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Conserved domains on  [gi|496457981|ref|WP_009166826|]
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2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Fructilactobacillus florum]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 6-235 1.80e-109

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


The actual alignment was detected with superfamily member TIGR03532:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 231  Bit Score: 314.38  E-value: 1.80e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981    6 AAAIIKYIGTAPKTTNVKVYIKGKLAELTFPQEIKAFTDEQIGILFGDWAVVKPFLARHQDQIADYQVENLARNQAVPLL 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981   86 DTKELDARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKP 165
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  166 VQIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVKDVNQQTLTKTKLEDDLRG 235
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRK 230
 
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 ...
 6-235 1.80e-109

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: 314.38  E-value: 1.80e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981    6 AAAIIKYIGTAPKTTNVKVYIKGKLAELTFPQEIKAFTDEQIGILFGDWAVVKPFLARHQDQIADYQVENLARNQAVPLL 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981   86 DTKELDARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKP 165
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  166 VQIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVKDVNQQTLTKTKLEDDLRG 235
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRK 230
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-185 1.18e-39

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: 133.66  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  92 ARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDD 171
Cdd:cd03350    2 RRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDD 81

                         90
                 ....*....|....
gi 496457981 172 VLIGANAVVIEGVH 185
Cdd:cd03350   82 VFIGANCEVVEGVI 95
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-86 1.07e-32

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: 113.79  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981    5 DAAAIIKYIGTAPKTTNVKVYIKGKLAELTFPQE-IKAFTDEQIGILFGDWAVVKPFLARHQDQIADYQVENLARNQAVP 83
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEFEeIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 496457981   84 LLD 86
Cdd:pfam08503  81 LLD 83
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 82-234 1.74e-27

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: 105.58  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  82 VPLL--DTKELDARIEPGALIREQVKIGKDaVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIE 159
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 160 PASAKPVQIDDDVLIGANAVVIEGVHVGT----------------GAVVAAGAVVTSDVAPHTVVAGM-----------P 212
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEgavlgagvyltastkiYDRVTGEVYYGRVPAGSVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 496457981 213 AVKVKDVNQQTLTKTKLEDDLR 234
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 86-184 3.93e-26

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 102.19  E-value: 3.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  86 DTKELDARIEPGALIREQVKIGKDaVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKP 165
Cdd:PRK11830  98 RFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANP 176

                         90
                 ....*....|....*....
gi 496457981 166 VQIDDDVLIGANAVVIEGV 184
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGV 195
 
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 ...
 6-235 1.80e-109

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: 314.38  E-value: 1.80e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981    6 AAAIIKYIGTAPKTTNVKVYIKGKLAELTFPQEIKAFTDEQIGILFGDWAVVKPFLARHQDQIADYQVENLARNQAVPLL 85
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981   86 DTKELDARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKP 165
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  166 VQIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVKDVNQQTLTKTKLEDDLRG 235
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRK 230
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 92-185 1.18e-39

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: 133.66  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  92 ARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDD 171
Cdd:cd03350    2 RRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDD 81

                         90
                 ....*....|....
gi 496457981 172 VLIGANAVVIEGVH 185
Cdd:cd03350   82 VFIGANCEVVEGVI 95
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-86 1.07e-32

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: 113.79  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981    5 DAAAIIKYIGTAPKTTNVKVYIKGKLAELTFPQE-IKAFTDEQIGILFGDWAVVKPFLARHQDQIADYQVENLARNQAVP 83
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEFEeIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 496457981   84 LLD 86
Cdd:pfam08503  81 LLD 83
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 82-234 1.74e-27

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: 105.58  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  82 VPLL--DTKELDARIEPGALIREQVKIGKDaVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIE 159
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 160 PASAKPVQIDDDVLIGANAVVIEGVHVGT----------------GAVVAAGAVVTSDVAPHTVVAGM-----------P 212
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEgavlgagvyltastkiYDRVTGEVYYGRVPAGSVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 496457981 213 AVKVKDVNQQTLTKTKLEDDLR 234
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 86-184 3.93e-26

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 102.19  E-value: 3.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  86 DTKELDARIEPGALIREQVKIGKDaVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKP 165
Cdd:PRK11830  98 RFKEAGVRVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANP 176

                         90
                 ....*....|....*....
gi 496457981 166 VQIDDDVLIGANAVVIEGV 184
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGV 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 38-213 1.28e-17

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: 77.92  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981   38 EIKAFTDEQ---IGILFGDWAVVKPF--LARHQDQIADYQV---ENLARNQAVPLLDTKELDAR--IEPGALIREQVKIG 107
Cdd:TIGR03570  24 EVVGFLDDNpalQGTEVDGLPVLGGDedLLRYPPDEVDLVVaigDNKLRRRLVEKLKAKGYRFAtlIHPSAIVSPSASIG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  108 KDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGviepasakPVQIDDDVLIGANAVVIEGVHVG 187
Cdd:TIGR03570 104 EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIG 175

                         170       180
                  ....*....|....*....|....*.
gi 496457981  188 TGAVVAAGAVVTSDVAPHTVVAGMPA 213
Cdd:TIGR03570 176 AGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 94-212 1.41e-15

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: 72.13  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  94 IEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGviepasakPVQIDDDVL 173
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496457981 174 IGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMP 212
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
99-220 1.07e-12

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 63.35  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  99 LIREQVKIGKDAVVMMGALINIG-AEIGAGSMIDMGAVLGGRALV--GKHCHIGAGAVLAGV--------IEPASAKPVQ 167
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPGGItiGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496457981 168 IDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVKDVN 220
Cdd:COG0110   84 IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 91-180 2.35e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 62.34  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVL-------AGVIEPASA 163
Cdd:COG1044  114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIgadgfgfAPDEDGGWV 193

                         90       100
                 ....*....|....*....|..
gi 496457981 164 K-P----VQIDDDVLIGANAVV 180
Cdd:COG1044  194 KiPqlgrVVIGDDVEIGANTTI 215
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 94-180 2.57e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.08  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  94 IEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAvlagVIEPAsakpVQIDDDVL 173
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANV----TIYHA----VRIGNRVI 174


                 ....*..
gi 496457981 174 IGANAVV 180
Cdd:PRK00892 175 IHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 91-180 8.04e-11

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: 59.34  E-value: 8.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAG-----VIEPASAKP 165
Cdd:cd03352    7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgfAPDGGGWVK 86

                         90       100
                 ....*....|....*....|.
gi 496457981 166 ------VQIDDDVLIGANAVV 180
Cdd:cd03352   87 ipqlggVIIGDDVEIGANTTI 107
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 122-184 2.98e-09

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: 52.25  E-value: 2.98e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496457981 122 AEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDDVLIGANAVVIEGV 184
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGV 63
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 91-177 4.55e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.53  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLA----GVIEPASA--K 164
Cdd:PRK00892 118 GVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGsdgfGFANDRGGwvK 197

                         90
                 ....*....|....*...
gi 496457981 165 PVQ-----IDDDVLIGAN 177
Cdd:PRK00892 198 IPQlgrviIGDDVEIGAN 215
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 92-180 2.46e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 53.48  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  92 ARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVlggralVGKHCHIGAGAVL-AGV-IEPAsakpVQID 169
Cdd:COG1044   97 PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV------IGDGVVIGDDCVLhPNVtIYER----CVIG 166

                         90
                 ....*....|.
gi 496457981 170 DDVLIGANAVV 180
Cdd:COG1044  167 DRVIIHSGAVI 177
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 118-217 4.73e-08

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: 51.24  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 118 INIGAEIGAGSMID--MGAVLGGRALVGKHC--------------------------HIGAGAVLAGviepasakPVQID 169
Cdd:COG1045   68 IHPGATIGRGFFIDhgTGVVIGETAVIGDNVtiyqgvtlggtgkekgkrhptigdnvVIGAGAKILG--------PITIG 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 496457981 170 DDVLIGANAVviegvhvgtgavvaagavVTSDVAPHTVVAGMPAVKVK 217
Cdd:COG1045  140 DNAKIGANSV------------------VLKDVPPGSTVVGVPARIVK 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 115-212 6.08e-08

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: 49.36  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 115 GALINIGAEIGAGSMID--MGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDDVLIGANAVVIEGVHVGTGAVV 192
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                         90       100
                 ....*....|....*....|
gi 496457981 193 AAGAVVTSDVAPHTVVAGMP 212
Cdd:cd03354   82 GANAVVTKDVPANSTVVGVP 101
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 106-217 1.39e-07

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: 48.65  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 106 IGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGVIEPASA-------KPVQIDDDVLIGANA 178
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKiyrkwelKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496457981 179 VVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVK 217
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 104-180 4.41e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.94  E-value: 4.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496457981 104 VKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVL-AGVIepasakpvqIDDDVLIGANAVV 180
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIyEGCI---------IGDRVIIHSGAVI 70
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 93-184 4.83e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 49.25  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  93 RIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGviEPASAKPVQIDDDV 172
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQDFTYKGEESRL 78

                         90
                 ....*....|..
gi 496457981 173 LIGANAVVIEGV 184
Cdd:PRK12461  79 EIGDRNVIREGV 90
PLN02739 PLN02739
serine acetyltransferase
 113-234 1.23e-06

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 48.49  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 113 MMGALINIGAEIGAGSMID--MGAVLGGRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDDVLIGANAVVIEGVHVGTGA 190
Cdd:PLN02739 203 VFGIDIHPAARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGA 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496457981 191 VVAAGAVVTSDVAPHTVVAGMPAVKVKDVNQQTLTKTKLEDDLR 234
Cdd:PLN02739 283 MVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYDATR 326
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 123-216 2.35e-06

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: 45.14  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 123 EIGAGSMIDMGAVLGGRALV--GKHCHIGAGAVLAGV-----------IEPASAKPVQIDDDVLIGANAVVIEGVHVGTG 189
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGGItiGDNVLIGPNVTIYDHnhdiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 496457981 190 AVVAAGAVVTSDVAPHTVVAGMPAVKV 216
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
92-184 3.22e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.63  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  92 ARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGviEPASAK----PVQ 167
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGE--DPQDLKykgePTR 80

                         90
                 ....*....|....*..
gi 496457981 168 idddVLIGANAVVIEGV 184
Cdd:PRK05289  81 ----LVIGDNNTIREFV 93
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 91-219 5.12e-06

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 45.10  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALI-----NIgaEIGAGSMIDMGAVL----GGRALVGKHCHIGAGAVLAGVIepa 161
Cdd:cd04645    5 SAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCT--- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 162 sakpvqIDDDVLIGANAVVIEGVHVGTGAVVAA--GAVVTSDVAPHTVVAGMPAVKVKDV 219
Cdd:cd04645   80 ------IGDNCLIGMGAIILDGAVIGKGSIVAAgsLVPPGKVIPPGSLVAGSPAKVVREL 133
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 89-151 5.40e-06

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: 45.27  E-value: 5.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496457981  89 ELDARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAG 151
Cdd:cd05636    3 EIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNS 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 92-157 2.29e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 44.35  E-value: 2.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496457981  92 ARIEPGALIREQVKIGKDAVVmmGAliniGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLAGV 157
Cdd:cd03351    6 AIVDPGAKIGENVEIGPFCVI--GP----NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEA 65
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 91-222 4.59e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.32  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALIN-----IgaEIGAGSMIDMGAVL----GGRALVGKHCHIGAGAVLAGVIepa 161
Cdd:COG0663   16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGCT--- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496457981 162 sakpvqIDDDVLIGANAVVIEGVHVGTGAVVAA--GAVVTSDVAPHTVVAGMPAVKVKDVNQQ 222
Cdd:COG0663   91 ------IGDNVLIGMGAIVLDGAVIGDGSIVGAgaLVTEGKVVPPGSLVVGSPAKVVRELTEE 147
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 93-180 7.57e-05

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: 41.63  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  93 RIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDmGAVLGGrALVGKHCHIGAGAVLAGVIEPASAKPVQIDDDV 172
Cdd:cd04649    3 RIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVE-GRISSG-VIVGKGSDVGGGASIMGTLSGGGNNVISIGKRC 80


                 ....*...
gi 496457981 173 LIGANAVV 180
Cdd:cd04649   81 LLGANSGI 88
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 104-164 9.40e-05

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


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 40.34  E-value: 9.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496457981 104 VKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGRALVGKHCHIGaGAVLAGVIEPASAK 164
Cdd:cd05635   12 IYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIG-GEVEDSIIEGYSNK 71
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 91-155 2.22e-04

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: 40.87  E-value: 2.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALIN-----IGAEIGAGSMIDmGAVLGGRALVGKHCHIGAGAVLA 155
Cdd:cd03353   21 DVVIDPGVILEGKTVIGEDCVIGPNCVIKdstigDGVVIKASSVIE-GAVIGNGATVGPFAHLRPGTVLG 89
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 91-155 3.16e-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: 41.17  E-value: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALInIGAEIGAGSMIDM----GAVLGGRALVGKHCHIGAGAVLA 155
Cdd:COG1207  272 DVVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKYsvieDAVVGAGATVGPFARLRPGTVLG 339
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 94-155 3.92e-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: 38.00  E-value: 3.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  94 IEPGALIREQVKIGKDAVVMMGALI--------NIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLA 155
Cdd:cd00208    9 IHPKAVIRGPVVIGDNVNIGPGAVIgaatgpneKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 123-216 5.43e-04

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: 38.36  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 123 EIGAGSMIDMGAVLGGRALVgkhcHIGAGAVL-------AG------VIEPASAKPVQIDDDVLIGANAVVIEGVHVGTG 189
Cdd:cd05825    5 TIGDNSWIGEGVWIYNLAPV----TIGSDACIsqgaylcTGshdyrsPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*..
gi 496457981 190 AVVAAGAVVTSDVAPHTVVAGMPAVKV 216
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 92-202 5.51e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.48  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  92 ARIEPGALIREQVKIG-----KDAVVMMGALIN----IG-AEIGAGSMIDMGAVLGGRALVGKH-CHIGAGAVLAGviEP 160
Cdd:PRK14356 334 ARLRPGAVLEEGARVGnfvemKKAVLGKGAKANhltyLGdAEIGAGANIGAGTITCNYDGVNKHrTVIGEGAFIGS--NT 411

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496457981 161 ASAKPVQIDDDVLIGANAVviegvhvgtgavvaagavVTSDV 202
Cdd:PRK14356 412 ALVAPVTIGDGALVGAGSV------------------ITKDV 435
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-178 5.91e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 5.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496457981 100 IREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGGrALVGKHCHIGAGAVLAGviepasakpVQIDDDVLIGANA 178
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAGSVLED---------SVVGDDVAIGPMA 333
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 119-213 7.76e-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: 38.94  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 119 NIgaEIGAGSMIDMGAVL--GGRALVGKHCHIGAGAVLAGV---IEPAS-------AKPVQIDDDVLIGANAVVIEGVHV 186
Cdd:cd03357   62 NI--HIGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIYTAghpLDPEErnrgleyAKPITIGDNVWIGGGVIILPGVTI 139

                         90       100
                 ....*....|....*....|....*..
gi 496457981 187 GTGAVVAAGAVVTSDVAPHTVVAGMPA 213
Cdd:cd03357  140 GDNSVIGAGSVVTKDIPANVVAAGNPA 166
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 91-148 8.46e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 8.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGG------------RALVGKHCHI 148
Cdd:COG1043   19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptRLEIGDNNTI 88
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 91-224 1.85e-03

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 38.25  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGkdAVVMMGALINIGAEIG-----AGSMIDMGAVLGGRA----LVGKHCHIGAGAVLAGVIepa 161
Cdd:PRK13627  16 TAFVHPSAVLIGDVIVG--AGVYIGPLASLRGDYGrlivqAGANLQDGCIMHGYCdtdtIVGENGHIGHGAILHGCV--- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496457981 162 sakpvqIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDV--APHTVVAGMPAVKVKDVNQQTL 224
Cdd:PRK13627  91 ------IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVSDDEL 149
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 104-180 2.12e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 36.67  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 104 VKIGKDAV----VMMGaliniGAEIGAGSMIDmgavlggRALVGKHCHIGAGAVLAGVIEPASAKPVQIDDD-VLIGANA 178
Cdd:cd04651   35 VRVGSGSVvedsVIMP-----NVGIGRNAVIR-------RAIIDKNVVIPDGVVIGGDPEEDRARFYVTEDGiVVVGKGM 102


                 ..
gi 496457981 179 VV 180
Cdd:cd04651  103 VI 104
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 91-214 2.19e-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: 38.18  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLGG-----------------------------RA- 140
Cdd:cd03351   17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptrleigdnntirefvtihRGt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 141 -------------------------LVGKHCHIGAGAVLAGviepasakPVQIDDDVLIGANAVVIEGVHVGTGAVVAAG 195
Cdd:cd03351   97 aqgggvtrignnnllmayvhvahdcVIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                        170
                 ....*....|....*....
gi 496457981 196 AVVTSDVAPHTVVAGMPAV 214
Cdd:cd03351  169 SGVVQDVPPYVIAAGNRAR 187
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 163-217 2.33e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 37.87  E-value: 2.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496457981 163 AKPVQIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPAVKVK 217
Cdd:PRK10092 127 GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 91-220 2.49e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981  91 DARIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVLG------------GRALVGKHCHIGAGAVL---- 154
Cdd:PRK12461  17 GVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGdepqdftykgeeSRLEIGDRNVIREGVTIhrgt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 155 -AG-----------------------------VIEPASAKPVQIDDDVLIGANAVVIEGVHVGTGAVVAAGAVVTSDVAP 204
Cdd:PRK12461  97 kGGgvtrigndnllmayshvahdcqignnvilVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPP 176

                        170
                 ....*....|....*.
gi 496457981 205 HTVVAGMPaVKVKDVN 220
Cdd:PRK12461 177 YCMMAGHP-TNVHGLN 191
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
121-150 3.79e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.79e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 496457981  121 GAEIGAGSMIDMGAVLGGRALVGKHCHIGA 150
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 122-185 4.49e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.43  E-value: 4.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496457981 122 AEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVL-AGVIEPASA---KPVQIDDDVLIGANAVVIEGVH 185
Cdd:PRK00892 101 AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIgDGVVIGAGAvigDGVKIGADCRLHANVTIYHAVR 168
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 118-185 5.91e-03

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: 36.63  E-value: 5.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496457981 118 INIGAEIGAGSMIDMGAVLGGRALVGKHCHIGAGAVLagviepasaKPVQIDDDVLIGANaVVIEGVH 185
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI---------KDSTIGDGVVIKAS-SVIEGAV 69
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 105-155 6.52e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.48  E-value: 6.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496457981 105 KIGKDaVVMMGALINIGAEIGAGSMIDMgAVLGGRALVGKHCHIGAGAVLA 155
Cdd:cd05787   24 KIGKN-VVIDNSYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLIS 72
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 123-213 7.50e-03

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 35.60  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496457981 123 EIGAGSMID--MGAVLGGRALVGKHCHIGAGAVL--------------------------AGVIEPASAKPVQIDDDVLI 174
Cdd:cd03349    3 SVGDYSYGSgpDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypfyifggeweddAKFDDWPSKGDVIIGNDVWI 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496457981 175 GANAVVIEGVHVGTGAVVAAGAVVTSDVAPHTVVAGMPA 213
Cdd:cd03349   83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPA 121
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
93-161 8.69e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 35.62  E-value: 8.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496457981  93 RIEPGALIREQVKIGKDAVVMMGALINIGAEIGAGSMIDMGAVlggralVGKhcHIGAGAVLAGViePA 161
Cdd:COG0110   71 DPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSV------VTK--DVPPYAIVAGN--PA 129
 
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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