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Conserved domains on  [gi|1063725715|ref|NP_001329097|]
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bacterial transferase hexapeptide repeat-containing protein [Arabidopsis thaliana]

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 ...
12-230 2.21e-105

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 cd03351:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 254  Bit Score: 304.74  E-value: 2.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:cd03351    46 GPTTIGKNNRIFPFASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:cd03351   125 NNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSRE 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGI 230
Cdd:cd03351   205 EIRALKRAYRILYRS----GLTLEEALEELE--EEAPDSPEVEELVDFIR----SSKRGI 254
 
Name Accession Description Interval E-value
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
12-230 2.21e-105

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: 304.74  E-value: 2.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:cd03351    46 GPTTIGKNNRIFPFASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:cd03351   125 NNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSRE 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGI 230
Cdd:cd03351   205 EIRALKRAYRILYRS----GLTLEEALEELE--EEAPDSPEVEELVDFIR----SSKRGI 254
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
12-232 2.81e-101

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: 294.62  E-value: 2.81e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:COG1043    48 GPTTIGKNNRIFPFASIGEEPQDLKYK-GEPTRLEIGDNNTIREFVTIHRgTVQGGGVTRIGDDNLLMAYVHVAHDCVVG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:COG1043   127 NNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSRE 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGICK 232
Cdd:COG1043   207 QIRALKRAYRLLYRS----GLTLEEALEELE--AELPDSPEVRELLDFIR----ASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
12-234 2.48e-100

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 292.39  E-value: 2.48e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:PRK05289   49 GHTTIGKNNRIFPFASIGEDPQDLKYK-GEPTRLVIGDNNTIREFVTINRgTVQGGGVTRIGDNNLLMAYVHVAHDCVVG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:PRK05289  128 NHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSRE 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGICKFR 234
Cdd:PRK05289  208 EIHALRRAYKLLYRS----GLTLEEALEELA--EEYPDSPEVKEILDFIE----SSKRGIIRPR 261
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
12-231 1.09e-80

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 242.17  E-value: 1.09e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:TIGR01852  45 GHTTIGEGTRIFPGAVIGGVPQDLKYK-GEKTRLIIGDNNTIREFVTINRGTASGGgVTRIGNNNLLMAYSHIAHDCVVG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:TIGR01852 124 NHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSRE 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063725715 171 EMKSLRAAYRKIFMSTetvsLSFEERLTELEQDQElySVPAVSAMLQSIRdsftESRRGIC 231
Cdd:TIGR01852 204 EITAIKRAYRTLFRSG----LPLREAAQQVAEEYE--DNPEVKEILDFIR----ESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
140-231 1.25e-29

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 106.01  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715 140 DVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMStetvSLSFEERLTELEQDQELYsvPAVSAMLQSI 219
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRS----GLTLEEALEELEEEVPDS--PEVQEILDFI 74
                          90
                  ....*....|..
gi 1063725715 220 RdsftESRRGIC 231
Cdd:pfam13720  75 R----SSKRGII 82
 
Name Accession Description Interval E-value
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
12-230 2.21e-105

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: 304.74  E-value: 2.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:cd03351    46 GPTTIGKNNRIFPFASIGEAPQDLKYK-GEPTRLEIGDNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:cd03351   125 NNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSRE 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGI 230
Cdd:cd03351   205 EIRALKRAYRILYRS----GLTLEEALEELE--EEAPDSPEVEELVDFIR----SSKRGI 254
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
12-232 2.81e-101

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: 294.62  E-value: 2.81e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:COG1043    48 GPTTIGKNNRIFPFASIGEEPQDLKYK-GEPTRLEIGDNNTIREFVTIHRgTVQGGGVTRIGDDNLLMAYVHVAHDCVVG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:COG1043   127 NNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSRE 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGICK 232
Cdd:COG1043   207 QIRALKRAYRLLYRS----GLTLEEALEELE--AELPDSPEVRELLDFIR----ASKRGIIR 258
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
12-234 2.48e-100

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 292.39  E-value: 2.48e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHR-SSKPSDKTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:PRK05289   49 GHTTIGKNNRIFPFASIGEDPQDLKYK-GEPTRLVIGDNNTIREFVTINRgTVQGGGVTRIGDNNLLMAYVHVAHDCVVG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:PRK05289  128 NHVILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSRE 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063725715 171 EMKSLRAAYRKIFMStetvSLSFEERLTELEqdQELYSVPAVSAMLQSIRdsftESRRGICKFR 234
Cdd:PRK05289  208 EIHALRRAYKLLYRS----GLTLEEALEELA--EEYPDSPEVKEILDFIE----SSKRGIIRPR 261
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
12-231 1.09e-80

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 242.17  E-value: 1.09e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  12 GYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSD-KTVIGDNNLIMGSCHIAHDCKIG 90
Cdd:TIGR01852  45 GHTTIGEGTRIFPGAVIGGVPQDLKYK-GEKTRLIIGDNNTIREFVTINRGTASGGgVTRIGNNNLLMAYSHIAHDCVVG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMS 170
Cdd:TIGR01852 124 NHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSRE 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063725715 171 EMKSLRAAYRKIFMSTetvsLSFEERLTELEQDQElySVPAVSAMLQSIRdsftESRRGIC 231
Cdd:TIGR01852 204 EITAIKRAYRTLFRSG----LPLREAAQQVAEEYE--DNPEVKEILDFIR----ESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
1-232 3.43e-73

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 223.36  E-value: 3.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715   1 MTGAVVGdelpGYTFIGCNNIIGHHAVVGVKCQDLKYKhGDECFLCIGNNNEIREFCSIHRSSKPSDKTVIGDNNLIMGS 80
Cdd:PRK12461   39 GPHAVIL----GPTRIGKNNKIHQGAVVGDEPQDFTYK-GEESRLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAY 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  81 CHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLE 160
Cdd:PRK12461  114 SHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAV 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063725715 161 GLRRNGFTMSEMKSLRAAYRKIFMStetvSLSFEERLTELEQDQElysvpaVSAMLQSIRDSFTESRRGICK 232
Cdd:PRK12461  194 GLRRRGFSSRAIRALKRAYKIIYRS----GLSVQQAVAELELQQF------ESPEVEELIDFIKASKRGIVR 255
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
140-231 1.25e-29

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 106.01  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715 140 DVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMStetvSLSFEERLTELEQDQELYsvPAVSAMLQSI 219
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRS----GLTLEEALEELEEEVPDS--PEVQEILDFI 74
                          90
                  ....*....|..
gi 1063725715 220 RdsftESRRGIC 231
Cdd:pfam13720  75 R----SSKRGII 82
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
4-149 3.51e-19

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: 82.15  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715   4 AVVGDELPGYTFIGCNNIIGHHAVVgvkcqDLKYKHGDECFLCIGNNN---EIREFCS---------IHRSSKPSD---- 67
Cdd:cd03360    25 GFLDDDPELKGTEGLGLPVGLDELL-----LLYPPPDDEFVVAIGDNKlrrKLAEKLLaagyrfatlIHPSAVVSPsavi 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  68 --------------KTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGG 133
Cdd:cd03360   100 gegcvimagavinpDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGA 179
                         170
                  ....*....|....*.
gi 1063725715 134 GSVVSQDVPKYMMVAG 149
Cdd:cd03360   180 GAVVTKDVPDGSVVVG 195
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
3-149 4.26e-18

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: 79.37  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715   3 GAVVGDElpgyTFIGCNNIIGHHAVVGVKCqdlkYKH-----GDECFLC-----------------IGNNNEIREFCSIH 60
Cdd:cd03352    37 GVVIGDD----CVIHPNVTIYEGCIIGDRV----IIHsgaviGSDGFGFapdgggwvkipqlggviIGDDVEIGANTTID 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  61 RSSKpsDKTVIGDN----NLimgsCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSV 136
Cdd:cd03352   109 RGAL--GDTVIGDGtkidNL----VQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSG 182
                         170
                  ....*....|...
gi 1063725715 137 VSQDVPKYMMVAG 149
Cdd:cd03352   183 VTSIVPPGEYVSG 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
11-149 8.39e-18

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 78.69  E-value: 8.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  11 PGYTFIgcnNIIGHHAVVGVKCQdlkykhgdecflcIGNNNEIREFCSIHRSSKpsdktvIGDNNLIMGSCHIAHDCKIG 90
Cdd:TIGR03570  82 KGYRFA---TLIHPSAIVSPSAS-------------IGEGTVIMAGAVINPDVR------IGDNVIINTGAIVEHDCVIG 139
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  91 DRNIFANNTLLAGHVVVEDNTHT-AGASVVHQfCHIGSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:TIGR03570 140 DFVHIAPGVTLSGGVVIGEGVFIgAGATIIQG-VTIGAGAIVGAGAVVTKDIPDGGVVVG 198
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
47-149 5.60e-13

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 64.12  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHRSskpsdKTVIGDNNLIMGSCHI--AHDCKIGDRNIFANNTLL----------------AGHVVVE 108
Cdd:COG0110    11 IGDGVVIGPGVRIYGG-----NITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIG 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063725715 109 DNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:COG0110    86 DDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAG 126
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
47-149 2.09e-11

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: 62.34  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHRSSkpSDKTVIGDN----NLImgscHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVV--H 120
Cdd:COG1044   203 IGDDVEIGANTTIDRGA--LGDTVIGDGtkidNLV----QIAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIagH 276
                          90       100
                  ....*....|....*....|....*....
gi 1063725715 121 qfCHIGSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:COG1044   277 --LTIGDGVIIGAQSGVTKSIPEGGVYSG 303
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
47-143 4.55e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.69  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHRSSkpSDKTVIGDN----NLimgsCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQF 122
Cdd:PRK00892  206 IGDDVEIGANTTIDRGA--LDDTVIGEGvkidNL----VQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGH 279
                          90       100
                  ....*....|....*....|.
gi 1063725715 123 CHIGSFAFIGGGSVVSQDVPK 143
Cdd:PRK00892  280 LEIGDGVTITAMSGVTKSIPE 300
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
47-149 7.16e-10

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: 54.77  E-value: 7.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHrsskPSDKTVIGDNNLIMGSCHI-AHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHI 125
Cdd:cd04647     4 IGDNVYIGPGCVIS----AGGGITIGDNVLIGPNVTIyDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTI 79
                          90       100
                  ....*....|....*....|....
gi 1063725715 126 GSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:cd04647    80 GDGAVVGAGSVVTKDVPPNSIVAG 103
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
71-156 7.52e-10

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: 55.20  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  71 IGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVED-----------NTHTAGAS----------VVHQFC------ 123
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDdvfigpnvvftNDLYPRSKiyrkwelkgtTVKRGAsigana 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063725715 124 ------HIGSFAFIGGGSVVSQDVPKYMMVAGERAELRG 156
Cdd:cd03358    81 tilpgvTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
68-149 6.09e-07

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 46.66  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  68 KTVIGDNnlimgsCHIAHDCKIGDRNIFANNtllaGHVVVEDNTHT-AGASVVHQfCHIGSFAFIGGGSVVSQDVPKYMM 146
Cdd:cd03354    28 TAVIGDN------CTIYQGVTLGGKGKGGGK----RHPTIGDNVVIgAGAKILGN-ITIGDNVKIGANAVVTKDVPANST 96

                  ...
gi 1063725715 147 VAG 149
Cdd:cd03354    97 VVG 99
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
40-149 7.07e-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: 44.71  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  40 GDECFLCIGNNNEIREFCSIHRSskPSDKTVIGDNNLImGSCHIAHDCKIGDRnifanntllaghVVVEDNthtagaSVV 119
Cdd:cd04645    34 GDVNPIRIGERTNIQDGSVLHVD--PGYPTIIGDNVTV-GHGAVLHGCTIGDN------------CLIGMG------AII 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063725715 120 HQFCHIGSFAFIGGGSVVSQD--VPKYMMVAG 149
Cdd:cd04645    93 LDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAG 124
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
68-156 1.12e-05

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 44.30  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  68 KTVIGDNnlimgsCHIAHDCKIGDRNIFANNtllaGHVVVEDNTHT-AGASV---VHqfchIGSFAFIGGGSVVSQDVPK 143
Cdd:COG1045    91 TAVIGDN------VTIYQGVTLGGTGKEKGK----RHPTIGDNVVIgAGAKIlgpIT----IGDNAKIGANSVVLKDVPP 156
                          90
                  ....*....|...
gi 1063725715 144 YMMVAGERAELRG 156
Cdd:COG1045   157 GSTVVGVPARIVK 169
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
68-97 1.29e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.78  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1063725715  68 KTVIGDNNLIMGSCHIAHDCKIGDRNIFAN 97
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
40-165 1.55e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.86  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  40 GDECFLCIGNNNEIREFCSIHrsSKPSDKTVIGDNnlimgsCHIAHD-----CKIGDRnifanntllaghVVVEDNthta 114
Cdd:COG0663    45 GDVGPIRIGEGSNIQDGVVLH--VDPGYPLTIGDD------VTIGHGailhgCTIGDN------------VLIGMG---- 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063725715 115 gaSVVHQFCHIGSFAFIGGGSVVSQD--VPKYMMVAGERAE-LRGLN---LEGLRRN 165
Cdd:COG0663   101 --AIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKvVRELTeeeIAFLRES 155
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
69-141 2.50e-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: 41.41  E-value: 2.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063725715  69 TVIGDNNLIMGSChIAHDCKIGDrNIFANNTLLAGHVVVEDNTHTAGaSVVHQFCHIGSFAFIGGGSVVSQDV 141
Cdd:cd05787     6 TSIGEGTTIKNSV-IGRNCKIGK-NVVIDNSYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLISFGV 75
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
69-141 4.42e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 42.79  E-value: 4.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063725715  69 TVIGDNNLIMGSCHIAHDCKIGDrNIFANNTLLAGHVVVEDNTHTAGaSVVHQFCHIGSFAFIGGGSVVSQDV 141
Cdd:cd03353    22 VVIDPGVILEGKTVIGEDCVIGP-NCVIKDSTIGDGVVIKASSVIEG-AVIGNGATVGPFAHLRPGTVLGEGV 92
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
67-149 9.11e-05

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: 40.67  E-value: 9.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  67 DKTVIGDNNLI--MGSCHIAHDCKI--------GDRNI----FAnntLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIG 132
Cdd:cd05825     8 DNSWIGEGVWIynLAPVTIGSDACIsqgaylctGSHDYrspaFP---LITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVG 84
                          90
                  ....*....|....*..
gi 1063725715 133 GGSVVSQDVPKYMMVAG 149
Cdd:cd05825    85 ARSVVVRDLPAWTVYAG 101
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
66-155 9.83e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 9.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  66 SDKTVIGDNNLImGSC-HIAHDCKIGdrnifaNNTLLAG--------HVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSV 136
Cdd:cd03350    35 DEGTMVDSWATV-GSCaQIGKNVHLS------AGAVIGGvleplqatPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVV 107
                          90
                  ....*....|....*....
gi 1063725715 137 VSQDVPKYMMVAGERAELR 155
Cdd:cd03350   108 LTQSTPIYDRETGEIYYGR 126
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
67-137 1.38e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.15  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063725715  67 DKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNT--LLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVV 137
Cdd:cd00208     5 EGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATgpNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
47-140 1.51e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHrsskpsDKTVIGDNNLIMGSCHIAHDCKIGDrnifanNTLLAGHVvvednthtagasVVHQFCHIG 126
Cdd:COG1044   111 IGEGVSIGPFAVIG------AGVVIGDGVVIGPGVVIGDGVVIGD------DCVLHPNV------------TIYERCVIG 166
                          90
                  ....*....|....
gi 1063725715 127 SFAFIGGGSVVSQD 140
Cdd:COG1044   167 DRVIIHSGAVIGAD 180
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
47-141 1.60e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 39.15  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHRSskpsdktVIGDNnlimgschiahdCKIGDrNIFANNTLLAGHVVVEDNTHTAGaSVVHQFCHIG 126
Cdd:cd03356     2 IGESTVIGENAIIKNS-------VIGDN------------VRIGD-GVTITNSILMDNVTIGANSVIVD-SIIGDNAVIG 60
                          90
                  ....*....|....*
gi 1063725715 127 SFAFIGGGSVVSQDV 141
Cdd:cd03356    61 ENVRVVNLCIIGDDV 75
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
71-149 5.60e-04

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 39.33  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  71 IGDNnlimgsCHIAHDC--------KIGDRNIFANNTLL--AGH----------------VVVEDNTHTAGASVVHQFCH 124
Cdd:cd03357    65 IGDN------FYANFNCtildvapvTIGDNVLIGPNVQIytAGHpldpeernrgleyakpITIGDNVWIGGGVIILPGVT 138
                          90       100
                  ....*....|....*....|....*
gi 1063725715 125 IGSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:cd03357   139 IGDNSVIGAGSVVTKDIPANVVAAG 163
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
68-141 7.47e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.01  E-value: 7.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063725715  68 KTVIGDNNLIMGSCHIaHDCKIGDrnifanntllagHVVVEdNTHTAGaSVVHQFCHIGSFAFIGGGSVVSQDV 141
Cdd:COG1207   284 KTVIGEGVVIGPNCTL-KDSTIGD------------GVVIK-YSVIED-AVVGAGATVGPFARLRPGTVLGEGV 342
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
47-137 1.93e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.02  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREFCSIHRSskpsdktVIGDNnlimgschiahdCKIGDRNIFANNTLLaGHVVVEDNthtagasVVHQFCHIG 126
Cdd:cd04652     2 VGENTQVGEKTSIKRS-------VIGAN------------CKIGKRVKITNCVIM-DNVTIEDG-------CTLENCIIG 54
                          90
                  ....*....|.
gi 1063725715 127 SFAFIGGGSVV 137
Cdd:cd04652    55 NGAVIGEKCKL 65
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
70-134 3.31e-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: 37.39  E-value: 3.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063725715  70 VIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGS----FAFIGGG 134
Cdd:cd03352    15 VIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgFAPDGGG 83
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
15-107 3.95e-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: 35.30  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  15 FIGCNNIIGHHAVVGVKCqdlkykhgdecflCIGNNNEIREFCSIHRSSKPSDK--TVIGDNNLIMGSCHIAHDCKIGDr 92
Cdd:cd00208     2 FIGEGVKIHPKAVIRGPV-------------VIGDNVNIGPGAVIGAATGPNEKnpTIIGDNVEIGANAVIHGGVKIGD- 67
                          90
                  ....*....|....*
gi 1063725715  93 nifanNTLLAGHVVV 107
Cdd:cd00208    68 -----NAVIGAGAVV 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
70-140 5.02e-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: 37.00  E-value: 5.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063725715  70 VIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQD 140
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSD 73
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
15-91 6.18e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.91  E-value: 6.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063725715  15 FIGCNNIIGHHAVVgvkcqdlkykhgDECFlcIGNNNEIREFCSIhRSSKPSDKTVIGDNNLIMGSCHIAHDCKIGD 91
Cdd:cd03356    18 VIGDNVRIGDGVTI------------TNSI--LMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
47-166 6.65e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.44  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  47 IGNNNEIREfCSIHRSSKPSDKTVIGDnnlimgsCHIAHDCKIGDRNIFANNTLLAGH-VVVEDNTHTAGASVVHQFCHI 125
Cdd:PRK14357  333 IGNFVEIKK-STIGENTKAQHLTYLGD-------ATVGKNVNIGAGTITCNYDGKKKNpTFIEDGAFIGSNSSLVAPVRI 404
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063725715 126 GSFAFIGGGSVVSQDVPKYMMVAGeRAelRGLNLEG--LRRNG 166
Cdd:PRK14357  405 GKGALIGAGSVITEDVPPYSLALG-RA--RQIVKEGwvLKKRK 444
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
124-149 7.35e-03

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 35.98  E-value: 7.35e-03
                          10        20
                  ....*....|....*....|....*.
gi 1063725715 124 HIGSFAFIGGGSVVSQDVPKYMMVAG 149
Cdd:cd03349    93 TIGDGAVIAAGAVVTKDVPPYAIVGG 118
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
59-140 7.44e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725715  59 IHRSSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTH-TAGASVVHQfCHIGSFAFIGGGSVV 137
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRlHANVTIYHA-VRIGNRVIIHSGAVI 181

                  ...
gi 1063725715 138 SQD 140
Cdd:PRK00892  182 GSD 184
 
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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