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Conserved domains on  [gi|1626990291|gb|TIK30890|]
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acetyltransferase [Escherichia coli]

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 ...
 16-174 3.05e-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: 134.25  E-value: 3.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDesaGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCF 95
Cdd:cd05636     8 VEEGVTIK---GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNY 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626990291  96 IADSVVANQAYLGAQVRTSNHRLDEQPVSVRTPEGIIATGCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIVE 174
Cdd:cd05636    85 VGDSVLGENVNLGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 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 ...
 16-174 3.05e-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: 134.25  E-value: 3.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDesaGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCF 95
Cdd:cd05636     8 VEEGVTIK---GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNY 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626990291  96 IADSVVANQAYLGAQVRTSNHRLDEQPVSVRTPEGIIATGCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIVE 174
Cdd:cd05636    85 VGDSVLGENVNLGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 27-173 2.02e-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: 133.10  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  27 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 106
Cdd:TIGR03992 247 GPVVIGEGAVIRSGTYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCN 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626990291 107 LGAQVRTSNHRLDEQPVSVRTPEGIIATGCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIV 173
Cdd:TIGR03992 327 FGAGTKVANLRHDDKPVKVTVKGKRVDTGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-115 8.10e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 65.62  E-value: 8.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDEsagEVVIGANTRIC-----HGAVIQGPVV----IGANCLIGNYAFIRPGTIISNGVKIGFATEIKN 81
Cdd:PRK14354  275 EPGVVIKGNTVIGE---DCVIGPGSRIVdstigDGVTITNSVIeeskVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKK 351

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1626990291  82 AVIEAEATIGPQCFIADSVVANQAYLGAQVRTSN 115
Cdd:PRK14354  352 STIGEGTKVSHLTYIGDAEVGENVNIGCGTITVN 385
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-103 1.98e-12

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: 64.66  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  13 NVQIADQVIIDEsagEVVIGANTRIC-----HGAVIQGPV----VIGANCLIGNYAFIRPGTIISNGVKIG-FAtEIKNA 82
Cdd:COG1207   278 NVILEGKTVIGE---GVVIGPNCTLKdstigDGVVIKYSViedaVVGAGATVGPFARLRPGTVLGEGVKIGnFV-EVKNS 353

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1626990291  83 VIEAE-----------ATIGPQCFI-ADSVVAN 103
Cdd:COG1207   354 TIGEGskvnhlsyigdAEIGEGVNIgAGTITCN 386
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
29-57 2.81e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 2.81e-04
                          10        20
                  ....*....|....*....|....*....
gi 1626990291  29 VVIGANTRICHGAVIQGPVVIGANCLIGN 57
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 ...
 16-174 3.05e-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: 134.25  E-value: 3.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDesaGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCF 95
Cdd:cd05636     8 VEEGVTIK---GPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNY 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626990291  96 IADSVVANQAYLGAQVRTSNHRLDEQPVSVRTPEGIIATGCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIVE 174
Cdd:cd05636    85 VGDSVLGENVNLGAGTITANLRFDDKPVKVRLKGERVDTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 27-173 2.02e-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: 133.10  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  27 GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 106
Cdd:TIGR03992 247 GPVVIGEGAVIRSGTYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCN 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626990291 107 LGAQVRTSNHRLDEQPVSVRTPEGIIATGCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIV 173
Cdd:TIGR03992 327 FGAGTKVANLRHDDKPVKVTVKGKRVDTGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 14-120 2.31e-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: 65.13  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  14 VQIAD--QVIIDesaGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIIsNGVKIGFATEIKNAVIEAEATIG 91
Cdd:cd03353     2 VTLIDpeTTYID---GDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIG-DGVVIKASSVIEGAVIGNGATVG 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1626990291  92 PQCFI-ADSVVANQAYLGAQVRTSNHRLDE 120
Cdd:cd03353    78 PFAHLrPGTVLGEGVHIGNFVEIKKSTIGE 107
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 11-115 3.05e-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: 64.75  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDESA--GEVVIGANTRICHGAVIQGpVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEA 88
Cdd:cd03353    31 EGKTVIGEDCVIGPNCviKDSTIGDGVVIKASSVIEG-AVIGNGATVGPFAHLRPGTVLGEGVHIGNFVEIKKSTIGEGS 109

                          90       100
                  ....*....|....*....|....*..
gi 1626990291  89 TIGPQCFIADSVVANQAYLGAQVRTSN 115
Cdd:cd03353   110 KANHLSYLGDAEIGEGVNIGAGTITCN 136
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-115 8.10e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 65.62  E-value: 8.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDEsagEVVIGANTRIC-----HGAVIQGPVV----IGANCLIGNYAFIRPGTIISNGVKIGFATEIKN 81
Cdd:PRK14354  275 EPGVVIKGNTVIGE---DCVIGPGSRIVdstigDGVTITNSVIeeskVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKK 351

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1626990291  82 AVIEAEATIGPQCFIADSVVANQAYLGAQVRTSN 115
Cdd:PRK14354  352 STIGEGTKVSHLTYIGDAEVGENVNIGCGTITVN 385
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-103 1.98e-12

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: 64.66  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  13 NVQIADQVIIDEsagEVVIGANTRIC-----HGAVIQGPV----VIGANCLIGNYAFIRPGTIISNGVKIG-FAtEIKNA 82
Cdd:COG1207   278 NVILEGKTVIGE---GVVIGPNCTLKdstigDGVVIKYSViedaVVGAGATVGPFARLRPGTVLGEGVKIGnFV-EVKNS 353

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1626990291  83 VIEAE-----------ATIGPQCFI-ADSVVAN 103
Cdd:COG1207   354 TIGEGskvnhlsyigdAEIGEGVNIgAGTITCN 386
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-115 1.42e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 62.19  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  29 VVIGANTRICHGAVIQG-----PVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVAN 103
Cdd:PRK14353  281 VVFGPGVTVASGAVIHAfshleGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGA 360

                          90
                  ....*....|..
gi 1626990291 104 QAYLGAQVRTSN 115
Cdd:PRK14353  361 GANIGAGTITCN 372
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 20-115 7.13e-11

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: 56.52  E-value: 7.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  20 VIIDESAGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfaTEIKNAVIEAEATIGPQCFIADS 99
Cdd:cd05635     3 AVLDAEDGPIYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIG--GEVEDSIIEGYSNKQHDGFLGHS 80

                          90
                  ....*....|....*.
gi 1626990291 100 VVANQAYLGAQVRTSN 115
Cdd:cd05635    81 YLGSWCNLGAGTNNSD 96
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 14-120 7.87e-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: 60.04  E-value: 7.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  14 VQIAD--QVIIDesaGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIGFaTEIKNAVIEAEATIG 91
Cdd:COG1207   253 VTIIDpaTTYID---GDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKY-SVIEDAVVGAGATVG 327

                          90       100       110
                  ....*....|....*....|....*....|
gi 1626990291  92 PQCFI-ADSVVANQAYLGAQVRTSNHRLDE 120
Cdd:COG1207   328 PFARLrPGTVLGEGVKIGNFVEVKNSTIGE 357
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-115 7.01e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 57.25  E-value: 7.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDESA---GEVVIGANTRICHGAVIQGPVV---------------IGANCLIGNYAFIRPGTIISNGVK 72
Cdd:PRK14360  260 SETVELGPDVIIEPQThlrGNTVIGSGCRIGPGSLIENSQIgenvtvlysvvsdsqIGDGVKIGPYAHLRPEAQIGSNCR 339

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1626990291  73 IGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLGAQVRTSN 115
Cdd:PRK14360  340 IGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITAN 382
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
29-181 5.80e-09

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 52.18  E-value: 5.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  29 VVIGANTRICHGAVIQGPVVIganclIGNYAFIRPGTIISNGVKIgfateiknavieaeaTIGPQCFIADsvvanqaylG 108
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGGNIT-----IGDNVYIGPGVTIDDPGGI---------------TIGDNVLIGP---------G 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626990291 109 AQVRTSNHRLDEQPVSVRTPEGIIatgcdklgcyIGKRSRLGVQVIILPGRIISPNTQLGPRVIVERNLPSGT 181
Cdd:COG0110    60 VTILTGNHPIDDPATFPLRTGPVT----------IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYA 122
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 29-101 1.66e-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: 52.03  E-value: 1.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626990291  29 VVIGANTRICHGAVIQGPVVIGANCLIGnyafirPGTIISNGVKIGfateiKNAVIEAEATIGPQCFIADSVV 101
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIG------PGVVIGDGVVIG-----DDCVIHPNVTIYEGCIIGDRVI 63
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 16-91 3.69e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.94  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDESA--GE-------VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEA 86
Cdd:COG1044    99 IHPSAVIDPSAkiGEgvsigpfAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIG-----DRVIIHS 173


                  ....*
gi 1626990291  87 EATIG 91
Cdd:COG1044   174 GAVIG 178
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-116 5.91e-08

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 51.57  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIdeSAGEV----VIGANTRICHGAVIQGPVViGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEA 86
Cdd:PRK09451  281 EGNVTLGNRVKI--GAGCVlkncVIGDDCEISPYSVVEDANL-GAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGK 357

                          90       100       110
                  ....*....|....*....|....*....|
gi 1626990291  87 EATIGPQCFIADSVVANQAYLGAQVRTSNH 116
Cdd:PRK09451  358 GSKAGHLTYLGDAEIGDNVNIGAGTITCNY 387
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 15-109 5.94e-08

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: 49.72  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  15 QIADQVIIDESA---GEVVIGANTRICHGAVIQG---PVVIGANCLIGNYAFIRP----GTIISNGVKIGfateiKNAVI 84
Cdd:cd04645     1 EIDPSAFIAPNAtviGDVTLGEGSSVWFGAVLRGdvnPIRIGERTNIQDGSVLHVdpgyPTIIGDNVTVG-----HGAVL 75

                          90       100
                  ....*....|....*....|....*.
gi 1626990291  85 EAeATIGPQCFIA-DSVVANQAYLGA 109
Cdd:cd04645    76 HG-CTIGDNCLIGmGAIILDGAVIGK 100
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 16-101 6.74e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.29  E-value: 6.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDESAgevVIGANTRICHGAVIqgpvviGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCF 95
Cdd:PRK00892  103 IHPSAVIDPSA---KIGEGVSIGPNAVI------GAGVVIGDGVVIGAGAVIGDGVKIG-----ADCRLHANVTIYHAVR 168


                  ....*.
gi 1626990291  96 IADSVV 101
Cdd:PRK00892  169 IGNRVI 174
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-116 9.81e-08

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 50.88  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  34 NTRICHGAVIQG-----PVVIGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLG 108
Cdd:PRK14356  304 DAVVSSGATIHSfshleGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIG 383


                  ....*...
gi 1626990291 109 AQVRTSNH 116
Cdd:PRK14356  384 AGTITCNY 391
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 15-111 1.12e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 49.26  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  15 QIADQVIIDESA---GEVVIGANTRICHGAVIQG---PVVIGANCLIGNYAFIR--PG--TIISNGVKIGfateiKNAVI 84
Cdd:COG0663    12 QIHPSAFVAPTAvviGDVTIGEDVSVWPGAVLRGdvgPIRIGEGSNIQDGVVLHvdPGypLTIGDDVTIG-----HGAIL 86

                          90       100
                  ....*....|....*....|....*...
gi 1626990291  85 EAeATIGPQCFIAD-SVVANQAYLGAQV 111
Cdd:COG0663    87 HG-CTIGDNVLIGMgAIVLDGAVIGDGS 113
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 20-101 1.16e-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: 49.79  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  20 VIIDESA---GEVVIGANTRICHGAVIQGPVVIGANCL------------IGNYAFIRPGTIISNGVKIGFATEI-KNAV 83
Cdd:cd03360    85 TLIHPSAvvsPSAVIGEGCVIMAGAVINPDARIGDNVIintgavighdcvIGDFVHIAPGVVLSGGVTIGEGAFIgAGAT 164

                          90
                  ....*....|....*....
gi 1626990291  84 IEAEATIGPQCFI-ADSVV 101
Cdd:cd03360   165 IIQGVTIGAGAIIgAGAVV 183
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 12-91 1.25e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.52  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  12 KNVQIADQVIIDesAGeVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIG 91
Cdd:PRK00892  111 PSAKIGEGVSIG--PN-AVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIG-----NRVIIHSGAVIG 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 13-95 1.65e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.33  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  13 NVQIADQVIIDESageVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGP 92
Cdd:cd03352     1 SAKIGENVSIGPN---AVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIG-----DRVIIHSGAVIGS 72


                  ...
gi 1626990291  93 QCF 95
Cdd:cd03352    73 DGF 75
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-101 3.43e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 47.56  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291   1 MKNYLKLNAK-EKNVQIADQVIIDEsaGEVVIGANTRICHGAVI--QGPVVIGANCLIGNYAFIRPGT------------ 65
Cdd:COG0110     1 MKLLLLFGARiGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNhpiddpatfplr 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1626990291  66 ----IISNGVKIGFateikNAVIEAEATIGPQCFI-ADSVV 101
Cdd:COG0110    79 tgpvTIGDDVWIGA-----GATILPGVTIGDGAVVgAGSVV 114
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 18-92 7.18e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.59  E-value: 7.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626990291  18 DQVIIDESageVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIGFATEIKNAVIEAEATIGP 92
Cdd:PRK14355  261 ETTYIDRG---VVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAGSVLEDSVVGDDVAIGP 331
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 26-125 8.48e-07

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 48.40  E-value: 8.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  26 AGEVVIGANTRICHGAVIQGPVV---------IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEA---------- 86
Cdd:PRK14352  293 GEDAVVGPDTTLTDVTVGEGASVvrthgseseIGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRgtkvphltyv 372

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1626990291  87 -EATIGPQCFI-ADSVVAN-------QAYLGAQVRTSNHRLDEQPVSV 125
Cdd:PRK14352  373 gDADIGEHSNIgASSVFVNydgvnkhRTTIGSHVRTGSDTMFVAPVTV 420
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 26-115 8.52e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 48.44  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  26 AGEVVIGANTRICHGAVIQGPVV----------IGANCLIGNYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCF 95
Cdd:PRK14358  292 ADGVTIGAYSVVTDSVLHEGAVIkphsvlegaeVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAY 371

                          90       100
                  ....*....|....*....|
gi 1626990291  96 IADSVVANQAYLGAQVRTSN 115
Cdd:PRK14358  372 LGDVTIGAETNVGAGTIVAN 391
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 13-92 1.44e-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: 45.87  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  13 NVQiaDQVIIDESAGE-VVIGANTRICHGAVIQGpvviganCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIG 91
Cdd:cd04645    46 NIQ--DGSVLHVDPGYpTIIGDNVTVGHGAVLHG-------CTIGDNCLIGMGAIILDGAVIG-----KGSIVAAGSLVP 111


                  .
gi 1626990291  92 P 92
Cdd:cd04645   112 P 112
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 30-101 2.83e-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: 2.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626990291  30 VIGANTRICHGAVIqGPVVIGANCLIGNYAFIRpGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVV 101
Cdd:cd03356     1 LIGESTVIGENAII-KNSVIGDNVRIGDGVTIT-NSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI 70
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 29-108 3.81e-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: 43.01  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  29 VVIGANTRICHGAVIQGPVVIGANCLIGNYAFIR--PGTIISNGVKIGfateiKNAVIEAEATIGPQCFIAD-SVVANQA 105
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaaTGPNEKNPTIIG-----DNVEIGANAVIHGGVKIGDnAVIGAGA 75


                  ...
gi 1626990291 106 YLG 108
Cdd:cd00208    76 VVT 78
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 30-109 5.05e-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: 44.54  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  30 VIGANTRICHGAVIQGPVVIGANCLIGNYAFIR----PGTIISNGVKI----------GFATEIKN-------AVIEAEA 88
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRadegTPIIIGANVNIqdgvvihaleGYSVWIGKnvsiahgAIVHGPA 83

                          90       100
                  ....*....|....*....|..
gi 1626990291  89 TIGPQCFIA-DSVVANqAYLGA 109
Cdd:cd00710    84 YIGDNCFIGfRSVVFN-AKVGD 104
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 31-74 5.44e-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: 43.64  E-value: 5.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1626990291  31 IGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG 74
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIG 44
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 12-56 5.91e-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: 44.54  E-value: 5.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1626990291  12 KNVQIADQVIIDESAG-EVVIGANTRICHGAVIQGPVVIGANCLIG 56
Cdd:cd00710    47 ANVNIQDGVVIHALEGySVWIGKNVSIAHGAIVHGPAYIGDNCFIG 92
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 11-108 6.50e-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: 45.01  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDESA---GEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIG 74
Cdd:COG1043    29 GPDVEIGDGTVIGSHVvieGPTTIGKNNRIFPFASIGEEpqdlkykgeptrLEIGDNNTIREFVTIHRGTVQGGGVtRIG 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1626990291  75 fateiKNAVIEAEATIGPQCFIADSVV-ANQAYLG 108
Cdd:COG1043   109 -----DDNLLMAYVHVAHDCVVGNNVIlANNATLA 138
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 21-77 9.46e-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: 44.73  E-value: 9.46e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1626990291  21 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG-FAT 77
Cdd:cd03351     7 IVDPGA---KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFpFAS 61
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 11-116 1.10e-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: 44.35  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDESA---GEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIG 74
Cdd:cd03351    27 GPNVEIGDGTVIGSHVvidGPTTIGKNNRIFPFASIGEApqdlkykgeptrLEIGDNNTIREFVTIHRGTAQGGGVtRIG 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1626990291  75 fateiKNAVIEAEATIGPQCFIADSVV-ANQAYLGAQVRTSNH 116
Cdd:cd03351   107 -----NNNLLMAYVHVAHDCVIGNNVIlANNATLAGHVEIGDY 144
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
11-108 1.13e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.32  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIADQVIIDESA---GEVVIGANTRICHGAVIQGP------------VVIGANCLIGNYAFIRPGTIISNGV-KIG 74
Cdd:PRK05289   30 GPNVVIGDGTVIGSHVvidGHTTIGKNNRIFPFASIGEDpqdlkykgeptrLVIGDNNTIREFVTINRGTVQGGGVtRIG 109

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1626990291  75 fateiKNAVIEAEATIGPQCFIADSVV-ANQAYLG 108
Cdd:PRK05289  110 -----DNNLLMAYVHVAHDCVVGNHVIlANNATLA 139
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 12-61 1.32e-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: 44.35  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1626990291  12 KNVQIADQVIIDEsagEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFI 61
Cdd:cd03351    16 ENVEIGPFCVIGP---NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 33-101 1.62e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.36  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626990291  33 ANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCFIADSVV 101
Cdd:PRK00892   99 PAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIG-----AGAVIGDGVKIGADCRLHANVT 162
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
21-73 2.03e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.55  E-value: 2.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1626990291  21 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKI 73
Cdd:PRK05289   10 IVEPGA---KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRI 59
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 12-61 2.06e-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: 43.85  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1626990291  12 KNVQIADQVIIDEsagEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFI 61
Cdd:COG1043    18 ENVEIGPFCVIGP---DVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 30-101 2.35e-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: 41.02  E-value: 2.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626990291  30 VIGANTRICHGAVIQGPVvIGANCLIGNY-----AFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVV 101
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSV-IGRNCKIGKNvvidnSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVV 76
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 12-112 2.59e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.47  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  12 KNVQIADQVIIdesAGEVVIGANTRICHGAVIQGPVVIGANC------------------------LIGNYAFIRPGTII 67
Cdd:PRK12461   16 SGVEIGPFAVI---GANVEIGDGTWIGPHAVILGPTRIGKNNkihqgavvgdepqdftykgeesrlEIGDRNVIREGVTI 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1626990291  68 SNGVKIGFATEIKNA-VIEAEATIGPQCFIADSVV-ANQAYLGAQVR 112
Cdd:PRK12461   93 HRGTKGGGVTRIGNDnLLMAYSHVAHDCQIGNNVIlVNGALLAGHVT 139
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 16-98 3.23e-05

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: 40.69  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  16 IADQVIIDESA--GEVVIGANTRICHGAVIQGPVVIGaNCLIGNYAFIRpGTIISNGVKIGfateiKNAVIEAEATIGPQ 93
Cdd:cd03356     2 IGESTVIGENAiiKNSVIGDNVRIGDGVTITNSILMD-NVTIGANSVIV-DSIIGDNAVIG-----ENVRVVNLCIIGDD 74


                  ....*
gi 1626990291  94 CFIAD 98
Cdd:cd03356    75 VVVED 79
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
11-61 3.54e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 3.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1626990291  11 EKNVQIADQVIIDESA---GEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFI 61
Cdd:PRK05289   12 EPGAKIGENVEIGPFCvigPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 21-77 3.84e-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: 42.70  E-value: 3.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1626990291  21 IIDESAgevVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG-FAT 77
Cdd:COG1043     9 IVDPGA---KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFpFAS 63
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 13-74 4.76e-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: 40.25  E-value: 4.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626990291  13 NVQIADQVIIDESA--GEVVIGANTRIcHGAVIQGPVVIGANCLIGnyafirPGTIISNGVKIG 74
Cdd:cd05787    22 NCKIGKNVVIDNSYiwDDVTIEDGCTI-HHSIVADGAVIGKGCTIP------PGSLISFGVVIG 78
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-116 8.33e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.44  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  31 IGANTRI----CHGAVIQGPVVIGAnclignYAFIRPGTIISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAY 106
Cdd:PRK14357  293 IGNNVKIirseCEKSVIEDDVSVGP------FSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVN 366

                          90
                  ....*....|
gi 1626990291 107 LGAQVRTSNH 116
Cdd:PRK14357  367 IGAGTITCNY 376
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 21-73 1.53e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1626990291  21 IIDESAGevvIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKI 73
Cdd:PRK12461    7 VIDPSAK---LGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKI 56
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 11-74 1.82e-04

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: 39.36  E-value: 1.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626990291  11 EKNVQIADQVIIdeSAGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG 74
Cdd:cd04647    25 GDNVLIGPNVTI--YDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVG 86
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
29-57 2.81e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 2.81e-04
                          10        20
                  ....*....|....*....|....*....
gi 1626990291  29 VVIGANTRICHGAVIQGPVVIGANCLIGN 57
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 80-173 5.25e-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: 39.62  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  80 KNAVIEAEATIGPQCFI-ADSVVANQAYLGAqvrtsnhrldeqpvsvrtpegiiatgcdklGCYIGKRSRLGVQVIILPG 158
Cdd:COG1044   107 PSAKIGEGVSIGPFAVIgAGVVIGDGVVIGP------------------------------GVVIGDGVVIGDDCVLHPN 156

                          90
                  ....*....|....*
gi 1626990291 159 RIISPNTQLGPRVIV 173
Cdd:COG1044   157 VTIYERCVIGDRVII 171
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
41-96 6.86e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 6.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1626990291  41 AVIQGPVVIGANCLIGnyafirPGTIISNGVKIGFATEIK-NAVIEAEATIGPQCFI 96
Cdd:PRK05289    9 AIVEPGAKIGENVEIG------PFCVIGPNVVIGDGTVIGsHVVIDGHTTIGKNNRI 59
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 29-92 1.24e-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: 38.56  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626990291  29 VVIGANTRICHGAVIQG--------PVVIGANCLIGNyafirpGTIISNGVKIGfateiKNAVIEAEATIGP 92
Cdd:COG2171   145 AQIGKNVHLSGGAGIGGvleplqaaPVIIEDNCFIGA------RSGVVEGVIVG-----EGAVLGAGVYLTA 205
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 66-112 1.29e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 1.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1626990291  66 IISNGVKIGFATEIKNAVIEAEATIGPQCFIADSVVANQAYLGAQVR 112
Cdd:PRK05293  310 VLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 12-61 1.57e-03

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: 36.07  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1626990291  12 KNVQIADQVII-----DESAGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFI 61
Cdd:cd00208    23 DNVNIGPGAVIgaatgPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 55-181 1.73e-03

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 36.43  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  55 IGNYAFIRPGTIISNGVKIgfateiknavieaeaTIGPqcfiaDSVVANQAYLGA---QVRTSNHRLDEQPVsvrtpegi 131
Cdd:cd05825     6 IGDNSWIGEGVWIYNLAPV---------------TIGS-----DACISQGAYLCTgshDYRSPAFPLITAPI-------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1626990291 132 iatgcdklgcYIGKRSRLGVQVIILPGRIISPNTQLGPRVIVERNLPSGT 181
Cdd:cd05825    58 ----------VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWT 97
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 55-181 1.76e-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: 36.67  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  55 IGNYAFIRPGTIISNGVKIgfateiknavieaeaTIGPQCFIADSVvanqaylgaQVRTSNHRLDEqpvsvrtPEGIIAT 134
Cdd:cd04647     4 IGDNVYIGPGCVISAGGGI---------------TIGDNVLIGPNV---------TIYDHNHDIDD-------PERPIEQ 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1626990291 135 GCDKLGCYIGKRSRLGVQVIILPGRIISPNTQLGPRVIVERNLPSGT 181
Cdd:cd04647    53 GVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNS 99
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-92 1.87e-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: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  11 EKNVQIAD--QVIIDESageVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRpGTIISNGVKIgFATEIKNAVIEAEA 88
Cdd:PRK14357  239 ENGVTILDpnTTYIHYD---VEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIV-DCEIGNNVKI-IRSECEKSVIEDDV 313


                  ....
gi 1626990291  89 TIGP 92
Cdd:PRK14357  314 SVGP 317
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 13-74 1.97e-03

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 36.43  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  13 NVQIADQVIIDESA-----GEVVIGANTRICHGA---------------VIQGPVVIGANCLIGNYAFIRPGTIISNGVK 72
Cdd:cd05825     3 NLTIGDNSWIGEGVwiynlAPVTIGSDACISQGAylctgshdyrspafpLITAPIVIGDGAWVAAEAFVGPGVTIGEGAV 82


                  ..
gi 1626990291  73 IG 74
Cdd:cd05825    83 VG 84
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 29-101 2.92e-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: 35.90  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  29 VVIGANTRICHGAVIQ--GPVVIGANCLIGNYAFIRPG-------------------TIISNGVKIGFateikNAVIEAE 87
Cdd:cd04647     2 ISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapIVIGDDVWIGA-----NVVILPG 76

                          90
                  ....*....|....*
gi 1626990291  88 ATIGPQCFI-ADSVV 101
Cdd:cd04647    77 VTIGDGAVVgAGSVV 91
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 16-74 4.08e-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: 36.62  E-value: 4.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626990291  16 IADQVIID---ESAGEVVIGANTRICHGAVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIG 74
Cdd:cd03352   117 IGDGTKIDnlvQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 41-96 5.22e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 36.64  E-value: 5.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1626990291  41 AVIQGPVVIGANCLIGNYAFIRPGTIISNGVKIGfateiKNAVIEAEATIGPQCFI 96
Cdd:cd03351     6 AIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIG-----SHVVIDGPTTIGKNNRI 56
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
46-74 6.24e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 6.24e-03
                          10        20
                  ....*....|....*....|....*....
gi 1626990291  46 PVVIGANCLIGNYAFIRPGTIISNGVKIG 74
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 27-98 8.19e-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: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626990291  27 GEVVIGANTRICHGAVI---QGPVVIGANCLIGNYAFIR----PGTIISNGVKIG-----------FATEI-KNAVIEAE 87
Cdd:cd04646    16 GDVTIGPGTVVHPRATIiaeAGPIIIGENNIIEEQVTIVnkkpKDPAEPKPMIIGsnnvfevgckcEALKIgNNNVFESK 95

                          90
                  ....*....|.
gi 1626990291  88 ATIGPQCFIAD 98
Cdd:cd04646    96 SFVGKNVIITD 106
 
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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