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Conserved domains on  [gi|1519714017|gb|RPG83664|]
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MAG: acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase [Coraliomargarita sp. TMED73]

Protein Classification

UDP-N-acetylglucosamine O-acyltransferase( domain architecture ID 11437198)

UDP-N-acetylglucosamine O-acyltransferase catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc, the first step of lipid A biosynthetic pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 2-258 4.49e-125

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: 355.48  E-value: 4.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRL 81
Cdd:COG1043     1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  82 EVGNGNTFREFTTVHCATSED-LVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVR 160
Cdd:COG1043    81 EIGDNNTIREFVTIHRGTVQGgGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 161 IGDHAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVH 240
Cdd:COG1043   161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELE-AELPDS 239

                         250
                  ....*....|....*...
gi 1519714017 241 PMARTFLDFAQSSERGLA 258
Cdd:COG1043   240 PEVRELLDFIRASKRGII 257
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 2-258 4.49e-125

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: 355.48  E-value: 4.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRL 81
Cdd:COG1043     1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  82 EVGNGNTFREFTTVHCATSED-LVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVR 160
Cdd:COG1043    81 EIGDNNTIREFVTIHRGTVQGgGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 161 IGDHAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVH 240
Cdd:COG1043   161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELE-AELPDS 239

                         250
                  ....*....|....*...
gi 1519714017 241 PMARTFLDFAQSSERGLA 258
Cdd:COG1043   240 PEVRELLDFIRASKRGII 257
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-257 1.28e-117

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 337.07  E-value: 1.28e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   1 MATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQR 80
Cdd:PRK05289    1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  81 LEVGNGNTFREFTTVHCATSEDL-VTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFV 159
Cdd:PRK05289   81 LVIGDNNTIREFVTINRGTVQGGgVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 160 RIGDHAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAV 239
Cdd:PRK05289  161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELA-EEYPD 239

                         250
                  ....*....|....*...
gi 1519714017 240 HPMARTFLDFAQSSERGL 257
Cdd:PRK05289  240 SPEVKEILDFIESSKRGI 257
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 5-257 3.52e-117

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: 335.56  E-value: 3.52e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRLEVG 84
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  85 NGNTFREFTTVHCATSEDL-VTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGD 163
Cdd:cd03351    82 DNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 164 HAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVHPMA 243
Cdd:cd03351   162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELE-EEAPDSPEV 240

                         250
                  ....*....|....
gi 1519714017 244 RTFLDFAQSSERGL 257
Cdd:cd03351   241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 5-258 2.04e-100

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: 293.01  E-value: 2.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRLEVG 84
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  85 NGNTFREFTTVHCAT-SEDLVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGD 163
Cdd:TIGR01852  81 DNNTIREFVTINRGTaSGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 164 HAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQssEDAVH-PM 242
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVA--EEYEDnPE 238

                         250
                  ....*....|....*.
gi 1519714017 243 ARTFLDFAQSSERGLA 258
Cdd:TIGR01852 239 VKEILDFIRESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 176-258 1.36e-30

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: 109.09  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 176 DVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVHPMARTFLDFAQSSER 255
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELE-EEVPDSPEVQEILDFIRSSKR 79


                  ...
gi 1519714017 256 GLA 258
Cdd:pfam13720  80 GII 82
 
Name Accession Description Interval E-value
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 2-258 4.49e-125

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: 355.48  E-value: 4.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRL 81
Cdd:COG1043     1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  82 EVGNGNTFREFTTVHCATSED-LVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVR 160
Cdd:COG1043    81 EIGDNNTIREFVTIHRGTVQGgGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 161 IGDHAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVH 240
Cdd:COG1043   161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELE-AELPDS 239

                         250
                  ....*....|....*...
gi 1519714017 241 PMARTFLDFAQSSERGLA 258
Cdd:COG1043   240 PEVRELLDFIRASKRGII 257
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-257 1.28e-117

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 337.07  E-value: 1.28e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   1 MATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQR 80
Cdd:PRK05289    1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  81 LEVGNGNTFREFTTVHCATSEDL-VTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFV 159
Cdd:PRK05289   81 LVIGDNNTIREFVTINRGTVQGGgVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 160 RIGDHAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAV 239
Cdd:PRK05289  161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELA-EEYPD 239

                         250
                  ....*....|....*...
gi 1519714017 240 HPMARTFLDFAQSSERGL 257
Cdd:PRK05289  240 SPEVKEILDFIESSKRGI 257
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 5-257 3.52e-117

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: 335.56  E-value: 3.52e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRLEVG 84
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  85 NGNTFREFTTVHCATSEDL-VTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGD 163
Cdd:cd03351    82 DNNTIREFVTIHRGTAQGGgVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 164 HAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVHPMA 243
Cdd:cd03351   162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELE-EEAPDSPEV 240

                         250
                  ....*....|....
gi 1519714017 244 RTFLDFAQSSERGL 257
Cdd:cd03351   241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 5-258 2.04e-100

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: 293.01  E-value: 2.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRLEVG 84
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  85 NGNTFREFTTVHCAT-SEDLVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGD 163
Cdd:TIGR01852  81 DNNTIREFVTINRGTaSGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 164 HAMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQssEDAVH-PM 242
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVA--EEYEDnPE 238

                         250
                  ....*....|....*.
gi 1519714017 243 ARTFLDFAQSSERGLA 258
Cdd:TIGR01852 239 VKEILDFIRESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 5-258 4.78e-93

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 274.21  E-value: 4.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVGGKTHDKKYTGGIQRLEVG 84
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  85 NGNTFREFTTVHCATSEDLVTRLGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGDH 164
Cdd:PRK12461   82 DRNVIREGVTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 165 AMVGASSKTVQDVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQSSeDAVHPMAR 244
Cdd:PRK12461  162 AMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQ-QFESPEVE 240

                         250
                  ....*....|....
gi 1519714017 245 TFLDFAQSSERGLA 258
Cdd:PRK12461  241 ELIDFIKASKRGIV 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 176-258 1.36e-30

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: 109.09  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 176 DVPPFCICDGNPATVRTINKIGLERAGYSSDEIALARRIYKLFYKDGLNRSQAIEQLQsSEDAVHPMARTFLDFAQSSER 255
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELE-EEVPDSPEVQEILDFIRSSKR 79


                  ...
gi 1519714017 256 GLA 258
Cdd:pfam13720  80 GII 82
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-179 5.68e-28

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: 108.95  E-value: 5.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATV-DGA-----------------TTLGHDNEVHP-- 61
Cdd:COG1044    96 APGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIgDGVvigddcvlhpnvtiyerCVIGDRVIIHSga 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  62 --------YAYVGGKTHDKKY-TGG--IQ-RLEVGNGntfrefTTVHCATSEDlvTRLGDH----NLIlaysHIAHECQV 125
Cdd:COG1044   176 vigadgfgFAPDEDGGWVKIPqLGRvvIGdDVEIGAN------TTIDRGALGD--TVIGDGtkidNLV----QIAHNVRI 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519714017 126 GNHLVMSSHAALGGHVIVGDHVNIAWGSGL--HqfVRIGDHAMVGASSKTVQDVPP 179
Cdd:COG1044   244 GEHTAIAAQVGIAGSTKIGDNVVIGGQVGIagH--LTIGDGVIIGAQSGVTKSIPE 297
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 5-188 3.03e-27

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: 104.03  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHP----------YAYVGGKTHDKKY 74
Cdd:cd03352    10 IGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSgavigsdgfgFAPDGGGWVKIPQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  75 TGGI---QRLEVGNGntfrefTTVHCATSEDlvTRLGDH----NLIlaysHIAHECQVGNHLVMSSHAALGGHVIVGDHV 147
Cdd:cd03352    90 LGGViigDDVEIGAN------TTIDRGALGD--TVIGDGtkidNLV----QIAHNVRIGENCLIAAQVGIAGSTTIGDNV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1519714017 148 NIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPA 188
Cdd:cd03352   158 IIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPA 198
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-179 2.84e-23

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 96.36  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHP-------------------- 61
Cdd:PRK00892  100 AAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAnvtiyhavrignrviihsga 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  62 ------YAYVGGK-THDK-KYTGG--IQ-RLEVGNGntfrefTTVHCATSEDlvTRLGDH----NLIlaysHIAHECQVG 126
Cdd:PRK00892  180 vigsdgFGFANDRgGWVKiPQLGRviIGdDVEIGAN------TTIDRGALDD--TVIGEGvkidNLV----QIAHNVVIG 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519714017 127 NHLVMSSHAALGGHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPP 179
Cdd:PRK00892  248 RHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPE 300
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 59-188 1.96e-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: 80.62  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  59 VHPYAYVGgkthdkkytggiQRLEVGNGNTFREFTTVHCATsedlvtRLGDHNLILAYSHIAHECQVGNHLVMSSHAALG 138
Cdd:TIGR03570  90 IHPSAIVS------------PSASIGEGTVIMAGAVINPDV------RIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLS 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519714017 139 GHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPA 188
Cdd:TIGR03570 152 GGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 59-187 3.60e-18

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: 79.84  E-value: 3.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  59 VHPYAYVGgkthdkkytggiQRLEVGNGNTFREFTTVHCATsedlvtRLGDHNLILAYSHIAHECQVGNHLVMSSHAALG 138
Cdd:cd03360    87 IHPSAVVS------------PSAVIGEGCVIMAGAVINPDA------RIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLS 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519714017 139 GHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNP 187
Cdd:cd03360   149 GGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
52-190 5.93e-11

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 58.73  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  52 TLGHDNEVHPYAYVGGKthdkkytggiqRLEVGNGNTFREFTTVHCATSedlvTRLGDHnlilaySHIAHECQV--GNHL 129
Cdd:COG0110    10 RIGDGVVIGPGVRIYGG-----------NITIGDNVYIGPGVTIDDPGG----ITIGDN------VLIGPGVTIltGNHP 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519714017 130 VMSSHAAL--GGHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPATV 190
Cdd:COG0110    69 IDDPATFPlrTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARV 131
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 80-190 4.75e-09

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: 52.84  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  80 RLEVGNGNTFREFTTVHCATSedlvTRLGDHnlilaySHIAHECQV--GNHLVMSSHAALGGH-----VIVGDHVNIAWG 152
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGG----ITIGDN------VLIGPNVTIydHNHDIDDPERPIEQGvtsapIVIGDDVWIGAN 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1519714017 153 SGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPATV 190
Cdd:cd04647    71 VVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKV 108
PRK10502 PRK10502
putative acyl transferase; Provisional
 107-191 2.98e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 49.18  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 107 LGDHNLI--------LAYSHIAHECQV--------GNHLVMSSHAAL-GGHVIVGDHVNIAWGSGLHQFVRIGDHAMVGA 169
Cdd:PRK10502   74 IGDYAWIgddvwlynLGEITIGAHCVIsqksylctGSHDYSDPHFDLnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGA 153

                          90       100
                  ....*....|....*....|..
gi 1519714017 170 SSKTVQDVPPFCICDGNPATVR 191
Cdd:PRK10502  154 RSSVFKSLPANTICRGNPAVPI 175
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 125-191 4.31e-07

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: 47.22  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 125 VGNHLVMSSHAAL--GGH-------------VIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPAT 189
Cdd:cd05825    26 IGSDACISQGAYLctGSHdyrspafplitapIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAV 105


                  ..
gi 1519714017 190 VR 191
Cdd:cd05825   106 PV 107
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 107-188 4.02e-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: 44.80  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 107 LGDHNLILAYSHIAHECQVGNHLVMSSHAALGGHVIVGDHVNIA----------WGSGLHQF------------------ 158
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGpnvvftndlyPRSKIYRKwelkgttvkrgasigana 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1519714017 159 -----VRIGDHAMVGASSKTVQDVPPFCICDGNPA 188
Cdd:cd03358    81 tilpgVTIGEYALVGAGAVVTKDVPPYALVVGNPA 115
PLN02694 PLN02694
serine O-acetyltransferase
 125-188 9.60e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 45.79  E-value: 9.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519714017 125 VGNHLVMSSHAALGG--------HVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPA 188
Cdd:PLN02694  189 IGNNVSILHHVTLGGtgkacgdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPA 260
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 139-190 2.09e-05

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: 43.30  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519714017 139 GHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPATV 190
Cdd:cd03349    72 GDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKV 123
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 118-190 4.82e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 42.88  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 118 HIAHECQV--GNHLVMSSH----------AALGGHVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDG 185
Cdd:PRK10092   95 RIGDNCMLapGVHIYTATHpldpvarnsgAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGG 174


                  ....*
gi 1519714017 186 NPATV 190
Cdd:PRK10092  175 NPARI 179
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 3-179 6.14e-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: 6.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   3 TEIHPAAIIEPGAELDEGVHVGAYAYIGaHVRIASGTHVMHHATVDGAtTLGHDNEVHPYAYVGGKTHDKKYTggiqrlE 82
Cdd:cd03353    22 VVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKASSVIEGA-VIGNGATVGPFAHLRPGTVLGEGV------H 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  83 VGNgntFREFTTvhcatsedlvTRLGDHnlilaySHIAHECQVGNhlvmsshAALGGHV-------------------IV 143
Cdd:cd03353    94 IGN---FVEIKK----------STIGEG------SKANHLSYLGD-------AEIGEGVnigagtitcnydgvnkhrtVI 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1519714017 144 GDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPP 179
Cdd:cd03353   148 GDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPP 183
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-178 9.86e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.17  E-value: 9.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELdegvhVGAYAYIGAhVRIASGTHVMHHATVDGAtTLGHDNEVHPYAYV-GGKTHDKKYTGGIQRLEV 83
Cdd:PRK14356  266 IGPRATIEPGAEI-----YGPCEIYGA-SRIARGAVIHSHCWLRDA-VVSSGATIHSFSHLeGAEVGDGCSVGPYARLRP 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  84 GN--------GNtFREF--TTVHCATSEDLVTRLGDhnlilaySHIAHECQVGNHLVMSSHAALGGH-VIVGDHVNIAWG 152
Cdd:PRK14356  339 GAvleegarvGN-FVEMkkAVLGKGAKANHLTYLGD-------AEIGAGANIGAGTITCNYDGVNKHrTVIGEGAFIGSN 410

                         170       180
                  ....*....|....*....|....*.
gi 1519714017 153 SGLHQFVRIGDHAMVGASSKTVQDVP 178
Cdd:PRK14356  411 TALVAPVTIGDGALVGAGSVITKDVP 436
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-179 1.24e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.90  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   4 EIHPAAIIEPGAELDEGVHVGAYAYIGAHVR-----IASGTHVMH----HATVDGATTLGhdnevhPYAYVGGKTHDKKy 74
Cdd:PRK14354  267 EIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRivdstIGDGVTITNsvieESKVGDNVTVG------PFAHLRPGSVIGE- 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  75 tggiqrlEVGNGNtfreFTTVHCATsedlvtrLGDHnlilaySHIAHECQVGNhlvmsshAALGGHV------------- 141
Cdd:PRK14354  340 -------EVKIGN----FVEIKKST-------IGEG------TKVSHLTYIGD-------AEVGENVnigcgtitvnydg 388

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1519714017 142 ------IVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPP 179
Cdd:PRK14354  389 knkfktIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPE 432
PLN02357 PLN02357
serine acetyltransferase
 125-188 1.25e-04

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 42.56  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519714017 125 VGNHLVMSSHAALGG--------HVIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPA 188
Cdd:PLN02357  255 VGNNVSILHNVTLGGtgkqsgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPA 326
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 101-195 2.67e-04

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 41.14  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 101 EDLVTRLGDH-----NLILAYS-HIAHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGsglhqfVRIGDHAMVGASSKTV 174
Cdd:PRK09527   92 DDYTVTIGDNvliapNVTLSVTgHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPG------VTIGDNSVIGAGSVVT 165

                          90       100
                  ....*....|....*....|..
gi 1519714017 175 QDVPPFCICDGNPATV-RTINK 195
Cdd:PRK09527  166 KDIPPNVVAAGVPCRViREIND 187
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 141-190 4.02e-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: 40.10  E-value: 4.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519714017 141 VIVGDHVNIAWGSGLHQFVRIGDHAMVGASSKTVQDVPPFCICDGNPATV 190
Cdd:cd03357   119 ITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARV 168
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 138-187 5.34e-04

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: 38.19  E-value: 5.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519714017 138 GGHVIVGDHVNIawGSGLHQF--VRIGDHAMVGASSKTVQDVPPFCICDGNP 187
Cdd:cd03354    52 KRHPTIGDNVVI--GAGAKILgnITIGDNVKIGANAVVTKDVPANSTVVGVP 101
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-179 5.72e-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: 40.78  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   3 TEIHPAAIIEPGAELDEGVHVGAYAYIgAHVRIASGTHVmHHATVDGAtTLGHDNEVHPYAY------VGGKTHdkkytg 76
Cdd:COG1207   273 VVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVI-KYSVIEDA-VVGAGATVGPFARlrpgtvLGEGVK------ 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  77 giqrleVGNgntFREfttvhcatsedlV--TRLGDHnlilaySHIAHECQVGNhlvmsshAALGGHV------------- 141
Cdd:COG1207   344 ------IGN---FVE------------VknSTIGEG------SKVNHLSYIGD-------AEIGEGVnigagtitcnydg 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1519714017 142 ------IVGDHVNIawGSGlHQF---VRIGDHAMVGASSkTV-QDVPP 179
Cdd:COG1207   390 vnkhrtVIGDGAFI--GSN-TNLvapVTIGDGATIGAGS-TItKDVPA 433
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 5-175 6.56e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.73  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017   5 IHPAAIIEPGAELDEGVHVGAYAYIGAHVrIASGTHVMHHATVDGATtLGHDNEVHPYAYV--GGKTHDKKYTGGIqrLE 82
Cdd:PRK14358  279 IEPGVLLRGQTRVADGVTIGAYSVVTDSV-LHEGAVIKPHSVLEGAE-VGAGSDVGPFARLrpGTVLGEGVHIGNF--VE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  83 VGNGNTFREFTTVHCATSEDLV----TRLGDHNLILAYSHI-AHECQVGNHLVMSSHAALGGHVIVGDHVNIAWGSGLHQ 157
Cdd:PRK14358  355 TKNARLDAGVKAGHLAYLGDVTigaeTNVGAGTIVANFDGVnKHQSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHD 434

                         170
                  ....*....|....*...
gi 1519714017 158 FVRIGDHAMVGASSKTVQ 175
Cdd:PRK14358  435 DVPEGAMAVARGKQRNLE 452
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-197 1.08e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 39.75  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  28 YIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPY-----AYVGGKT------------HDKKYTGGIQRLEVGN----- 85
Cdd:PRK14357  251 YIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMtrivdCEIGNNVkiirseceksviEDDVSVGPFSRLREGTvlkks 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  86 ---GNtFREF--TTVHCATSEDLVTRLGDhnlilaySHIAHECQVGNHLVMSSHAALGGH-VIVGDHVNIAWGSGLHQFV 159
Cdd:PRK14357  331 vkiGN-FVEIkkSTIGENTKAQHLTYLGD-------ATVGKNVNIGAGTITCNYDGKKKNpTFIEDGAFIGSNSSLVAPV 402

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1519714017 160 RIGDHAMVGASSKTVQDVPPFCICDGNpatVRTINKIG 197
Cdd:PRK14357  403 RIGKGALIGAGSVITEDVPPYSLALGR---ARQIVKEG 437
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-66 1.25e-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: 36.84  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519714017   2 ATEIHPAAIIEPGAELDEGVHVGAYAYIGA--------HVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVG 66
Cdd:cd00208     6 GVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 34-190 2.27e-03

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  34 RIASGTHVMHHATVDGATTLGHDNEVHPYAYVggkthdkkyTGGIQRLEVGNGNTFREFTTVHcaTSEDLVTRLGDHnLI 113
Cdd:cd04650     2 RISPKAYVHPTSYVIGDVVIGELTSVWHYAVI---------RGDNDSIYIGKYSNVQENVSIH--TDHGYPTEIGDY-VT 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519714017 114 LAYSHIAHECQVGNHlvmsshaalgghVIVGdhvniaWGSGLHQFVRIGDHAMVGASSKTVQ--DVPPFCICDGNPATV 190
Cdd:cd04650    70 IGHNAVVHGAKVGNY------------VIVG------MGAILLNGAKIGDHVIIGAGAVVTPgkEIPDYSLVLGVPAKV 130
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 26-223 3.22e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 37.31  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017  26 YAYIGAHVRIASGTHVMHHATVDGATTLGHDNEVHPYAYVggkthdkkyTGGIQRLEVGNGNTFREFTTVHCatSEDLVT 105
Cdd:COG0663     4 YSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVL---------RGDVGPIRIGEGSNIQDGVVLHV--DPGYPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519714017 106 RLGDHnlilaySHIAHECQVgnhlvmssHAAlgghvIVGDHVNIAWGSGLHQFVRIGDHAMVGASSkTVQD---VPPFCI 182
Cdd:COG0663    73 TIGDD------VTIGHGAIL--------HGC-----TIGDNVLIGMGAIVLDGAVIGDGSIVGAGA-LVTEgkvVPPGSL 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1519714017 183 CDGNPAT-VRTINKIGLERAGYSSDE-IALARRiyklfYKDGL 223
Cdd:COG0663   133 VVGSPAKvVRELTEEEIAFLRESAENyVELARR-----YLAEL 170
 
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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