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Conserved domains on  [gi|446171984|ref|WP_000249839|]
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MULTISPECIES: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Staphylococcus]

Protein Classification

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase( domain architecture ID 11497020)

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 7-237 4.83e-131

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


:

Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 369.08  E-value: 4.83e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984    7 AEEIIQYISDAKKSTPIKVYLNGNFEGITYPESFKVFGSEQSKVIFCEADDWKPFYEAYGSQFEDIEIEMDRRNSAIPLK 86
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984   87 DLTNTNARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASP 166
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446171984  167 VIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQASEVQDTKKEIVAALRKL 237
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 7-237 4.83e-131

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 369.08  E-value: 4.83e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984    7 AEEIIQYISDAKKSTPIKVYLNGNFEGITYPESFKVFGSEQSKVIFCEADDWKPFYEAYGSQFEDIEIEMDRRNSAIPLK 86
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984   87 DLTNTNARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASP 166
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446171984  167 VIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQASEVQDTKKEIVAALRKL 237
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-214 6.31e-52

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: 164.86  E-value: 6.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASPVIIED 171
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446171984 172 DVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGTPA 214
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGSVVvAGSLP 139
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 83-235 7.30e-43

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 146.03  E-value: 7.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  83 IPLK--DLTNTNARIEPGAFIREQAIIEDGaVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIE 160
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 161 PPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGT-----------P 213
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGSVVvPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 446171984 214 AKVIKQASEVQDTKKEIVAALR 235
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 83-235 3.92e-42

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 144.18  E-value: 3.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  83 IPLK-------DLTNTNARIEPGAFIREQAIIEDGaVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVL 155
Cdd:PRK11830  87 VPLKfagwdeaRFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 156 AGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGT------- 212
Cdd:PRK11830 166 GGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGSVVvPGSlpskdgg 245

                        170       180
                 ....*....|....*....|....*..
gi 446171984 213 ----PAKVIKQASEVQDTKKEIVAALR 235
Cdd:PRK11830 246 yslyCAVIVKKVDAKTRSKTSINELLR 272
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 6-87 3.17e-37

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 125.35  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984    6 TAEEIIQYISDAKKSTPIKVYLNGNFEGITYP-ESFKVFGSEQSKVIFCEADDWKPFYEAYGSQFEDIEIEMDRRNSAIP 84
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 446171984   85 LKD 87
Cdd:pfam08503  81 LLD 83
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 7-237 4.83e-131

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 369.08  E-value: 4.83e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984    7 AEEIIQYISDAKKSTPIKVYLNGNFEGITYPESFKVFGSEQSKVIFCEADDWKPFYEAYGSQFEDIEIEMDRRNSAIPLK 86
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984   87 DLTNTNARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASP 166
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446171984  167 VIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQASEVQDTKKEIVAALRKL 237
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-214 6.31e-52

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: 164.86  E-value: 6.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASPVIIED 171
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446171984 172 DVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGTPA 214
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGSVVvAGSLP 139
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 83-235 7.30e-43

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 146.03  E-value: 7.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  83 IPLK--DLTNTNARIEPGAFIREQAIIEDGaVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIE 160
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 161 PPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGT-----------P 213
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGSVVvPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 446171984 214 AKVIKQASEVQDTKKEIVAALR 235
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 83-235 3.92e-42

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 144.18  E-value: 3.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  83 IPLK-------DLTNTNARIEPGAFIREQAIIEDGaVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVL 155
Cdd:PRK11830  87 VPLKfagwdeaRFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 156 AGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ---------------DVPAGAVV-AGT------- 212
Cdd:PRK11830 166 GGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGSVVvPGSlpskdgg 245

                        170       180
                 ....*....|....*....|....*..
gi 446171984 213 ----PAKVIKQASEVQDTKKEIVAALR 235
Cdd:PRK11830 246 yslyCAVIVKKVDAKTRSKTSINELLR 272
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 6-87 3.17e-37

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 125.35  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984    6 TAEEIIQYISDAKKSTPIKVYLNGNFEGITYP-ESFKVFGSEQSKVIFCEADDWKPFYEAYGSQFEDIEIEMDRRNSAIP 84
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 446171984   85 LKD 87
Cdd:pfam08503  81 LLD 83
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
100-222 2.89e-31

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 111.89  E-value: 2.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 100 FIREQAIIEDGAVVMMGATINIG-AVVGEGTMIDMNATL--GGRATTGKNVHVGAGAVLAGV--------IEPPSASPVI 168
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446171984 169 IEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQASE 222
Cdd:COG0110   84 IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-214 1.55e-30

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: 112.20  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984   95 IEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGvieppsasPVIIEDDVL 174
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446171984  175 IGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPA 214
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 95-213 4.74e-30

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: 110.65  E-value: 4.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGvieppsasPVIIEDDVL 174
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446171984 175 IGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTP 213
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 123-219 2.03e-26

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: 99.54  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 123 AVVGEGTMIDMNATLGGRA--------TTGKNVHVGAGAVLAGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIVA 194
Cdd:cd03349   22 LSIGKFCSIAPGVKIGLGGnhptdwvsTYPFYIFGGEWEDDAKFDDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIA 101

                         90       100
                 ....*....|....*....|....*
gi 446171984 195 AGAIVTQDVPAGAVVAGTPAKVIKQ 219
Cdd:cd03349  102 AGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 124-217 3.24e-25

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: 95.22  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 124 VVGEGTMIDMNATLGGRA--TTGKNVHVGAGAVLAGV-----------IEPPSASPVIIEDDVLIGANAVILEGVRVGKG 190
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVTIYDHnhdiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 446171984 191 AIVAAGAIVTQDVPAGAVVAGTPAKVI 217
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 116-218 1.89e-24

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: 93.72  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 116 GATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSAS-------PVIIEDDVLIGANAVILEGVRVG 188
Cdd:cd03358   10 NVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIyrkwelkGTTVKRGASIGANATILPGVTIG 89

                         90       100       110
                 ....*....|....*....|....*....|
gi 446171984 189 KGAIVAAGAIVTQDVPAGAVVAGTPAKVIK 218
Cdd:cd03358   90 EYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 94-222 2.17e-24

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: 94.40  E-value: 2.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIREQA------IIEDGAVVMMGATI-----NIgaVVGEGTMIDMNATL----GGRATTGKNVHVGAGAVLAGV 158
Cdd:cd04645    1 EIDPSAFIAPNAtvigdvTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGC 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 159 IeppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQD--VPAGAVVAGTPAKVIKQASE 222
Cdd:cd04645   79 T---------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTD 135
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 125-217 2.78e-24

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: 94.80  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 125 VGEGTMIDMNATL--GGRATTGKNVHVGAGAVLAGV---IEPPS-------ASPVIIEDDVLIGANAVILEGVRVGKGAI 192
Cdd:cd03357   65 IGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIYTAghpLDPEErnrgleyAKPITIGDNVWIGGGVIILPGVTIGDNSV 144

                         90       100
                 ....*....|....*....|....*
gi 446171984 193 VAAGAIVTQDVPAGAVVAGTPAKVI 217
Cdd:cd03357  145 IGAGSVVTKDIPANVVAAGNPARVI 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 94-222 7.53e-24

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 93.55  E-value: 7.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIREQA------IIEDGAVVMMGATIN-----IgaVVGEGTMIDMNATL---GGRATT-GKNVHVGAGAVLAGV 158
Cdd:COG0663   12 QIHPSAFVAPTAvvigdvTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdPGYPLTiGDDVTIGHGAILHGC 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 159 IeppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQD--VPAGAVVAGTPAKVIKQASE 222
Cdd:COG0663   90 T---------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTE 146
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 116-220 3.59e-21

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: 86.68  E-value: 3.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 116 GATINIGAVVGEGTMID--MNATLGGRATTGKNVHVGAGAVLAGV-IEPPSASPVIiEDDVLIGANAVILEGVRVGKGAI 192
Cdd:COG1045   65 GIDIHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPTI-GDNVVIGAGAKILGPITIGDNAK 143

                         90       100
                 ....*....|....*....|....*...
gi 446171984 193 VAAGAIVTQDVPAGAVVAGTPAKVIKQA 220
Cdd:COG1045  144 IGANSVVLKDVPPGSTVVGVPARIVKRK 171
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 116-213 6.53e-19

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 78.64  E-value: 6.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 116 GATINIGAVVGEGTMID--MNATLGGRATTGKNVHVGAGAVLAGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIV 193
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                         90       100
                 ....*....|....*....|
gi 446171984 194 AAGAIVTQDVPAGAVVAGTP 213
Cdd:cd03354   82 GANAVVTKDVPANSTVVGVP 101
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 92-239 7.98e-19

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: 83.53  E-value: 7.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAG-----VIEP----- 161
Cdd:COG1044  114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGAdgfgfAPDEdggwv 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 162 --PSASPVIIEDDVLIGANA----------VILEGVR------------------------------------------- 186
Cdd:COG1044  194 kiPQLGRVVIGDDVEIGANTtidrgalgdtVIGDGTKidnlvqiahnvrigehtaiaaqvgiagstkigdnvviggqvgi 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446171984 187 -----VGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQAsevqdtkKEIVAALRKLND 239
Cdd:COG1044  274 aghltIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREW-------LRNAAALRRLPE 324
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 123-200 1.81e-16

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: 71.51  E-value: 1.81e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446171984 123 AVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVT 200
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 92-219 4.56e-16

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: 73.98  E-value: 4.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVL-----------AGVIE 160
Cdd:cd03352    7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgGGWVK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 161 PPSASPVIIEDDVLIGANA----------VILEGV--------------------------------------------- 185
Cdd:cd03352   87 IPQLGGVIIGDDVEIGANTtidrgalgdtVIGDGTkidnlvqiahnvrigencliaaqvgiagsttigdnviiggqvgia 166

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446171984 186 ---RVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQ 219
Cdd:cd03352  167 ghlTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
PLN02739 PLN02739
serine acetyltransferase
 95-225 6.55e-16

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 75.84  E-value: 6.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAIIEDGAVVMMGATinigAVVGEGTMIDMNATLGGratTGKNVhvgagavlaGVIEPPsaspviIEDDVL 174
Cdd:PLN02739 208 IHPAARIGKGILLDHGTGVVIGET----AVIGDRVSILHGVTLGG---TGKET---------GDRHPK------IGDGAL 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446171984 175 IGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQASEvQD 225
Cdd:PLN02739 266 LGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE-QD 315
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 91-209 1.72e-15

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: 72.07  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  91 TNARIEPGAFIR-----EQAIIEDGAVVMMGATINIGAVVGEGTMID-----MNATLG-----------GRATTGKNVHV 149
Cdd:cd03353   49 KDSTIGDGVVIKassviEGAVIGNGATVGPFAHLRPGTVLGEGVHIGnfveiKKSTIGegskanhlsylGDAEIGEGVNI 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 150 GAGAVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVV 209
Cdd:cd03353  129 GAGTITCnydGV----NKHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 91-218 2.57e-15

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: 74.29  E-value: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  91 TNARIEPGAFIReQAIIEDGAVVMM----GATINIGAVVG------EGTMIDM-----------NATLG----------- 138
Cdd:COG1207  289 EGVVIGPNCTLK-DSTIGDGVVIKYsvieDAVVGAGATVGpfarlrPGTVLGEgvkignfvevkNSTIGegskvnhlsyi 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 139 GRATTGKNVHVGAGAVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGA-VVAGTPA 214
Cdd:COG1207  368 GDAEIGEGVNIGAGTITCnydGV----NKHRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGAlAIARARQ 443


                 ....
gi 446171984 215 KVIK 218
Cdd:COG1207  444 RNIE 447
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 164-219 4.58e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 70.61  E-value: 4.58e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 164 ASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQ 219
Cdd:PRK10092 127 GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 164-217 1.04e-14

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: 67.63  E-value: 1.04e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446171984 164 ASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVI 217
Cdd:cd05825   54 TAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 94-228 1.16e-14

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 68.93  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIREQA-IIEDgavVMMGATINIGA-----------VVGEGTMIDMNATLGGR----ATTGKNVHVGAGAVLAG 157
Cdd:cd04745    2 VVDPSSFVHPTAvLIGD---VIIGKNCYIGPhaslrgdfgriVIRDGANVQDNCVIHGFpgqdTVLEENGHIGHGAILHG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 158 VIeppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ--DVPAGAVVAGTPAKVIKQASEVQDTKK 228
Cdd:cd04745   79 CT---------IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSDEEVAWK 142
PLN02296 PLN02296
carbonate dehydratase
 95-222 3.52e-14

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 69.77  E-value: 3.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAIIEDGAVVMMGATINIGAV---------VGEGTMIDMNA-------TLGGR---ATTGKNVHVGAGAVL 155
Cdd:PLN02296  55 VDKDAFVAPSASVIGDVQVGRGSSIWYGCVlrgdvnsisVGSGTNIQDNSlvhvaktNLSGKvlpTIIGDNVTIGHSAVL 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446171984 156 AGVIeppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQD--VPAGAVVAGTPAKVIKQASE 222
Cdd:PLN02296 135 HGCT---------VEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTE 194
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 92-219 4.01e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.47  E-value: 4.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVL----------AGVIEP 161
Cdd:PRK00892 118 GVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandRGGWVK 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 162 -PSASPVIIEDDVLIGANA----------VILEGVR-------------------------------------------- 186
Cdd:PRK00892 198 iPQLGRVIIGDDVEIGANTtidrgalddtVIGEGVKidnlvqiahnvvigrhtaiaaqvgiagstkigrycmiggqvgia 277

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446171984 187 ----VGKGAIVAAGAIVTQDVPA-GAVVAGTPAKVIKQ 219
Cdd:PRK00892 278 ghleIGDGVTITAMSGVTKSIPEpGEYSSGIPAQPNKE 315
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 92-216 4.37e-13

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: 66.58  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGG-----------------------------RAT 142
Cdd:COG1043   19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptrleigdnntirefvtihRGT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 143 TGK--------------NVHVG------------AGAVLAGvieppsasPVIIEDDVLIGANAVILEGVRVGKGAIVAAG 196
Cdd:COG1043   99 VQGggvtrigddnllmaYVHVAhdcvvgnnvilaNNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGG 170

                        170       180
                 ....*....|....*....|
gi 446171984 197 AIVTQDVPAGAVVAGTPAKV 216
Cdd:COG1043  171 SGVVKDVPPYVLAAGNPARL 190
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 161-218 1.53e-12

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 64.13  E-value: 1.53e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446171984 161 PPSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIK 218
Cdd:PRK09677 125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-219 1.61e-12

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 66.33  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGavVMMGATINI-GAVVGEGTMIDmNATLGGRATTGKNVHVGAGAVLAGvIEPPSASPVIIE 170
Cdd:PRK14357 312 DVSVGPFSRLREGTVLKKS--VKIGNFVEIkKSTIGENTKAQ-HLTYLGDATVGKNVNIGAGTITCN-YDGKKKNPTFIE 387

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446171984 171 DDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQ 219
Cdd:PRK14357 388 DGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 92-216 3.15e-12

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: 63.99  E-value: 3.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGG-----------------------------RAT 142
Cdd:cd03351   17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptrleigdnntirefvtihRGT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 143 TGK--------------NVHVG------------AGAVLAGvieppsasPVIIEDDVLIGANAVILEGVRVGKGAIVAAG 196
Cdd:cd03351   97 AQGggvtrignnnllmaYVHVAhdcvignnvilaNNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                        170       180
                 ....*....|....*....|
gi 446171984 197 AIVTQDVPAGAVVAGTPAKV 216
Cdd:cd03351  169 SGVVQDVPPYVIAAGNRARL 188
PLN02694 PLN02694
serine O-acetyltransferase
 95-217 4.81e-12

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 64.28  E-value: 4.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAIIEDGAVVMMGATinigAVVGEGTMIDMNATLGGRATTGKNVHVGAGavlagvieppsaspviieDDVL 174
Cdd:PLN02694 163 IHPAAKIGKGILFDHATGVVIGET----AVIGNNVSILHHVTLGGTGKACGDRHPKIG------------------DGVL 220

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446171984 175 IGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVI 217
Cdd:PLN02694 221 IGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PLN02357 PLN02357
serine acetyltransferase
 95-217 5.26e-12

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 64.52  E-value: 5.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAIIEDGAVVMMGATinigAVVGEGTMIDMNATLGGratTGKNvhvgagavlAGVIEPPsaspviIEDDVL 174
Cdd:PLN02357 229 IHPGAKIGQGILLDHATGVVIGET----AVVGNNVSILHNVTLGG---TGKQ---------SGDRHPK------IGDGVL 286

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446171984 175 IGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVI 217
Cdd:PLN02357 287 IGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
PRK10502 PRK10502
putative acyl transferase; Provisional
 125-222 6.06e-12

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 62.27  E-value: 6.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 125 VGEGTMIDmnaTLGgRATTGKNVHVGAGAVLAG---VIEPPS----ASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGA 197
Cdd:PRK10502  80 IGDDVWLY---NLG-EITIGAHCVISQKSYLCTgshDYSDPHfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARS 155

                         90       100
                 ....*....|....*....|....*
gi 446171984 198 IVTQDVPAGAVVAGTPAKVIKQASE 222
Cdd:PRK10502 156 SVFKSLPANTICRGNPAVPIRPRVE 180
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 99-229 2.04e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 61.17  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  99 AFIREQAIIEDGAVVMMGATINIG----------------AVVGEGTMIDMNATLggrATTGKNVHVG---AGAVLAgvi 159
Cdd:PRK09527  56 ATVGENAWVEPPVYFSYGSNIHIGrnfyanfnltivddytVTIGDNVLIAPNVTL---SVTGHPVHHElrkNGEMYS--- 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 160 eppsaSPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIKqasEVQDTKKE 229
Cdd:PRK09527 130 -----FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR---EINDRDKQ 191
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 91-218 2.44e-11

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 62.64  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  91 TNARIEPGAFIrEQAIIEDGAVVMM--------GATINIG--------AVVGEGTMID-----MNATLG----------- 138
Cdd:PRK14360 285 SGCRIGPGSLI-ENSQIGENVTVLYsvvsdsqiGDGVKIGpyahlrpeAQIGSNCRIGnfveiKKSQLGegskvnhlsyi 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 139 GRATTGKNVHVGAGAVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAK 215
Cdd:PRK14360 364 GDATLGEQVNIGAGTITAnydGV----KKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQ 439


                 ...
gi 446171984 216 VIK 218
Cdd:PRK14360 440 VIK 442
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-218 5.85e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 61.42  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIR-----EQAIIEDGAVVMMGATINIGAVVGEGTMID-----MNATLG-----------GRATTGKNVHVGAG 152
Cdd:PRK14353 288 TVASGAVIHafshlEGAHVGEGAEVGPYARLRPGAELGEGAKVGnfvevKNAKLGegakvnhltyiGDATIGAGANIGAG 367

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446171984 153 AVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKVIK 218
Cdd:PRK14353 368 TITCnydGF----NKHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-207 1.00e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 61.00  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGavVMMGATINI-GAVVGEGTMIDmNATLGGRATTGKNVHVGAGAVLA---GVieppSASPV 167
Cdd:PRK14354 322 NVTVGPFAHLRPGSVIGEE--VKIGNFVEIkKSTIGEGTKVS-HLTYIGDAEVGENVNIGCGTITVnydGK----NKFKT 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446171984 168 IIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGA 207
Cdd:PRK14354 395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDA 434
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-217 3.52e-10

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 59.18  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  87 DLTNTNARIEPGAFIR----EQAIIEDGAVVMMGATINIGAVVGE----GTMIDM-NATLG-----------GRATTGKN 146
Cdd:PRK14352 301 DTTLTDVTVGEGASVVrthgSESEIGAGATVGPFTYLRPGTVLGEegklGAFVETkNATIGrgtkvphltyvGDADIGEH 380

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446171984 147 VHVGAGAVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGA-VVAGTPAKVI 217
Cdd:PRK14352 381 SNIGASSVFVnydGV----NKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGAlAVSEGPQRNI 451
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-208 3.92e-10

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 58.97  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIR-----EQAIIEDGAVVMMGATINIGAVVGE----GTMIDMN-ATLG-----------GRATTGKNVHVG 150
Cdd:PRK14356 304 DAVVSSGATIHsfshlEGAEVGDGCSVGPYARLRPGAVLEEgarvGNFVEMKkAVLGkgakanhltylGDAEIGAGANIG 383

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446171984 151 AGAVLA---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAV 208
Cdd:PRK14356 384 AGTITCnydGV----NKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
92-216 1.02e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 57.03  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGG-----------------------------RAT 142
Cdd:PRK05289  20 NVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEdpqdlkykgeptrlvigdnntirefvtinRGT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 143 TGK--------------NVHVG------------AGAVLAGvieppsasPVIIEDDVLIGANAVILEGVRVGKGAIVAAG 196
Cdd:PRK05289 100 VQGggvtrigdnnllmaYVHVAhdcvvgnhvilaNNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGM 171

                        170       180
                 ....*....|....*....|
gi 446171984 197 AIVTQDVPAGAVVAGTPAKV 216
Cdd:PRK05289 172 SGVSQDVPPYVLAEGNPARL 191
cysE PRK11132
serine acetyltransferase; Provisional
 113-221 1.27e-09

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 57.01  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 113 VMMGATINIGAVVGEGTMIDmNAT---LGGRATTGKNVHVGAGAVLAGVIEPPSASPVIIEDDVLIGANAVILEGVRVGK 189
Cdd:PRK11132 138 VAFQVDIHPAAKIGRGIMLD-HATgivIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGR 216

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446171984 190 GAIVAAGAIVTQDVPAGAVVAGTPAKVIKQAS 221
Cdd:PRK11132 217 GAKIGAGSVVLQPVPPHTTAAGVPARIVGKPE 248
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 93-200 3.69e-09

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 54.13  E-value: 3.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  93 ARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEG-----------TMIDMNATLG-----GRATTGKNVHVGAGAVLA 156
Cdd:cd05636   24 AIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGcvvgnsvevknSIIMDGTKVPhlnyvGDSVLGENVNLGAGTITA 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 157 GVIEPPSASPV----------------IIEDDVLIGANAVILEGVRVGKGAIVAAGAIVT 200
Cdd:cd05636  104 NLRFDDKPVKVrlkgervdtgrrklgaIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-209 1.26e-08

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 54.65  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  93 ARIEPGAFIREQAIIEDgAVVMMGATINIGAVVGEGTMIdmnatlgGRATTGKNVHVGAGAVLAGViEPPSASPVIIEDD 172
Cdd:PRK09451 330 ARLRPGAELAEGAHVGN-FVEMKKARLGKGSKAGHLTYL-------GDAEIGDNVNIGAGTITCNY-DGANKFKTIIGDD 400

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446171984 173 VLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAVV 209
Cdd:PRK09451 401 VFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 94-222 1.43e-08

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: 52.19  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIREQAI------IEDGAVVMMGATI---NIGAVVGEGTMIDMNATL----GGRATTGKNVHVGAGAVLAGVIe 160
Cdd:cd04650    2 RISPKAYVHPTSYvigdvvIGELTSVWHYAVIrgdNDSIYIGKYSNVQENVSIhtdhGYPTEIGDYVTIGHNAVVHGAK- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446171984 161 ppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQ--DVPAGAVVAGTPAKVIKQASE 222
Cdd:cd04650   81 --------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPgkEIPDYSLVLGVPAKVVRKLTE 136
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-213 3.50e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.21  E-value: 3.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMM---------GATINIG-------AVVGEGTMIDmNATLGGRATTGKNVHVGAGAVL 155
Cdd:PRK14355 309 DVTVKAGSVLEDSVVGDDVAIGPMahlrpgtelSAHVKIGnfvetkkIVMGEGSKAS-HLTYLGDATIGRNVNIGCGTIT 387

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446171984 156 A---GVieppSASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAV-VAGTP 213
Cdd:PRK14355 388 CnydGV----KKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLaIARSP 445
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 95-222 4.27e-08

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 51.73  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  95 IEPGAFIREQAI-IEDgavVMMGATINIGA-----------VVGEGTMIDMNATLGGRATT----GKNVHVGAGAVLAGV 158
Cdd:PRK13627  13 VHPTAFVHPSAVlIGD---VIVGAGVYIGPlaslrgdygrlIVQAGANLQDGCIMHGYCDTdtivGENGHIGHGAILHGC 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 159 IeppsaspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGA--VVAGTPAKVIKQASE 222
Cdd:PRK13627  90 V---------IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKrqLLMGTPARAVRSVSD 146
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 106-216 6.16e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 51.95  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 106 IIEDGAVVMMGATINIG------AVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEppsaspviIEDDVLIGANA 179
Cdd:PRK12461  79 EIGDRNVIREGVTIHRGtkgggvTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVT--------VGDRAIISGNC 150

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446171984 180 VILEGVRVGKGAIVAAGAIVTQDVPAGAVVAGTPAKV 216
Cdd:PRK12461 151 LVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNV 187
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 92-234 2.23e-07

Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP succinyltransferase), C-terminal left-handed parallel alpha-helix (LbH) domain: This group is composed of mostly uncharacterized proteins containing an N-terminal domain of unknown function and a C-terminal LbH domain with similarity to THP succinyltransferase LbH. THP 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 trimeric and displays the left-handed parallel alpha-helix (LbH) structural motif encoded by the hexapeptide repeat motif.


Pssm-ID: 100054  Cd Length: 147  Bit Score: 48.95  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGgrATTGKNVHVGAGAVLAGVIEPPSASPVIIED 171
Cdd:cd04649    1 GVRIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVEGRISSG--VIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 172 DVLIGANAVIleGVRVGKGAIVAAGAIVTqdvpagavvAGTPAKVIKQasevQDTKKEIVAAL 234
Cdd:cd04649   79 RCLLGANSGI--GISLGDNCIVEAGLYVT---------AGTKVTLPDN----EEFEKNVVKAR 126
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 98-215 1.51e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.59  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984   98 GAFIREQAIIEDGAVVMMG-ATINIGAVVGEGTMIdmnatLGGRATTGKnVHVGagavlagvieppsasPVIIEDDVLIG 176
Cdd:TIGR02353 112 GAKIGKGVDIGSLPPVCTDlLTIGAGTIVRKEVML-----LGYRAERGR-LHTG---------------PVTLGRDAFIG 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446171984  177 ANAVILEGVRVGKGAIVAAGAIVT--QDVPAGAVVAGTPAK 215
Cdd:TIGR02353 171 TRSTLDIDTSIGDGAQLGHGSALQggQSIPDGERWHGSPAQ 211
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 104-237 2.99e-06

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 45.67  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 104 QAIIEDGAVVMmG--ATINIG--AVVGEGTMID--MNATLGGRA----TTGKNVHVGAGAVL-AGVIeppsASPVIIEDD 172
Cdd:cd03359   27 KTIIQSDVIIR-GdlATVSIGryCILSEGCVIRppFKKFSKGVAffplHIGDYVFIGENCVVnAAQI----GSYVHIGKN 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446171984 173 VLIGANAVILEGVRVGKGAIVAAGAIvtqdVPAGAVVAGTPAKVIKQASEVqdTKKEIVAALRKL 237
Cdd:cd03359  102 CVIGRRCIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFIGELPEC--TQELMEEETKEY 160
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
167-201 6.07e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 42.04  E-value: 6.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446171984  167 VIIEDDVLIGANAVIleGVRVGKGAIVAAGAIVTQ 201
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 91-208 8.88e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.13  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  91 TNARIEPGAFIREQAIIEdGAVVMMG------ATINIGAVVGEGTMI-----DMNATLG-----------GRATTGKNVH 148
Cdd:PRK14358 304 TDSVLHEGAVIKPHSVLE-GAEVGAGsdvgpfARLRPGTVLGEGVHIgnfveTKNARLDagvkaghlaylGDVTIGAETN 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 149 VGAGAVLA---GVIEPPSAspviIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDVPAGAV 208
Cdd:PRK14358 383 VGAGTIVAnfdGVNKHQSK----VGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAM 441
PLN02472 PLN02472
uncharacterized protein
 92-239 9.80e-06

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 45.34  E-value: 9.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  92 NARIEPGAFIREQAIIEDGAVVMMGA---------TINIGAVVGEGTMIDM--NATLGGRATT--GKNVHVGAGAVLagv 158
Cdd:PLN02472  65 DAYVAPNVVLAGQVTVWDGASVWNGAvlrgdlnkiTVGFCSNVQERCVLHAawNSPTGLPAETliDRYVTIGAYSLL--- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 159 ieppsaSPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVT--QDVPAGAVVAGTPAKVIKQASevQDTKKEIVAALRK 236
Cdd:PLN02472 142 ------RSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLT--NEETLEIPKLAVA 213


                 ...
gi 446171984 237 LND 239
Cdd:PLN02472 214 IND 216
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 159-203 1.42e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 1.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446171984 159 IEPPS--ASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDV 203
Cdd:PRK00892 103 IHPSAviDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 119-203 5.67e-05

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 40.25  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 119 INIGAVVGEGTMIdMNATLGGRATTGKNVHVGAGAVLAGVIeppsaspviIEDDVLIGaNAVILEGVRVGKGAIVAAGAI 198
Cdd:cd05787    2 IGRGTSIGEGTTI-KNSVIGRNCKIGKNVVIDNSYIWDDVT---------IEDGCTIH-HSIVADGAVIGKGCTIPPGSL 70


                 ....*
gi 446171984 199 VTQDV 203
Cdd:cd05787   71 ISFGV 75
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 130-202 6.55e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.09  E-value: 6.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 130 MIDMNATLGGRATTGKNVHVGAGAVLAGvieppsasPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQD 202
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGA--------NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE 65
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 159-203 7.31e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.08  E-value: 7.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446171984 159 IEPPS--ASPVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDV 203
Cdd:COG1044   99 IHPSAviDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
PRK10191 PRK10191
putative acyl transferase; Provisional
 128-216 1.32e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 41.03  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 128 GTMIDMNATLGGRATTGK------NVHVGAG-------AVLAGVIEPPSASPVIIEDDVLIGANAVILEGVRVGKGAIVA 194
Cdd:PRK10191  41 GYEIQAAATIGRRFTIHHgyavviNKNVVAGddftirhGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVG 120

                         90       100
                 ....*....|....*....|..
gi 446171984 195 AGAIVTQDVPAGAVVAGTPAKV 216
Cdd:PRK10191 121 AGSVVLDSVPDNALVVGEKARV 142
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
129-202 1.66e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 1.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446171984 129 TMIDMNATLGGRATTGKNVHVGAGAVlagvIEPPsaspVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIV---TQD 202
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCV----IGPN----VVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedPQD 71
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 94-190 1.68e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.55  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984  94 RIEPGAFIREQAIIEDGAVVMMGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGviEPPSASPVIIEDDV 173
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQDFTYKGEESRL 78

                         90
                 ....*....|....*..
gi 446171984 174 LIGANAVILEGVRVGKG 190
Cdd:PRK12461  79 EIGDRNVIREGVTIHRG 95
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
166-195 2.19e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 2.19e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 446171984  166 PVIIEDDVLIGANAVILEGVRVGKGAIVAA 195
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 90-156 5.33e-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: 37.61  E-value: 5.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446171984  90 NTNARIEPGAFIREQAIIEDGAVVM--MGATINIGAVVGEGTMIDMNATLGGRATTGKNVHVGAGAVLA 156
Cdd:cd00208   10 HPKAVIRGPVVIGDNVNIGPGAVIGaaTGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 167-203 9.53e-04

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: 38.93  E-value: 9.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446171984 167 VIIEDDVLIGANAVILEGVRVGKGAIVAAGAIVTQDV 203
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 130-202 1.66e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 38.57  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 130 MIDMNATLGGRATTGKNVHVGAGAVlagvIEPPsaspVIIEDDVLIGANAVILEGVRVGKGAIVAAGAIV---TQD 202
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCV----IGPN----VEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeaPQD 68
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-193 2.08e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.85  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446171984 131 IDMNATLGGRATTGKNVHVGAGAVLAGvieppsaspVIIEDDVLIGANAVIlEGVRVGKGAIV 193
Cdd:PRK09451 274 IDTNVIIEGNVTLGNRVKIGAGCVLKN---------CVIGDDCEISPYSVV-EDANLGAACTI 326
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-218 2.18e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.82  E-value: 2.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446171984 144 GKNVHVGAGAVLAgvieppsaSPVIIEDDVLIganavilegvrvgkgaivAAGAIVTQDVPAGA-VVAGTPAKVIK 218
Cdd:PRK14359 371 GKNVFIGSDTQLV--------APVNIEDNVLI------------------AAGSTVTKDVPKGSlAISRAPQKNIK 420
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 124-203 3.74e-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: 35.30  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446171984 124 VVGEGTMIDMNATLGgRATTGKNVHVGAGAVLagvieppsaSPVIIEDDVLIGANA-----VILEGVRVGKGAIVAAGAI 198
Cdd:cd03356    1 LIGESTVIGENAIIK-NSVIGDNVRIGDGVTI---------TNSILMDNVTIGANSvivdsIIGDNAVIGENVRVVNLCI 70


                 ....*
gi 446171984 199 VTQDV 203
Cdd:cd03356   71 IGDDV 75
PLN03161 PLN03161
Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional
 4-58 8.20e-03

Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional


Pssm-ID: 178706 [Multi-domain]  Cd Length: 291  Bit Score: 36.80  E-value: 8.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446171984   4 HLTAEEIIQYISdakkSTPIKVYLNGNFEGITYP--ESFKVFGSeqskviFCEADDW 58
Cdd:PLN03161 149 HWNPSEVVWYVD----GTPIRVFRNYENEGIAYPnkQGMRVYSS------LWNADNW 195
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 149-209 9.80e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 36.73  E-value: 9.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446171984 149 VGAGAVL-AGVIEPPSASP-VIIEDDVLIgANAVILEGVRVGKGAIVaAGAIVTQDV--PAGAVV 209
Cdd:PRK00844 318 VSAGSIIsGATVRNSVLSPnVVVESGAEV-EDSVLMDGVRIGRGAVV-RRAILDKNVvvPPGATI 380
 
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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