTEIGAN 166
Cdd:PRK14354  259 STYIDADVEIGS-DTVIEPGVVIKGNTVIGEDCVIGPGSRIVDST-------IGDGVTIT--NSVIEESKVGDNVTVGPF 328

                          90
                  ....*....|....*.
gi 2098067313 167 AVILPDVIVGADCKIG 182
Cdd:PRK14354  329 AHLRPGSVIGEEVKIG 344
PLN02694 PLN02694
serine O-acetyltransferase
 124-203 1.15e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 53.49  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 124 GTFINKSTVISHDVRIGRYCEVSPGAKVLG--RAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAGVP 201
Cdd:PLN02694  180 GVVIGETAVIGNNVSILHHVTLGGTGKACGdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNP 259


                  ..
gi 2098067313 202 AR 203
Cdd:PLN02694  260 AR 261
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 112-187 1.25e-07

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: 51.43  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 112 GATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGA-----NAVILP-----------DVIV 175
Cdd:cd05636    11 GVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNsvevkNSIIMDgtkvphlnyvgDSVL 90

                          90
                  ....*....|..
gi 2098067313 176 GADCKIGAGAVV 187
Cdd:cd05636    91 GENVNLGAGTIT 102
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 87-218 1.76e-07

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 50.83  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGyDNTIEPGVVILSGATITCN---VSIGQGTFINKSTVI----SHDVRIGRYCEVSPGAKVLGrAIIGD 159
Cdd:cd04745     6 SSFVHPTAVLIG-DVIIGKNCYIGPHASLRGDfgrIVIRDGANVQDNCVIhgfpGQDTVLEENGHIGHGAILHG-CTIGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098067313 160 RTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTTVAGVPARSITKSSNNAFKLKSK 218
Cdd:cd04745    84 NALVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSDEEVAWKTR 144
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 127-187 2.01e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 52.33  E-value: 2.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098067313 127 INKSTVISHDVRIGRYCEVSPGAKvlgraiIGDRTEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:COG1043    10 VDPGAKLGENVEIGPFCVIGPDVE------IGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
132-187 3.00e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.02  E-value: 3.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2098067313 132 VISHDVRIGRYCEVSPGAKvlgraiIGDRTEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:PRK05289   16 KIGENVEIGPFCVIGPNVV------IGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 137-198 3.11e-07

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: 48.01  E-value: 3.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2098067313 137 VRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVIL--------PDVIVGADCKIGAGAVVTRN--------IDSHTTVA 198
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIGANAVIHGGvkigdnavIGAGAVVT 78
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 127-187 3.42e-07

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: 51.66  E-value: 3.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098067313 127 INKSTVISHDVRIGRYCEVSPGAKvlgraiIGDRTEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:cd03351     8 VDPGAKIGENVEIGPFCVIGPNVE------IGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 95-203 4.03e-07

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: 51.28  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  95 LVGGYDNTIEPGVVI----LSGATITcnvSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVIL 170
Cdd:cd03351    78 LEIGDNNTIREFVTIhrgtAQGGGVT---RIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVH 154

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2098067313 171 PDVIVGADCKIGAGAVVTRNIDSHTTVAGVPAR 203
Cdd:cd03351   155 QFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRAR 187
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 94-203 6.08e-07

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: 50.72  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  94 ALVGGYDNTIEPGVVI----LSGATITcnvSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVI 169
Cdd:TIGR01852  76 RLIIGDNNTIREFVTInrgtASGGGVT---RIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAV 152

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2098067313 170 LPDVIVGADCKIGAGAVVTRNIDSHTTVAGVPAR 203
Cdd:TIGR01852 153 HQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRAR 186
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 103-183 6.67e-07

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: 47.24  E-value: 6.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATIT-----CNVSIGQGTFINKStVISHDVRIGRYCEVSpgakvlgRAIIGDRTEIGANAVILPDVIVGA 177
Cdd:cd03356     2 IGESTVIGENAIIKnsvigDNVRIGDGVTITNS-ILMDNVTIGANSVIV-------DSIIGDNAVIGENVRVVNLCIIGD 73


                  ....*.
gi 2098067313 178 DCKIGA 183
Cdd:cd03356    74 DVVVED 79
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 119-202 1.15e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 51.29  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 119 VSIGQGTFINKSTVISHD-VRIGRYCEVSPGAKV-----------LGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAV 186
Cdd:TIGR02353 598 VKIGRGVYIDGTDLTERDlVTIGDDSTLNEGSVIqthlfedrvmkSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677

                          90
                  ....*....|....*...
gi 2098067313 187 VTR--NIDSHTTVAGVPA 202
Cdd:TIGR02353 678 VMKgeEVPAHTRWRGNPA 695
PLN02357 PLN02357
serine acetyltransferase
 103-210 1.16e-06

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 50.65  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATI--TCNVSIGQGTFINKSTVISHDVRIGRYCEVSpGAKvlgRAIIGDRTEIGANAVILPDVIVGADCK 180
Cdd:PLN02357  229 IHPGAKIGQGILLdhATGVVIGETAVVGNNVSILHNVTLGGTGKQS-GDR---HPKIGDGVLIGAGTCILGNITIGEGAK 304

                          90       100       110
                  ....*....|....*....|....*....|
gi 2098067313 181 IGAGAVVTRNIDSHTTVAGVPARSITKSSN 210
Cdd:PLN02357  305 IGAGSVVLKDVPPRTTAVGNPARLIGGKEN 334
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
87-199 1.84e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 49.33  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGyDNTIEPGVVILSgatitcNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAkVLG------------- 153
Cdd:PRK05289    8 TAIVEPGAKIGE-NVEIGPFCVIGP------NVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFA-SIGedpqdlkykgept 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2098067313 154 RAIIGDR-------------------TEIGANAVILPDVIVGADCKIGAGAVVTRNidshTTVAG 199
Cdd:PRK05289   80 RLVIGDNntirefvtinrgtvqgggvTRIGDNNLLMAYVHVAHDCVVGNHVILANN----ATLAG 140
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 102-205 2.16e-06

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.41  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITcNVSIGQGTFINKS----------------------TVISHDVRIGRYCEV-----SPGAKV--- 151
Cdd:COG1207   286 VIGEGVVIGPNCTLK-DSTIGDGVVIKYSviedavvgagatvgpfarlrpgTVLGEGVKIGNFVEVknstiGEGSKVnhl 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 152 --LGRAIIGD-------------------RTEIGANAVILPD------VIVGADCKIGAGAVVTRNIDSHT-TVAGVPAR 203
Cdd:COG1207   365 syIGDAEIGEgvnigagtitcnydgvnkhRTVIGDGAFIGSNtnlvapVTIGDGATIGAGSTITKDVPAGAlAIARARQR 444


                  ..
gi 2098067313 204 SI 205
Cdd:COG1207   445 NI 446
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 113-199 2.48e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.93  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 113 ATITCNVSIGQGTFI-NKSTVISHdvrigrycevspgakvlgRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNI 191
Cdd:PRK14360  366 ATLGEQVNIGAGTITaNYDGVKKH------------------RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDV 427


                  ....*...
gi 2098067313 192 DSHTTVAG 199
Cdd:PRK14360  428 PDNSLAIA 435
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 102-190 4.16e-06

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: 46.60  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRycevspGAKVLGRAIIGDRTEIGANAVI---------LP- 171
Cdd:cd03350     3 RVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDS------WATVGSCAQIGKNVHLSAGAVIggvleplqaTPv 76

                          90       100
                  ....*....|....*....|...
gi 2098067313 172 ----DVIVGADCKIGAGAVVTRN 190
Cdd:cd03350    77 iiedDVFIGANCEVVEGVIVGKG 99
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 127-187 4.67e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.09  E-value: 4.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098067313 127 INKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 145-197 7.04e-06

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 47.71  E-value: 7.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2098067313 145 VSPGAKvlgraiIGDRTEIGANAVILPDVIVGADCKIGAGAVvtrnIDSHTTV 197
Cdd:COG1043    10 VDPGAK------LGENVEIGPFCVIGPDVEIGDGTVIGSHVV----IEGPTTI 52
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 145-197 7.08e-06

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: 47.81  E-value: 7.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2098067313 145 VSPGAKvlgraiIGDRTEIGANAVILPDVIVGADCKIGAGAVvtrnIDSHTTV 197
Cdd:cd03351     8 VDPGAK------IGENVEIGPFCVIGPNVEIGDGTVIGSHVV----IDGPTTI 50
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 94-202 1.06e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 47.32  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  94 ALVGGYDNTIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDV 173
Cdd:PRK12461   77 RLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFC 156

                          90       100
                  ....*....|....*....|....*....
gi 2098067313 174 IVGADCKIGAGAVVTRNIDSHTTVAGVPA 202
Cdd:PRK12461  157 RIGALAMMAGGSRISKDVPPYCMMAGHPT 185
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 125-189 1.11e-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: 48.10  E-value: 1.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2098067313 125 TFIN-KSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVIlpdvivgADCKIGAGAVVTR 189
Cdd:COG1207   254 TIIDpATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-------KDSTIGDGVVIKY 312
PLN02739 PLN02739
serine acetyltransferase
 122-205 1.12e-05

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 47.72  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 122 GQGTFINKSTVISHDVRIGRYCEVSPGAKVLG--RAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRNIDSHTTVAG 199
Cdd:PLN02739  223 GTGVVIGETAVIGDRVSILHGVTLGGTGKETGdrHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAG 302


                  ....*.
gi 2098067313 200 VPARSI 205
Cdd:PLN02739  303 NPAKLI 308
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
155-183 1.30e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 2098067313 155 AIIGDRTEIGANAVILPDVIVGADCKIGA 183
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-199 1.33e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.80  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFIN-----KSTVISHDVRI-----------------GRYCEVSPGAKVLGRAIIGD 159
Cdd:PRK14356  271 TIEPGAEIYGPCEIYGASRIARGAVIHshcwlRDAVVSSGATIhsfshlegaevgdgcsvGPYARLRPGAVLEEGARVGN 350

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2098067313 160 RTEI-------GANA---VILPDVIVGADCKIGAGaVVTRNID---SHTTVAG 199
Cdd:PRK14356  351 FVEMkkavlgkGAKAnhlTYLGDAEIGAGANIGAG-TITCNYDgvnKHRTVIG 402
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-197 1.52e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 47.62  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 106 GVVILSGAT--ITCNVSIGQ------GTFINKSTVISHDVRIGRYC-----EVSPGAKVL----GRAIIGDRTEIGANAV 168
Cdd:PRK14352  257 GVTIVDPATtwIDVDVTIGRdvvihpGTQLLGRTTIGEDAVVGPDTtltdvTVGEGASVVrthgSESEIGAGATVGPFTY 336

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2098067313 169 ILPDVIVGADCKIGAgAVVTRN--IDSHTTV 197
Cdd:PRK14352  337 LRPGTVLGEEGKLGA-FVETKNatIGRGTKV 366
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 103-199 1.59e-05

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: 46.55  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAkVLG-------------RAIIGDR--------- 160
Cdd:COG1043    16 LGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFA-SIGeepqdlkykgeptRLEIGDNntirefvti 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2098067313 161 ----------TEIGANAVILPDVIVGADCKIGAGAVVTRNidshTTVAG 199
Cdd:COG1043    95 hrgtvqgggvTRIGDDNLLMAYVHVAHDCVVGNNVILANN----ATLAG 139
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
103-169 1.84e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.63  E-value: 1.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTfinkstVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVI 169
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEIGPFC------VIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 103-210 2.73e-05

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 45.88  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGaTITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLG--------RAIIGDRTEIGANAVILPDVI 174
Cdd:COG2171   112 LAPGVVLMPS-FVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGvleplqaaPVIIEDNCFIGARSGVVEGVI 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2098067313 175 VGADCKIGAGAVVTRN------IDSHTTVAGVPARSITKSSN 210
Cdd:COG2171   191 VGEGAVLGAGVYLTAStkiydrVTGEVYYGRVPAGSVVVPGS 232
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-191 3.93e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.26  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGY----DNTIEPGVVI-----LSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVS-----PGAKV- 151
Cdd:PRK14356  287 ASRIARGAVIHSHcwlrDAVVSSGATIhsfshLEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKkavlgKGAKAn 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2098067313 152 ----LGRAIIGDRTEIGA-------------------------NAVILPDVIVGADCKIGAGAVVTRNI 191
Cdd:PRK14356  367 hltyLGDAEIGAGANIGAgtitcnydgvnkhrtvigegafigsNTALVAPVTIGDGALVGAGSVITKDV 435
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 121-191 3.98e-05

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: 42.18  E-value: 3.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2098067313 121 IGQGTFINKSTVISHDVrIGRYCEVSP-----GAKVLGRAIIGDRTEIGaNAVILPDVIVGADCKIGAGAVVTRNI 191
Cdd:cd05787     2 IGRGTSIGEGTTIKNSV-IGRNCKIGKnvvidNSYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGV 75
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 125-197 4.09e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.36  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 125 TFIN-KSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILpdvivgaDCKIGAGAVVTR------NIDSHTTV 197
Cdd:PRK14354  253 TIIDpESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIV-------DSTIGDGVTITNsvieesKVGDNVTV 325
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 125-197 7.07e-05

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: 43.95  E-value: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 125 TFINKSTV-ISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILpdvivgaDCKIGAGAVVTRN-------IDSHTT 196
Cdd:cd03353     3 TLIDPETTyIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-------DSTIGDGVVIKASsviegavIGNGAT 75


                  .
gi 2098067313 197 V 197
Cdd:cd03353    76 V 76
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-182 7.87e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILS------GATITCNVSIGQGTFINKSTVIShDVRIGRYCEVSPGAkVLGRAIIGDRTEIGANAVILPDVIVG 176
Cdd:PRK14355  265 IDRGVVIGRdttiypGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAGS-VLEDSVVGDDVAIGPMAHLRPGTELS 342


                  ....*.
gi 2098067313 177 ADCKIG 182
Cdd:PRK14355  343 AHVKIG 348
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 102-203 8.19e-05

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: 44.24  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATItcnvsIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKI 181
Cdd:COG1043    93 TIHRGTVQGGGVTR-----IGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMV 167

                          90       100
                  ....*....|....*....|..
gi 2098067313 182 GAGAVVTRNIDSHTTVAGVPAR 203
Cdd:COG1043   168 GGGSGVVKDVPPYVLAAGNPAR 189
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-206 8.79e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  95 LVGGYDNTIEPGVVILSGATITCNVSIGQGTFInKSTVISHDVRIGRY-----------CEVSP---------------- 147
Cdd:PRK09451  266 LTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVL-KNCVIGDDCEISPYsvvedanlgaaCTIGPfarlrpgaelaegahv 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 148 -------------GAKV-----LGRAIIGDRTEIGANA-------------VILPDVIVGADCK------------IGAG 184
Cdd:PRK09451  345 gnfvemkkarlgkGSKAghltyLGDAEIGDNVNIGAGTitcnydgankfktIIGDDVFVGSDTQlvapvtvgkgatIGAG 424

                         170       180
                  ....*....|....*....|...
gi 2098067313 185 AVVTRNI-DSHTTVAGVPARSIT 206
Cdd:PRK09451  425 TTVTRDVaENELVISRVPQRHIQ 447
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
156-189 1.30e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 39.35  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2098067313 156 IIGDRTEIGANAVIlpDVIVGADCKIGAGAVVTR 189
Cdd:pfam14602   2 IIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 103-189 1.37e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.86  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTFINKstvishDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPD---------- 172
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGA------NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEpqdftykgee 75

                          90
                  ....*....|....*....
gi 2098067313 173 --VIVGADCKIGAGAVVTR 189
Cdd:PRK12461   76 srLEIGDRNVIREGVTIHR 94
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 102-199 1.46e-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: 43.57  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSgatitcNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAkVLG-------------RAIIGDR-------- 160
Cdd:cd03351    19 EIGPFCVIGP------NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFA-SIGeapqdlkykgeptRLEIGDNntirefvt 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2098067313 161 -----------TEIGANAVILPDVIVGADCKIGAGAVVTRNidshTTVAG 199
Cdd:cd03351    92 ihrgtaqgggvTRIGNNNLLMAYVHVAHDCVIGNNVILANN----ATLAG 137
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 103-169 1.77e-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: 43.19  E-value: 1.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098067313 103 IEPGVVILSGATITCNVSIGQGTfinkstVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVI 169
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFC------VIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
102-203 1.97e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATItcnvsIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKI 181
Cdd:PRK05289   94 TINRGTVQGGGVTR-----IGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMV 168

                          90       100
                  ....*....|....*....|..
gi 2098067313 182 GAGAVVTRNIDSHTTVAGVPAR 203
Cdd:PRK05289  169 GGMSGVSQDVPPYVLAEGNPAR 190
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 109-189 2.51e-04

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: 40.52  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 109 ILSGATITcNVSIGQGTFINKSTV----ISHDVRIGRYCEVSpGAKVLGRAIIGDRTEIGaNAVILPDVIVGADCKIGAG 184
Cdd:cd04651     4 IGRRGEVK-NSLVSEGCIISGGTVensvLFRGVRVGSGSVVE-DSVIMPNVGIGRNAVIR-RAIIDKNVVIPDGVVIGGD 80


                  ....*
gi 2098067313 185 AVVTR 189
Cdd:cd04651    81 PEEDR 85
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 155-199 2.79e-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: 42.70  E-value: 2.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2098067313 155 AIIGDRTEIGANAVILPDVIVGADCKIGAGAVvtrnIDSHTTVAG 199
Cdd:COG1043     8 AIVDPGAKLGENVEIGPFCVIGPDVEIGDGTV----IGSHVVIEG 48
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 125-186 3.39e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.19  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2098067313 125 TFIN-KSTVISHDVRIGRYCEVSPGAKVLGRAIIGDRTEIGANAVIlPDVIVGADCKIGAGAV 186
Cdd:PRK14355  256 TLIDpETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSV 317
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 102-182 4.51e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.32  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAkVLG-------------RAIIGDR-------- 160
Cdd:PRK12461   13 KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGA-VVGdepqdftykgeesRLEIGDRnviregvt 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2098067313 161 ----------TEIGANAVILPDVIVGADCKIG 182
Cdd:PRK12461   92 ihrgtkgggvTRIGNDNLLMAYSHVAHDCQIG 123
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 138-191 4.73e-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: 39.15  E-value: 4.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2098067313 138 RIGRYCEVSPGAKVlGRAIIGDRTEIGANAVIlPDVIVGADCKIGAGAVVTRNI 191
Cdd:cd03356     1 LIGESTVIGENAII-KNSVIGDNVRIGDGVTI-TNSILMDNVTIGANSVIVDSI 52
PLN02296 PLN02296
carbonate dehydratase
 89-207 4.85e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 42.03  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  89 FISQKALVGGyDNTIEPGVVILSGATI---TCNVSIGQGTFINKSTVishdVRIGRyceVSPGAKVLgRAIIGDRTEIGA 165
Cdd:PLN02296   60 FVAPSASVIG-DVQVGRGSSIWYGCVLrgdVNSISVGSGTNIQDNSL----VHVAK---TNLSGKVL-PTIIGDNVTIGH 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098067313 166 NAVI-----------------LPDVIVGADCKIGAGAVVTRN--IDSHTTVAGVPARSITK 207
Cdd:PLN02296  131 SAVLhgctvedeafvgmgatlLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRK 191
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 82-182 6.32e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.22  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  82 LGGVltTFISQKALVGGYDNTIEPGVVI-----LSGAT-ITCNVSIGQGTFINKStvishdvRIGRYCEVSpgAKVLGRA 155
Cdd:PRK14360  246 LAGV--TFIDPASCTISETVELGPDVIIepqthLRGNTvIGSGCRIGPGSLIENS-------QIGENVTVL--YSVVSDS 314

                          90       100
                  ....*....|....*....|....*..
gi 2098067313 156 IIGDRTEIGANAVILPDVIVGADCKIG 182
Cdd:PRK14360  315 QIGDGVKIGPYAHLRPEAQIGSNCRIG 341
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 145-197 9.61e-04

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: 41.54  E-value: 9.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2098067313 145 VSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTTV 197
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDcvLHPNVTI 159
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-191 1.42e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  87 TTFISQKALVGGY----DNTIEPGVVIL----SGATITCNVSIGQGTFINKSTVISHDVRIGRYCE-----VSPGAKV-- 151
Cdd:PRK14352  289 RTTIGEDAVVGPDttltDVTVGEGASVVrthgSESEIGAGATVGPFTYLRPGTVLGEEGKLGAFVEtknatIGRGTKVph 368

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2098067313 152 ---LGRAIIGDRTEIGANAV-------------ILPDVIVGADCKI------------GAGAVVTRNI 191
Cdd:PRK14352  369 ltyVGDADIGEHSNIGASSVfvnydgvnkhrttIGSHVRTGSDTMFvapvtvgdgaytGAGTVIREDV 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 119-236 2.02e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 40.89  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 119 VSIGQGTFInkstviSHDVRIGRYcEVSPGAKVLGRAIIGDRTEIGANAVILPDVIVGADCKIGAGAVVTRN--IDSHTT 196
Cdd:TIGR02353 373 TDIGEETFI------ADGLLMGNA-RLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDgkVREGVG 445

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2098067313 197 VAGVPARSITKSSNNAFKLKSKIRNLLYHIRIAdfRKLRE 236
Cdd:TIGR02353 446 WLGSPPFELPRRVNRDDELEALTFEPDPRRRLA--RKNVE 483
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-205 2.30e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313  98 GYDNTIEPGVViLSGATITCNVSIGQGTFINKSTVISHDVRIGRYCE-----VSPGAKV-----LGRAIIGDRTEIGA-- 165
Cdd:PRK14355  307 GDDVTVKAGSV-LEDSVVGDDVAIGPMAHLRPGTELSAHVKIGNFVEtkkivMGEGSKAshltyLGDATIGRNVNIGCgt 385

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2098067313 166 -----------NAVILPDVIVGADCKIGAGAVVTRN--IDSHTTVA-GVPARSI 205
Cdd:PRK14355  386 itcnydgvkkhRTVIEDDVFVGSDVQFVAPVTVGRNslIAAGTTVTkDVPPDSL 439
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
161-187 2.84e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 2098067313 161 TEIGANAVILPDVIVGADCKIGAGAVV 187
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVII 28
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 121-187 3.08e-03

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: 38.76  E-value: 3.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098067313 121 IGQGTFINKSTVISHDVRIGRYCEVSPGAKVlgRA------IIGDRTEIGANAVILP----DVIVGADCKIGAGAVV 187
Cdd:cd00710     5 IDPSAYVHPTAVVIGDVIIGDNVFVGPGASI--RAdegtpiIIGANVNIQDGVVIHAlegySVWIGKNVSIAHGAIV 79
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-191 3.84e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 39.75  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 103 IEPGVVILSGAT--ITCNVSIGQGTFINKSTVISHDVRIGRYCEVSPGAKVLgRAIIGDRTEIGAN----AVILPDVIVG 176
Cdd:PRK14357  238 MENGVTILDPNTtyIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIV-DCEIGNNVKIIRSecekSVIEDDVSVG 316

                          90
                  ....*....|....*
gi 2098067313 177 ADCKIGAGAVVTRNI 191
Cdd:PRK14357  317 PFSRLREGTVLKKSV 331
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 102-199 5.30e-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: 38.08  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098067313 102 TIEPGVVILSGATITCNVSIGQGTFINKSTVI---SHDVRIGRYCEVSPGAKVLGRAI---------------------- 156
Cdd:cd04646     1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIiaeAGPIIIGENNIIEEQVTIVNKKPkdpaepkpmiigsnnvfevgck 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2098067313 157 -----IGDRTEIGANAVILPDVIVGADCKIGAGAVVT--RNIDSHTTVAG 199
Cdd:cd04646    81 cealkIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPssEILPENTVIYG 130
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
118-147 6.75e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 6.75e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2098067313 118 NVSIGQGTFINKSTVISHDVRIGRYCEVSP 147
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
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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