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Conserved domains on  [gi|488286804|ref|WP_002358012|]
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MULTISPECIES: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Enterococcus]

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 ...
 3-233 5.32e-121

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: 343.27  E-value: 5.32e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804    3 AYEIIQYIGDAKKQTPVKVTLKGQLKEVTFPETIKVFNNCKTGTLFGDWADVKPFLEANKEKIEDYVVENDARNSAIPFL 82
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804   83 DLKDINARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAP 162
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286804  163 VVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTKSKTEILEELRKL 233
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 ...
 3-233 5.32e-121

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: 343.27  E-value: 5.32e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804    3 AYEIIQYIGDAKKQTPVKVTLKGQLKEVTFPETIKVFNNCKTGTLFGDWADVKPFLEANKEKIEDYVVENDARNSAIPFL 82
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804   83 DLKDINARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAP 162
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286804  163 VVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTKSKTEILEELRKL 233
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 2-83 5.42e-44

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: 142.68  E-value: 5.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804    2 DAYEIIQYIGDAKKQTPVKVTLKGQLKEVTFP-ETIKVFNNCKTGTLFGDWADVKPFLEANKEKIEDYVVENDARNSAIP 80
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 488286804   81 FLD 83
Cdd:pfam08503  81 LLD 83
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 88-182 1.12e-41

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: 138.67  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIEN 167
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90
                 ....*....|....*
gi 488286804 168 EVVIGANAVVLEGVR 182
Cdd:cd03350   81 DVFIGANCEVVEGVI 95
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 83-231 9.13e-28

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 106.43  E-value: 9.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  83 DLKDINARIEPGALIREKVEIGdQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAP 162
Cdd:PRK11830  98 RFKEAGVRVVPGAVVRRGAYIA-PNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 163 VVIENEVVIGANAVVLEGVRVGEGAV---------------VAAGAVVVEDVPAHTVV-AG-VPAK----------VIKQ 215
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGVIVEEGSVlgmgvflgqstkiydRETGEVHYGRVPAGSVVvPGsLPSKdggyslycavIVKK 256

                        170
                 ....*....|....*.
gi 488286804 216 IDDKTKSKTEILEELR 231
Cdd:PRK11830 257 VDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 81-231 6.67e-26

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: 101.35  E-value: 6.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  81 FLDLKDINARIEPGALIREKVEIGdQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSA 160
Cdd:COG2171   90 FDYFKPAGVRIVPGARVRLGAYLA-PGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQA 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 161 APVVIENEVVIGANAVVLEGVRVGEG---------------AVVAAGAVVVEDVPAH-TVVAGV-----------PAKVI 213
Cdd:COG2171  169 APVIIEDNCFIGARSGVVEGVIVGEGavlgagvyltastkiYDRVTGEVYYGRVPAGsVVVPGSlpgkdgdyglyCAVIV 248

                        170
                 ....*....|....*...
gi 488286804 214 KQIDDKTKSKTEILEELR 231
Cdd:COG2171  249 KRRDEKTRSKTSLNELLR 266
 
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 ...
 3-233 5.32e-121

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: 343.27  E-value: 5.32e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804    3 AYEIIQYIGDAKKQTPVKVTLKGQLKEVTFPETIKVFNNCKTGTLFGDWADVKPFLEANKEKIEDYVVENDARNSAIPFL 82
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804   83 DLKDINARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAP 162
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286804  163 VVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTKSKTEILEELRKL 233
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 2-83 5.42e-44

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: 142.68  E-value: 5.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804    2 DAYEIIQYIGDAKKQTPVKVTLKGQLKEVTFP-ETIKVFNNCKTGTLFGDWADVKPFLEANKEKIEDYVVENDARNSAIP 80
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEANKDKIEDYHIENDRRNSAIP 80


                  ...
gi 488286804   81 FLD 83
Cdd:pfam08503  81 LLD 83
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 88-182 1.12e-41

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: 138.67  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIEN 167
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90
                 ....*....|....*
gi 488286804 168 EVVIGANAVVLEGVR 182
Cdd:cd03350   81 DVFIGANCEVVEGVI 95
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 83-231 9.13e-28

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 106.43  E-value: 9.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  83 DLKDINARIEPGALIREKVEIGdQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAP 162
Cdd:PRK11830  98 RFKEAGVRVVPGAVVRRGAYIA-PNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 163 VVIENEVVIGANAVVLEGVRVGEGAV---------------VAAGAVVVEDVPAHTVV-AG-VPAK----------VIKQ 215
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGVIVEEGSVlgmgvflgqstkiydRETGEVHYGRVPAGSVVvPGsLPSKdggyslycavIVKK 256

                        170
                 ....*....|....*.
gi 488286804 216 IDDKTKSKTEILEELR 231
Cdd:PRK11830 257 VDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 81-231 6.67e-26

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: 101.35  E-value: 6.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  81 FLDLKDINARIEPGALIREKVEIGdQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSA 160
Cdd:COG2171   90 FDYFKPAGVRIVPGARVRLGAYLA-PGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQA 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 161 APVVIENEVVIGANAVVLEGVRVGEG---------------AVVAAGAVVVEDVPAH-TVVAGV-----------PAKVI 213
Cdd:COG2171  169 APVIIEDNCFIGARSGVVEGVIVGEGavlgagvyltastkiYDRVTGEVYYGRVPAGsVVVPGSlpgkdgdyglyCAVIV 248

                        170
                 ....*....|....*...
gi 488286804 214 KQIDDKTKSKTEILEELR 231
Cdd:COG2171  249 KRRDEKTRSKTSLNELLR 266
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
96-221 1.80e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 76.06  E-value: 1.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  96 LIREKVEIGDQAVIMMGAILNIG-AVVGAGTMIDMGAVL--GGRATVGKHCHIGAGTVLAGV--------IEPPSAAPVV 164
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488286804 165 IENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTK 221
Cdd:COG0110   84 IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 91-210 1.68e-16

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: 74.84  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804   91 IEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGvieppsaaPVVIENEVV 170
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488286804  171 IGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPA 210
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 91-209 4.61e-16

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: 73.67  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  91 IEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGvieppsaaPVVIENEVV 170
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488286804 171 IGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVP 209
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-177 8.37e-13

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: 66.58  E-value: 8.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAG-----VIEP----- 157
Cdd:COG1044  114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGAdgfgfAPDEdggwv 193

                         90       100
                 ....*....|....*....|..
gi 488286804 158 --PSAAPVVIENEVVIGANAVV 177
Cdd:COG1044  194 kiPQLGRVVIGDDVEIGANTTI 215
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 91-219 1.29e-12

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: 63.56  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  91 IEPGAlirekvEIGDQAVIM--MGAILNIGAVVGAGTMIDMGAVLGGRA--------TVGKHCHIGAGTVLAGvieppsa 160
Cdd:COG1045   68 IHPGA------TIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTGkekgkrhpTIGDNVVIGAGAKILG------- 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488286804 161 aPVVIENEVVIGANAVVLegvrvgegavvaagavvvEDVPAHTVVAGVPAKVIKQIDDK 219
Cdd:COG1045  135 -PITIGDNAKIGANSVVL------------------KDVPPGSTVVGVPARIVKRKGSK 174
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 88-177 2.98e-12

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: 63.20  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVL-----------AGVIE 156
Cdd:cd03352    7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgGGWVK 86

                         90       100
                 ....*....|....*....|.
gi 488286804 157 PPSAAPVVIENEVVIGANAVV 177
Cdd:cd03352   87 IPQLGGVIIGDDVEIGANTTI 107
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 103-214 1.85e-11

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: 59.44  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 103 IGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSA-------APVVIENEVVIGANA 175
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKiyrkwelKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488286804 176 VVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIK 214
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 91-182 2.70e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.00  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  91 IEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGtvlagvieppsaapVVIENEVV 170
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHAN--------------VTIYHAVR 168

                         90
                 ....*....|..
gi 488286804 171 IGANAVVLEGVR 182
Cdd:PRK00892 169 IGNRVIIHSGAV 180
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-174 3.00e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.00  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVL----------AGVIEP 157
Cdd:PRK00892 118 GVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandRGGWVK 197

                         90
                 ....*....|....*...
gi 488286804 158 -PSAAPVVIENEVVIGAN 174
Cdd:PRK00892 198 iPQLGRVIIGDDVEIGAN 215
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 120-215 3.25e-10

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: 56.40  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 120 VVGAGTMID--MGAVLGGRATVGKHCHIGAGTVL--------------------------AGVIEPPSAAPVVIENEVVI 171
Cdd:cd03349    3 SVGDYSYGSgpDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypfyifggeweddAKFDDWPSKGDVIIGNDVWI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488286804 172 GANAVVLEGV---------------RvgegavvaagavvveDVPAHTVVAGVPAKVIKQ 215
Cdd:cd03349   83 GHGATILPGVtigdgaviaagavvtK---------------DVPPYAIVGGNPAKVIRY 126
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 120-213 4.70e-10

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 55.16  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 120 VVGAGTMIDMGAVLGGRA--TVGKHCHIGAGTVLAGV-----------IEPPSAAPVVIENEVVIGANAVVLEGVRVGEG 186
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVTIYDHnhdiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 488286804 187 AVVAAGAVVVEDVPAHTVVAGVPAKVI 213
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 101-213 2.22e-09

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: 54.74  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 101 VEIGDQAVIMMGA-ILNIGAV-VGAGTMI------------------DMGAVLGGRATVGKHCHIGAG-TVLAGViepps 159
Cdd:cd03357   63 IHIGDNFYANFNCtILDVAPVtIGDNVLIgpnvqiytaghpldpeerNRGLEYAKPITIGDNVWIGGGvIILPGV----- 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488286804 160 aapvVIENEVVIGANAVVlegvrvgegavvaagavvVEDVPAHTVVAGVPAKVI 213
Cdd:cd03357  138 ----TIGDNSVIGAGSVV------------------TKDIPANVVAAGNPARVI 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 88-219 2.73e-09

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: 53.95  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAIL-----NIgaVVGAGTMIDMGAVL----GGRATVGKHCHIGAGTVLAGViepp 158
Cdd:cd04645    5 SAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGC---- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804 159 saapvVIENEVVIGANAVVLEGVRVGEGAVVAA--GAVVVEDVPAHTVVAGVPAKVIKQIDDK 219
Cdd:cd04645   79 -----TIGDNCLIGMGAIILDGAVIGKGSIVAAgsLVPPGKVIPPGSLVAGSPAKVVRELTDE 136
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 118-211 2.76e-09

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 54.22  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  118 GAVVGAGTMID--MGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVV 195
Cdd:TIGR01172  67 GARIGRGVFIDhgTGVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVV 146

                          90
                  ....*....|....*.
gi 488286804  196 VEDVPAHTVVAGVPAK 211
Cdd:TIGR01172 147 LKDVPPGATVVGVPAR 162
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 89-177 2.88e-09

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: 56.18  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIREKVEIGDQAVImmGAilniGAVVGAGTMIDMGAVLGGRATVGKHCHIGAG-TVLAGvieppsaapVVIEN 167
Cdd:COG1044  103 AVIDPSAKIGEGVSIGPFAVI--GA----GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNvTIYER---------CVIGD 167

                         90
                 ....*....|
gi 488286804 168 EVVIGANAVV 177
Cdd:COG1044  168 RVIIHSGAVI 177
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 118-209 7.02e-09

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: 51.67  E-value: 7.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 118 GAVVGAGTMID--MGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVV 195
Cdd:cd03354    8 GAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVV 87

                         90
                 ....*....|....
gi 488286804 196 VEDVPAHTVVAGVP 209
Cdd:cd03354   88 TKDVPANSTVVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 91-224 7.15e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 55.04  E-value: 7.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  91 IEPGALIREKVEIgDQAVimmGAILNIGAVVGAGTMIDMGAVLGG--RATVGKHCHIGAGTVLAgvieppsaAPVVIENE 168
Cdd:PLN02739 208 IHPAARIGKGILL-DHGT---GVVIGETAVIGDRVSILHGVTLGGtgKETGDRHPKIGDGALLG--------ACVTILGN 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488286804 169 VVIGANAVVLEGvrvgegavvaagAVVVEDVPAHTVVAGVPAKVIKQIDDKTKSKT 224
Cdd:PLN02739 276 ISIGAGAMVAAG------------SLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLT 319
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 88-219 1.80e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 52.34  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILN-----IgaVVGAGTMIDMGAVL----GGRATVGKHCHIGAGTVLAGViepp 158
Cdd:COG0663   16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGC---- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804 159 saapvVIENEVVIGANAVVLEGVRVGEGAVVAA--GAVVVEDVPAHTVVAGVPAKVIKQIDDK 219
Cdd:COG0663   90 -----TIGDNVLIGMGAIVLDGAVIGDGSIVGAgaLVTEGKVVPPGSLVVGSPAKVVRELTEE 147
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 119-189 1.23e-07

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: 47.63  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286804 119 AVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVV 189
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVI 71
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 100-213 4.58e-07

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 46.83  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 100 KVEIGDQAVIMMGA-ILNIGAVVgagtmidmgavLGGRATVGKHCHIGAGT-----VLAGVIeppsAAPVVIENEVVIGA 173
Cdd:cd05825    3 NLTIGDNSWIGEGVwIYNLAPVT-----------IGSDACISQGAYLCTGShdyrsPAFPLI----TAPIVIGDGAWVAA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488286804 174 NAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVI 213
Cdd:cd05825   68 EAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 89-182 1.59e-06

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: 48.09  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIREKVEIGDqavimmgailniGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGtvlagvieppsaapVVIENE 168
Cdd:COG1044   97 PGIHPSAVIDPSAKIGE------------GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDG--------------VVIGDD 150

                         90
                 ....*....|....
gi 488286804 169 VVIGANAVVLEGVR 182
Cdd:COG1044  151 CVLHPNVTIYERCV 164
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 89-181 1.62e-06

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 47.43  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIREKVEIGDQAVImmGAilniGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGviEP--------PSa 160
Cdd:cd03351    6 AIVDPGAKIGENVEIGPFCVI--GP----NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGE--APqdlkykgePT- 76

                         90       100
                 ....*....|....*....|.
gi 488286804 161 apvvienEVVIGANAVVLEGV 181
Cdd:cd03351   77 -------RLEIGDNNTIREFV 90
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 89-181 3.29e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 46.55  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIREKVEIGDQAVImmGAilniGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVLAGviEPPSAAPVVIENE 168
Cdd:PRK12461   6 AVIDPSAKLGSGVEIGPFAVI--GA----NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQDFTYKGEESR 77

                         90
                 ....*....|...
gi 488286804 169 VVIGANAVVLEGV 181
Cdd:PRK12461  78 LEIGDRNVIREGV 90
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 162-221 7.89e-06

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 45.38  E-value: 7.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 162 PVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTK 221
Cdd:PRK09527 131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDK 190
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 162-216 1.18e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 44.42  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488286804 162 PVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQI 216
Cdd:PRK10092 129 PVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 87-149 1.51e-05

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: 43.73  E-value: 1.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804  87 INARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGT 149
Cdd:cd05636    4 IEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSV 66
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 87-176 2.38e-05

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 44.68  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  87 INARIEPGALIREkveigdqaVIMMGailniGAVVGAGTMIDmgavlggRATVGKHCHIGAGTVLAGVIEPPSAAPVVIE 166
Cdd:COG0448  308 RGVRVESGAVVEN--------SVIMP-----GVVIGEGAVIE-------NAIIDKNVVIPPGVVIGEDPEEDRKRFTVSS 367

                         90
                 ....*....|
gi 488286804 167 NEVVIGANAV 176
Cdd:COG0448  368 GIVVVGKGAV 377
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 88-215 3.12e-05

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: 43.55  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGA------------------ILNIGAVV-------GAGTMIDMGAVlgGRATVGKH 142
Cdd:cd03352   43 DCVIHPNVTIYEGCIIGDRVIIHSGAvigsdgfgfapdgggwvkIPQLGGVIigddveiGANTTIDRGAL--GDTVIGDG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 143 ------------CHIGAGTVLAG--VIeppsAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGV 208
Cdd:cd03352  121 tkidnlvqiahnVRIGENCLIAAqvGI----AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGT 196


                 ....*..
gi 488286804 209 PAKVIKQ 215
Cdd:cd03352  197 PAQPHRE 203
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 91-152 4.69e-05

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: 43.86  E-value: 4.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488286804  91 IEPGALIREKVEIGDQAVIMMGAILnIGAVVGAGTMIDM----GAVLGGRATVGKHCHIGAGTVLA 152
Cdd:COG1207  275 IDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKYsvieDAVVGAGATVGPFARLRPGTVLG 339
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 91-219 4.98e-05

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: 42.36  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  91 IEPGALIREKVEIGDQAVIMMGAIL--NIGA-VVGAGTMIDMGAVLGGR----ATVGKHCHIGAGTVLAGVIeppsaapv 163
Cdd:cd04745    9 VHPTAVLIGDVIIGKNCYIGPHASLrgDFGRiVIRDGANVQDNCVIHGFpgqdTVLEENGHIGHGAILHGCT-------- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488286804 164 vIENEVVIGANAVVLEG--VRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDK 219
Cdd:cd04745   81 -IGRNALVGMNAVVMDGavIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDE 137
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 157-221 9.25e-05

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 41.78  E-value: 9.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286804 157 PPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQIDDKTK 221
Cdd:PRK09677 125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETK 189
cysE PRK11132
serine acetyltransferase; Provisional
 119-213 9.49e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 42.38  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 119 AVVGAGTMID--MGAVLGGRATV---------------GKHC---H--------IGAGTVLAGVIEPPSAAPvvienevv 170
Cdd:PRK11132 148 AKIGRGIMLDhaTGIVIGETAVIendvsilqsvtlggtGKTSgdrHpkiregvmIGAGAKILGNIEVGRGAK-------- 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488286804 171 IGANAVVLEGVrvgegavvaagavvvedvPAHTVVAGVPAKVI 213
Cdd:PRK11132 220 IGAGSVVLQPV------------------PPHTTAAGVPARIV 244
PRK10502 PRK10502
putative acyl transferase; Provisional
 89-215 1.32e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.47  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIRE--------KVEIGDQAVIMMGAIL-NIGAVvgagtmidmgavlggraTVGKHCHIGAGTVLAG---VIE 156
Cdd:PRK10502  52 AKIGKGVVIRPsvritypwKLTIGDYAWIGDDVWLyNLGEI-----------------TIGAHCVISQKSYLCTgshDYS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804 157 PPS----AAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQ 215
Cdd:PRK10502 115 DPHfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 110-182 1.44e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 1.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804 110 MMGAILNIGAVVGAGTMIDMGAVLGGRATVGKHCHIGAGTVlagvIEppsaAPVVIENEVVIGANAVVLEGVR 182
Cdd:PRK00892  86 RLAQLFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAV----IG----AGVVIGDGVVIGAGAVIGDGVK 150
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 88-145 2.83e-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: 40.77  E-value: 2.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGG------------RATVGKHCHI 145
Cdd:COG1043   19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptRLEIGDNNTI 88
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
88-181 3.06e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.85  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDqavimmgailnigavvgaGTMIDMGAVLGGRATVGKHCHIGAGTVLAGviEPP----SAAPV 163
Cdd:PRK05289  20 NVEIGPFCVIGPNVVIGD------------------GTVIGSHVVIDGHTTIGKNNRIFPFASIGE--DPQdlkyKGEPT 79

                         90
                 ....*....|....*...
gi 488286804 164 vienEVVIGANAVVLEGV 181
Cdd:PRK05289  80 ----RLVIGDNNTIREFV 93
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 91-152 3.60e-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: 40.10  E-value: 3.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286804  91 IEPGALIREKVEIGDQAVIMMGAILN-----IGAVVGAGTMIDmGAVLGGRATVGKHCHIGAGTVLA 152
Cdd:cd03353   24 IDPGVILEGKTVIGEDCVIGPNCVIKdstigDGVVIKASSVIE-GAVIGNGATVGPFAHLRPGTVLG 89
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 88-212 6.22e-04

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: 39.72  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAILNIGAVVGAGTMIDMGAVLGG-----------------------------RAT 138
Cdd:cd03351   17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptrleigdnntirefvtihRGT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 139 --------------------------VGKHCHIGAGTVLAGvieppsaaPVVIENEVVIGANAVVLEGVRVGEGAVVAAG 192
Cdd:cd03351   97 aqgggvtrignnnllmayvhvahdcvIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                        170       180
                 ....*....|....*....|
gi 488286804 193 AVVVEDVPAHTVVAGVPAKV 212
Cdd:cd03351  169 SGVVQDVPPYVIAAGNRARL 188
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-214 9.74e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.85  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  89 ARIEPGALIREKVEIGD-----QAVIMMGAILN----IG-AVVGAGTMIDMGA-------VLGGRATVGKHCHIGAGTVL 151
Cdd:PRK14353 316 ARLRPGAELGEGAKVGNfvevkNAKLGEGAKVNhltyIGdATIGAGANIGAGTitcnydgFNKHRTEIGAGAFIGSNSAL 395

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488286804 152 AgvieppsaAPVVIENEVVIGANAVVlegvrvgegavvaagavvVEDVPAHTVVAGVPAKVIK 214
Cdd:PRK14353 396 V--------APVTIGDGAYIASGSVI------------------TEDVPDDALALGRARQETK 432
PLN02694 PLN02694
serine O-acetyltransferase
 119-229 1.03e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 39.24  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 119 AVVGAGTMID--MGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVV 196
Cdd:PLN02694 167 AKIGKGILFDhaTGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVL 246

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488286804 197 EDVPAHTVVAGVPAKVIkqiddKTKSKTEILEE 229
Cdd:PLN02694 247 IDVPPRTTAVGNPARLV-----GGKEKPAKHEE 274
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
118-147 1.21e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 488286804  118 GAVVGAGTMIDMGAVLGGRATVGKHCHIGA 147
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PLN02357 PLN02357
serine acetyltransferase
 118-221 1.54e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 39.09  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 118 GAVVGAGTMID--MGAVLGGRATVGKHCHIGAGTVLAGVIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVV 195
Cdd:PLN02357 232 GAKIGQGILLDhaTGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 311

                         90       100
                 ....*....|....*....|....*.
gi 488286804 196 VEDVPAHTVVAGVPAKVIKQIDDKTK 221
Cdd:PLN02357 312 LKDVPPRTTAVGNPARLIGGKENPIK 337
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-214 1.91e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 38.76  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  88 NARIEPGALIREKVEIGDQAVImmGAILNI-GAVVGAGTMIDMGAVLGGrATVGKHCHIGAGTVLA---GVIEPPS---- 159
Cdd:PRK14360 319 GVKIGPYAHLRPEAQIGSNCRI--GNFVEIkKSQLGEGSKVNHLSYIGD-ATLGEQVNIGAGTITAnydGVKKHRTvigd 395

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286804 160 ----------AAPVVIENEVVIGANAVVlegvrvgegavvaagavvVEDVPAHTVVAGVPAKVIK 214
Cdd:PRK14360 396 rsktgansvlVAPITLGEDVTVAAGSTI------------------TKDVPDNSLAIARSRQVIK 442
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 87-177 2.10e-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: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  87 INARIEPGALIREkveigdqaVIMMGailniGAVVGAGTMIDmgavlggRATVGKHCHIGAGTVLAGVIEPPSAAPVVIE 166
Cdd:cd04651   33 RGVRVGSGSVVED--------SVIMP-----NVGIGRNAVIR-------RAIIDKNVVIPDGVVIGGDPEEDRARFYVTE 92

                         90
                 ....*....|..
gi 488286804 167 NE-VVIGANAVV 177
Cdd:cd04651   93 DGiVVVGKGMVI 104
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 88-149 2.56e-03

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: 36.10  E-value: 2.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488286804  88 NARIEPGALIREKVEIGDQAVIMMGAIL----NIGAVVGAGTMIDmGAVLGGRAT-----------VGKHCHIGAGT 149
Cdd:cd05635   17 DAVIEPFAVIEGPVYIGPGSRVKMGARIygntTIGPTCKIGGEVE-DSIIEGYSNkqhdgflghsyLGSWCNLGAGT 92
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 65-205 7.63e-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: 36.24  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  65 IEDYVVENDArnSAIPFldlkdinARIEPGALIREKVEIGD-----QAVIMMGAILN----IG-AVVGAGTMIdmGA--- 131
Cdd:cd03353   65 IEGAVIGNGA--TVGPF-------AHLRPGTVLGEGVHIGNfveikKSTIGEGSKANhlsyLGdAEIGEGVNI--GAgti 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804 132 ------VLGGRATVGKHCHIGAGTVLAgvieppsaAPVVIENEVVIGANAVVlegvrvgegavvaagavvVEDVPAHTVV 205
Cdd:cd03353  134 tcnydgVNKHRTVIGDNVFIGSNSQLV--------APVTIGDGATIAAGSTI------------------TKDVPPGALA 187
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 61-215 8.25e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.05  E-value: 8.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286804  61 NKEKIEDYVVENDArnSAIPFldlkdinARIEPGALIREKVEIGDQAVIMmgailniGAVVGAGTMIDMGAVLGGrATVG 140
Cdd:PRK14357 300 IRSECEKSVIEDDV--SVGPF-------SRLREGTVLKKSVKIGNFVEIK-------KSTIGENTKAQHLTYLGD-ATVG 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286804 141 KHCHIGAGTVLAGvIEPPSAAPVVIENEVVIGANAVVLEGVRVGEGAVVAAGAVVVEDVPAHTVVAGVPAKVIKQ 215
Cdd:PRK14357 363 KNVNIGAGTITCN-YDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
 
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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