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Conserved domains on  [gi|446504714|ref|WP_000582568|]
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MULTISPECIES: acetyltransferase [Escherichia]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 8-155 3.41e-40

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd05636:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 163  Bit Score: 133.48  E-value: 3.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:cd05636   16 GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVN 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504714  88 LGAQVRTSNHRLDEQPVSVRTPDGIIATGCDKLGCYIGQRSRLGVQVIILPGRIISPNTQLGPRVIVE 155
Cdd:cd05636   96 LGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
 
Name Accession Description Interval E-value
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 8-155 3.41e-40

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: 133.48  E-value: 3.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:cd05636   16 GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVN 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504714  88 LGAQVRTSNHRLDEQPVSVRTPDGIIATGCDKLGCYIGQRSRLGVQVIILPGRIISPNTQLGPRVIVE 155
Cdd:cd05636   96 LGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-154 1.30e-37

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 132.72  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714    8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:TIGR03992 247 GPVVIGEGAVIRSGTYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCN 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714   88 LGAQVRTSNHRLDEQPVSVRTPDGIIATGCDKLGCYIGQRSRLGVQVIILPGRIISPNTQLGPRVIV 154
Cdd:TIGR03992 327 FGAGTKVANLRHDDKPVKVTVKGKRVDTGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-96 1.52e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.47  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   9 EVVIGANTRIC-----HGAVIQGPVV----IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIAD 79
Cdd:PRK14354 289 DCVIGPGSRIVdstigDGVTITNSVIeeskVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGD 368

                         90
                 ....*....|....*..
gi 446504714  80 SVVANQAYLGAQVRTSN 96
Cdd:PRK14354 369 AEVGENVNIGCGTITVN 385
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 10-84 3.38e-11

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: 60.43  E-value: 3.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRIC-----HGAVIQGPV----VIGANCLIGNYAFIRPGTIISNGVKIG-FAtEIKNAVIEAE----------- 68
Cdd:COG1207  291 VVIGPNCTLKdstigDGVVIKYSViedaVVGAGATVGPFARLRPGTVLGEGVKIGnFV-EVKNSTIGEGskvnhlsyigd 369

                         90
                 ....*....|....*..
gi 446504714  69 ATIGPQCFI-ADSVVAN 84
Cdd:COG1207  370 AEIGEGVNIgAGTITCN 386
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
10-38 3.95e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 3.95e-04
                          10        20
                  ....*....|....*....|....*....
gi 446504714   10 VVIGANTRICHGAVIQGPVVIGANCLIGN 38
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 8-155 3.41e-40

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: 133.48  E-value: 3.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:cd05636   16 GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVN 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504714  88 LGAQVRTSNHRLDEQPVSVRTPDGIIATGCDKLGCYIGQRSRLGVQVIILPGRIISPNTQLGPRVIVE 155
Cdd:cd05636   96 LGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-154 1.30e-37

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 132.72  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714    8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:TIGR03992 247 GPVVIGEGAVIRSGTYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCN 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714   88 LGAQVRTSNHRLDEQPVSVRTPDGIIATGCDKLGCYIGQRSRLGVQVIILPGRIISPNTQLGPRVIV 154
Cdd:TIGR03992 327 FGAGTKVANLRHDDKPVKVTVKGKRVDTGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 8-101 4.85e-13

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: 63.98  E-value: 4.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIIsNGVKIGFATEIKNAVIEAEATIGPQCFI-ADSVVANQA 86
Cdd:cd03353   14 GDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIG-DGVVIKASSVIEGAVIGNGATVGPFAHLrPGTVLGEGV 92

                         90
                 ....*....|....*
gi 446504714  87 YLGAQVRTSNHRLDE 101
Cdd:cd03353   93 HIGNFVEIKKSTIGE 107
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-96 1.52e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.47  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   9 EVVIGANTRIC-----HGAVIQGPVV----IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIAD 79
Cdd:PRK14354 289 DCVIGPGSRIVdstigDGVTITNSVIeeskVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGD 368

                         90
                 ....*....|....*..
gi 446504714  80 SVVANQAYLGAQVRTSN 96
Cdd:PRK14354 369 AEVGENVNIGCGTITVN 385
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 11-96 5.15e-12

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: 61.28  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  11 VIGANTRICHGAVIQGpVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLGA 90
Cdd:cd03353   52 TIGDGVVIKASSVIEG-AVIGNGATVGPFAHLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGA 130


                 ....*.
gi 446504714  91 QVRTSN 96
Cdd:cd03353  131 GTITCN 136
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-96 1.39e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 61.80  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRICHGAVIQG-----PVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVAN 84
Cdd:PRK14353 281 VVFGPGVTVASGAVIHAfshleGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGA 360

                         90
                 ....*....|..
gi 446504714  85 QAYLGAQVRTSN 96
Cdd:PRK14353 361 GANIGAGTITCN 372
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 10-84 3.38e-11

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: 60.43  E-value: 3.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRIC-----HGAVIQGPV----VIGANCLIGNYAFIRPGTIISNGVKIG-FAtEIKNAVIEAE----------- 68
Cdd:COG1207  291 VVIGPNCTLKdstigDGVVIKYSViedaVVGAGATVGPFARLRPGTVLGEGVKIGnFV-EVKNSTIGEGskvnhlsyigd 369

                         90
                 ....*....|....*..
gi 446504714  69 ATIGPQCFI-ADSVVAN 84
Cdd:COG1207  370 AEIGEGVNIgAGTITCN 386
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-101 9.77e-11

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: 59.27  E-value: 9.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIGFaTEIKNAVIEAEATIGPQCFI-ADSVVANQA 86
Cdd:COG1207  265 GDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKY-SVIEDAVVGAGATVGPFARLrPGTVLGEGV 342

                         90
                 ....*....|....*
gi 446504714  87 YLGAQVRTSNHRLDE 101
Cdd:COG1207  343 KIGNFVEVKNSTIGE 357
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 2-96 1.56e-10

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


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 55.36  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   2 IIDESAGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfaTEIKNAVIEAEATIGPQCFIADSV 81
Cdd:cd05635    4 VLDAEDGPIYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIG--GEVEDSIIEGYSNKQHDGFLGHSY 81

                         90
                 ....*....|....*
gi 446504714  82 VANQAYLGAQVRTSN 96
Cdd:cd05635   82 LGSWCNLGAGTNNSD 96
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-96 3.91e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 54.55  E-value: 3.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGPVV---------------IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIG 72
Cdd:PRK14360 279 GNTVIGSGCRIGPGSLIENSQIgenvtvlysvvsdsqIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVN 358

                         90       100
                 ....*....|....*....|....
gi 446504714  73 PQCFIADSVVANQAYLGAQVRTSN 96
Cdd:PRK14360 359 HLSYIGDATLGEQVNIGAGTITAN 382
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-82 7.99e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   2 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGnyafirPGTIISNGVKIGfateiKNAVIEAEATIGPQCFIADSV 81
Cdd:PRK00892 108 VIDPSA---KIGEGVSIGPNAVIGAGVVIGDGVVIG------AGAVIGDGVKIG-----ADCRLHANVTIYHAVRIGNRV 173


                 .
gi 446504714  82 V 82
Cdd:PRK00892 174 I 174
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 10-82 3.67e-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: 50.87  E-value: 3.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446504714  10 VVIGANTRICHGAVIQGPVVIGANCLIGnyafirPGTIISNGVKIGfateiKNAVIEAEATIGPQCFIADSVV 82
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIG------PGVVIGDGVVIG-----DDCVIHPNVTIYEGCIIGDRVI 63
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 15-97 8.37e-08

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 50.49  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  15 NTRICHGAVIQG-----PVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLG 89
Cdd:PRK14356 304 DAVVSSGATIHSfshleGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIG 383


                 ....*...
gi 446504714  90 AQVRTSNH 97
Cdd:PRK14356 384 AGTITCNY 391
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-72 1.69e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 49.63  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   2 IIDESA--GE-------VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIG 72
Cdd:COG1044  104 VIDPSAkiGEgvsigpfAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIG-----DRVIIHSGAVIG 178
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-82 3.16e-07

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: 48.25  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   2 IIDESA---GEVVIGANTRICHGAVIQGPVVIGANCL------------IGNYAFIRPGTIISNGVKIGFATEI-KNAVI 65
Cdd:cd03360   86 LIHPSAvvsPSAVIGEGCVIMAGAVINPDARIGDNVIintgavighdcvIGDFVHIAPGVVLSGGVTIGEGAFIgAGATI 165

                         90
                 ....*....|....*...
gi 446504714  66 EAEATIGPQCFI-ADSVV 82
Cdd:cd03360  166 IQGVTIGAGAIIgAGAVV 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
10-162 5.39e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.40  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRICHGAVIQGPVVIganclIGNYAFIRPGTIISNGVKIgfateiknavieaeaTIGPQCFIADsvvanqaylG 89
Cdd:COG0110    9 ARIGDGVVIGPGVRIYGGNIT-----IGDNVYIGPGVTIDDPGGI---------------TIGDNVLIGP---------G 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446504714  90 AQVRTSNHRLDEQPVSVRTPDGIIatgcdklgcyIGQRSRLGVQVIILPGRIISPNTQLGPRVIVERNLPTGT 162
Cdd:COG0110   60 VTILTGNHPIDDPATFPLRTGPVT----------IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYA 122
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 7-96 8.44e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 47.67  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   7 AGEVVIGANTRICHGAVIQGPVV----------IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCF 76
Cdd:PRK14358 292 ADGVTIGAYSVVTDSVLHEGAVIkphsvlegaeVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAY 371

                         90       100
                 ....*....|....*....|
gi 446504714  77 IADSVVANQAYLGAQVRTSN 96
Cdd:PRK14358 372 LGDVTIGAETNVGAGTIVAN 391
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 10-76 1.21e-06

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: 46.63  E-value: 1.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714  10 VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCF 76
Cdd:cd03352   14 AVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIG-----DRVIIHSGAVIGSDGF 75
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-106 1.55e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 46.85  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   7 AGEVVIGANTRICHGAVIQGPVV---------IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEA---------- 67
Cdd:PRK14352 293 GEDAVVGPDTTLTDVTVGEGASVvrthgseseIGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRgtkvphltyv 372

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446504714  68 -EATIGPQCFI-ADSVVAN-------QAYLGAQVRTSNHRLDEQPVSV 106
Cdd:PRK14352 373 gDADIGEHSNIgASSVFVNydgvnkhRTTIGSHVRTGSDTMFVAPVTV 420
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-73 1.83e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 46.66  E-value: 1.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446504714  10 VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIGFATEIKNAVIEAEATIGP 73
Cdd:PRK14355 269 VVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAGSVLEDSVVGDDVAIGP 331
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 3-90 1.84e-06

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: 45.48  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   3 IDESA---GEVVIGANTRICHGAVIQG---PVVIGANCLIGNYAFIRP----GTIISNGVKIGfateiKNAVIEAeATIG 72
Cdd:cd04645    8 IAPNAtviGDVTLGEGSSVWFGAVLRGdvnPIRIGERTNIQDGSVLHVdpgyPTIIGDNVTVG-----HGAVLHG-CTIG 81

                         90
                 ....*....|....*....
gi 446504714  73 PQCFIA-DSVVANQAYLGA 90
Cdd:cd04645   82 DNCLIGmGAIILDGAVIGK 100
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 3-92 2.03e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 45.40  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   3 IDESA---GEVVIGANTRICHGAVIQG---PVVIGANCLIGNYAFIR--PG--TIISNGVKIGfateiKNAVIEAeATIG 72
Cdd:COG0663   19 VAPTAvviGDVTIGEDVSVWPGAVLRGdvgPIRIGEGSNIQDGVVLHvdPGypLTIGDDVTIG-----HGAILHG-CTIG 92

                         90       100
                 ....*....|....*....|.
gi 446504714  73 PQCFIAD-SVVANQAYLGAQV 92
Cdd:COG0663   93 DNVLIGMgAIVLDGAVIGDGS 113
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 11-82 2.56e-06

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: 43.38  E-value: 2.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446504714  11 VIGANTRICHGAVIqGPVVIGANCLIGNYAFIRpGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVV 82
Cdd:cd03356    1 LIGESTVIGENAII-KNSVIGDNVRIGDGVTIT-NSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI 70
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-97 2.76e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 46.17  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRICHGAVIQGPVViGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLG 89
Cdd:PRK09451 301 CVIGDDCEISPYSVVEDANL-GAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIG 379


                 ....*...
gi 446504714  90 AQVRTSNH 97
Cdd:PRK09451 380 AGTITCNY 387
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 12-55 6.28e-06

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: 43.26  E-value: 6.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446504714  12 IGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG 55
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIG 44
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 10-89 8.49e-06

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: 41.85  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIR--PGTIISNGVKIGfateiKNAVIEAEATIGPQCFIAD-SVVANQA 86
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaaTGPNEKNPTIIG-----DNVEIGANAVIHGGVKIGDnAVIGAGA 75


                 ...
gi 446504714  87 YLG 89
Cdd:cd00208   76 VVT 78
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 11-90 9.12e-06

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 43.77  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  11 VIGANTRICHGAVIQGPVVIGANCLIGNYAFIR----PGTIISNGVKI----------GFATEIKN-------AVIEAEA 69
Cdd:cd00710    4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRadegTPIIIGANVNIqdgvvihaleGYSVWIGKnvsiahgAIVHGPA 83

                         90       100
                 ....*....|....*....|..
gi 446504714  70 TIGPQCFIA-DSVVANqAYLGA 90
Cdd:cd00710   84 YIGDNCFIGfRSVVFN-AKVGD 104
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 8-73 1.10e-05

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: 43.17  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVI----QGPVVIGAN-----------CLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIG 72
Cdd:cd04645   37 NPIRIGERTNIQDGSVLhvdpGYPTIIGDNvtvghgavlhgCTIGDNCLIGMGAIILDGAVIG-----KGSIVAAGSLVP 111


                 .
gi 446504714  73 P 73
Cdd:cd04645  112 P 112
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 2-58 1.24e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 43.96  E-value: 1.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446504714   2 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG-FAT 58
Cdd:cd03351    7 IVDPGA---KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFpFAS 61
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 14-82 1.86e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 1.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446504714  14 ANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCFIADSVV 82
Cdd:PRK00892  99 PAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIG-----AGAVIGDGVKIGADCRLHANVT 162
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
2-54 2.44e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 2.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446504714   2 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKI 54
Cdd:PRK05289  10 IVEPGA---KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRI 59
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 11-82 3.02e-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: 40.64  E-value: 3.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714  11 VIGANTRICHGAVIQGPVvIGANCLIGNY-----AFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVV 82
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSV-IGRNCKIGKNvvidnSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVV 76
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 22-93 3.09e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.08  E-value: 3.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446504714  22 AVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCFI-ADSVVANQAYLGAQVR 93
Cdd:COG1044  103 AVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIG-----PGVVIGDGVVIGDDCVLhPNVTIYERCVIGDRVI 170
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-97 3.96e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.83  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  12 IGANTRI----CHGAVIQGPVVIGAnclignYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 87
Cdd:PRK14357 293 IGNNVKIirseCEKSVIEDDVSVGP------FSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVN 366

                         90
                 ....*....|
gi 446504714  88 LGAQVRTSNH 97
Cdd:PRK14357 367 IGAGTITCNY 376
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 2-58 5.15e-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: 42.31  E-value: 5.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446504714   2 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG-FAT 58
Cdd:COG1043    9 IVDPGA---KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFpFAS 63
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
8-82 5.58e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 41.01  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVI--QGPVVIGANCLIGNYAFIRPGT----------------IISNGVKIGFateikNAVIEAEA 69
Cdd:COG0110   26 GNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNhpiddpatfplrtgpvTIGDDVWIGA-----GATILPGV 100

                         90
                 ....*....|....
gi 446504714  70 TIGPQCFI-ADSVV 82
Cdd:COG0110  101 TIGDGAVVgAGSVV 114
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 2-54 1.84e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.39  E-value: 1.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446504714   2 IIDESAGevvIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKI 54
Cdd:PRK12461   7 VIDPSAK---LGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKI 56
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 6-79 2.46e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.99  E-value: 2.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446504714   6 SAGEVVIGANTRICHGAVIQGPVVIGaNCLIGNYAFIRpGTIISNGVKIGfateiKNAVIEAEATIGPQCFIAD 79
Cdd:cd03356   13 IIKNSVIGDNVRIGDGVTITNSILMD-NVTIGANSVIV-DSIIGDNAVIG-----ENVRVVNLCIIGDDVVVED 79
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-93 3.01e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.01  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   7 AGEVVIGANTRICHGAVIQGPVVIGANC------------------------LIGNYAFIRPGTIISNGVKIGFATEIKN 62
Cdd:PRK12461  27 GANVEIGDGTWIGPHAVILGPTRIGKNNkihqgavvgdepqdftykgeesrlEIGDRNVIREGVTIHRGTKGGGVTRIGN 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446504714  63 A-VIEAEATIGPQCFIADSVV-ANQAYLGAQVR 93
Cdd:PRK12461 107 DnLLMAYSHVAHDCQIGNNVIlVNGALLAGHVT 139
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 8-89 3.62e-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: 39.62  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIGfateiKNAVIEAEATIGPQ 74
Cdd:COG1043   48 GPTTIGKNNRIFPFASIGEEpqdlkykgeptrLEIGDNNTIREFVTIHRGTVQGGGVtRIG-----DDNLLMAYVHVAHD 122

                         90
                 ....*....|....*.
gi 446504714  75 CFIADSVV-ANQAYLG 89
Cdd:COG1043  123 CVVGNNVIlANNATLA 138
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
10-38 3.95e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 3.95e-04
                          10        20
                  ....*....|....*....|....*....
gi 446504714   10 VVIGANTRICHGAVIQGPVVIGANCLIGN 38
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 6-37 4.92e-04

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 38.76  E-value: 4.92e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446504714   6 SAGEVVIGANTRICHGAVIQGPVVIGANCLIG 37
Cdd:cd00710   61 EGYSVWIGKNVSIAHGAIVHGPAYIGDNCFIG 92
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
7-89 5.09e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   7 AGEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIGfateiKNAVIEAEATIGP 73
Cdd:PRK05289  48 DGHTTIGKNNRIFPFASIGEDpqdlkykgeptrLVIGDNNTIREFVTINRGTVQGGGVtRIG-----DNNLLMAYVHVAH 122

                         90
                 ....*....|....*..
gi 446504714  74 QCFIADSVV-ANQAYLG 89
Cdd:PRK05289 123 DCVVGNHVIlANNATLA 139
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
6-55 5.68e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 38.31  E-value: 5.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446504714   6 SAGEVVIGANTRICHGAVI----------------QGPVVIGANCLIGNYAFIRPGTIISNGVKIG 55
Cdd:COG0110   44 DPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDDVWIGAGATILPGVTIGDGAVVG 109
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 8-97 5.97e-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: 38.95  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIGfateiKNAVIEAEATIGPQ 74
Cdd:cd03351   46 GPTTIGKNNRIFPFASIGEApqdlkykgeptrLEIGDNNTIREFVTIHRGTAQGGGVtRIG-----NNNLLMAYVHVAHD 120

                         90       100
                 ....*....|....*....|....
gi 446504714  75 CFIADSVV-ANQAYLGAQVRTSNH 97
Cdd:cd03351  121 CVIGNNVIlANNATLAGHVEIGDY 144
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 47-93 8.02e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 8.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446504714  47 IISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLGAQVR 93
Cdd:PRK05293 310 VLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
22-77 9.12e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.54  E-value: 9.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714  22 AVIQGPVVIGANCLIGnyafirPGTIISNGVKIGFATEIK-NAVIEAEATIGPQCFI 77
Cdd:PRK05289   9 AIVEPGAKIGENVEIG------PFCVIGPNVVIGDGTVIGsHVVIDGHTTIGKNNRI 59
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 61-154 1.00e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.46  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  61 KNAVIEAEATIGPQCFI-ADSVVANQAYLGAqvrtsnhrldeqpvsvrtpdgiiatgcdklGCYIGQRSRLGVQVIILPG 139
Cdd:COG1044  107 PSAKIGEGVSIGPFAVIgAGVVIGDGVVIGP------------------------------GVVIGDGVVIGDDCVLHPN 156

                         90
                 ....*....|....*
gi 446504714 140 RIISPNTQLGPRVIV 154
Cdd:COG1044  157 VTIYERCVIGDRVII 171
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 10-55 1.40e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.02  E-value: 1.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446504714  10 VVIGANTRIcHGAVIQGPVVIGANCLIGnyafirPGTIISNGVKIG 55
Cdd:cd05787   40 VTIEDGCTI-HHSIVADGAVIGKGCTIP------PGSLISFGVVIG 78
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 10-73 1.54e-03

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: 37.79  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446504714  10 VVIGANTRICHGAVIQG--------PVVIGANCLIGNyafirpGTIISNGVKIGfateiKNAVIEAEATIGP 73
Cdd:COG2171  145 AQIGKNVHLSGGAGIGGvleplqaaPVIIEDNCFIGA------RSGVVEGVIVG-----EGAVLGAGVYLTA 205
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-73 1.61e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.21  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446504714   9 EVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIgFATEIKNAVIEAEATIGP 73
Cdd:PRK14357 255 DVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIV-DCEIGNNVKI-IRSECEKSVIEDDVSVGP 317
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 30-89 3.39e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 36.93  E-value: 3.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446504714  30 IGANCLIGNYAFIRPGTIIS------NGVKIGFATEIKNAVIEAEATIgPQCFIADSVVANQAYLG 89
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEgktvigEGVVIGPNCTLKDSTIGDGVVI-KYSVIEDAVVGAGATVG 327
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 22-77 3.66e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 36.53  E-value: 3.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446504714  22 AVIQGPVVIGANCLIGnyafirPGTIISNGVKIGFATEIK-NAVIEAEATIGPQCFI 77
Cdd:COG1043    8 AIVDPGAKLGENVEIG------PFCVIGPDVEIGDGTVIGsHVVIEGPTTIGKNNRI 58
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
4-37 4.46e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 35.62  E-value: 4.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446504714   4 DESAGEVVIGANTRICHGAVIQGPVVIGANCLIG 37
Cdd:COG0110   76 PLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVG 109
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 10-82 5.90e-03

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: 34.74  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  10 VVIGANTRICHGAVIQ--GPVVIGANCLIGNYAFIRPG-------------------TIISNGVKIGFateikNAVIEAE 68
Cdd:cd04647    2 ISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapIVIGDDVWIGA-----NVVILPG 76

                         90
                 ....*....|....*
gi 446504714  69 ATIGPQCFI-ADSVV 82
Cdd:cd04647   77 VTIGDGAVVgAGSVV 91
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 36-162 6.11e-03

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 34.89  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714  36 IGNYAFIRPGTIISNGVKIgfateiknavieaeaTIGPqcfiaDSVVANQAYLGA---QVRTSNHRLDEQPVsvrtpdgi 112
Cdd:cd05825    6 IGDNSWIGEGVWIYNLAPV---------------TIGS-----DACISQGAYLCTgshDYRSPAFPLITAPI-------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446504714 113 iatgcdklgcYIGQRSRLGVQVIILPGRIISPNTQLGPRVIVERNLPTGT 162
Cdd:cd05825   58 ----------VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWT 97
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 22-77 6.27e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 35.87  E-value: 6.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446504714  22 AVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCFI 77
Cdd:cd03351    6 AIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIG-----SHVVIDGPTTIGKNNRI 56
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 8-79 6.72e-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: 35.38  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504714   8 GEVVIGANTRICHGAVI---QGPVVIGANCLIGNYAFIR----PGTIISNGVKIG-----------FATEI-KNAVIEAE 68
Cdd:cd04646   16 GDVTIGPGTVVHPRATIiaeAGPIIIGENNIIEEQVTIVnkkpKDPAEPKPMIIGsnnvfevgckcEALKIgNNNVFESK 95

                         90
                 ....*....|.
gi 446504714  69 ATIGPQCFIAD 79
Cdd:cd04646   96 SFVGKNVIITD 106
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
27-55 8.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 8.60e-03
                          10        20
                  ....*....|....*....|....*....
gi 446504714   27 PVVIGANCLIGNYAFIRPGTIISNGVKIG 55
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 10-55 8.81e-03

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: 35.46  E-value: 8.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446504714  10 VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG 55
Cdd:cd03352  133 VRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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