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Conserved domains on  [gi|488994759|ref|WP_002905478|]
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MULTISPECIES: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Streptococcus]

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 ...
 8-232 1.20e-119

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: 339.81  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759    8 AQEIIKFIADAKKKTPVKVTFDGELHG-SIPWSVVKLGN----VLFGDWEEIKPLL-ANLEENKTYVVEQDARNSAVPLL 81
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQvDFPESIKKFGSghsgVLFGEWEDIEPFIeANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759   82 DKRDINARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEP 161
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994759  162 VRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQQKTALEDALRTL 232
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 ...
 8-232 1.20e-119

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: 339.81  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759    8 AQEIIKFIADAKKKTPVKVTFDGELHG-SIPWSVVKLGN----VLFGDWEEIKPLL-ANLEENKTYVVEQDARNSAVPLL 81
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQvDFPESIKKFGSghsgVLFGEWEDIEPFIeANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759   82 DKRDINARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEP 161
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994759  162 VRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQQKTALEDALRTL 232
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 87-209 1.97e-44

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: 145.60  E-value: 1.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGD 166
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488994759 167 NVLIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGVPA 209
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGsVVVAGSLP 139
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 78-230 2.91e-40

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: 138.71  E-value: 2.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  78 VPLLDK--RDINARIEPGAIIRDQVEIGDNaVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIE 155
Cdd:COG2171   86 VPLKFDyfKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 156 PASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGV-----------P 208
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGsVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 488994759 209 ARVIKTIDEKTQQKTALEDALR 230
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 89-230 1.86e-37

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 131.85  E-value: 1.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  89 RIEPGAIIRDQVEIGDNaVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNV 168
Cdd:PRK11830 105 RVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPVIIEDNC 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 169 LIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGV-----------PARVIKTIDEKTQQ 221
Cdd:PRK11830 184 FIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGsVVVPGSlpskdggyslyCAVIVKKVDAKTRS 263


                 ....*....
gi 488994759 222 KTALEDALR 230
Cdd:PRK11830 264 KTSINELLR 272
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 7-82 4.66e-30

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: 106.86  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759    7 NAQEIIKFIADAKKKTPVKVTFDGELHG-SIPWSVVKL-----GNVLFGDWEEIKPLLANLEEN-KTYVVEQDARNSAVP 79
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGeDLEFEEIKVfgsgdFGVLFGDWKEIKPFLEANKDKiEDYHIENDRRNSAIP 80


                  ...
gi 488994759   80 LLD 82
Cdd:pfam08503  81 LLD 83
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 8-232 1.20e-119

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: 339.81  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759    8 AQEIIKFIADAKKKTPVKVTFDGELHG-SIPWSVVKLGN----VLFGDWEEIKPLL-ANLEENKTYVVEQDARNSAVPLL 81
Cdd:TIGR03532   1 AQEIIRYIGNAKKSTPVKVYVKGDLEQvDFPESIKKFGSghsgVLFGEWEDIEPFIeANKDKIKDYRIENDRRNSAIPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759   82 DKRDINARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEP 161
Cdd:TIGR03532  81 DLKNINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994759  162 VRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQQKTALEDALRTL 232
Cdd:TIGR03532 161 VVIEDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 87-209 1.97e-44

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: 145.60  E-value: 1.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGD 166
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488994759 167 NVLIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGVPA 209
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGsVVVAGSLP 139
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 78-230 2.91e-40

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: 138.71  E-value: 2.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  78 VPLLDK--RDINARIEPGAIIRDQVEIGDNaVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIE 155
Cdd:COG2171   86 VPLKFDyfKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 156 PASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGV-----------P 208
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGsVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 488994759 209 ARVIKTIDEKTQQKTALEDALR 230
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 89-230 1.86e-37

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 131.85  E-value: 1.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  89 RIEPGAIIRDQVEIGDNaVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNV 168
Cdd:PRK11830 105 RVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPVIIEDNC 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 169 LIGANAVVIEGVQIGSGSVVAAGAIVTQ---------------DVPEN-VVVAGV-----------PARVIKTIDEKTQQ 221
Cdd:PRK11830 184 FIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGsVVVPGSlpskdggyslyCAVIVKKVDAKTRS 263


                 ....*....
gi 488994759 222 KTALEDALR 230
Cdd:PRK11830 264 KTSINELLR 272
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 90-209 1.19e-32

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: 117.21  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759   90 IEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGviepasaePVRVGDNVL 169
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488994759  170 IGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPA 209
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 90-208 3.01e-32

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: 116.04  E-value: 3.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGviepasaePVRVGDNVL 169
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488994759 170 IGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVP 208
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
95-220 6.60e-32

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 113.43  E-value: 6.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  95 IIRDQVEIGDNAVIMMGAVINIG-AEIGAGTMIDMGAIL--GGRAIVGKNSHVGAGAVLAGV--------IEPASAEPVR 163
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488994759 164 VGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQ 220
Cdd:COG0110   84 IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 7-82 4.66e-30

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: 106.86  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759    7 NAQEIIKFIADAKKKTPVKVTFDGELHG-SIPWSVVKL-----GNVLFGDWEEIKPLLANLEEN-KTYVVEQDARNSAVP 79
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGeDLEFEEIKVfgsgdFGVLFGDWKEIKPFLEANKDKiEDYHIENDRRNSAIP 80


                  ...
gi 488994759   80 LLD 82
Cdd:pfam08503  81 LLD 83
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 87-218 5.40e-25

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 96.63  E-value: 5.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVIN-----IgaEIGAGTMIDMGAIL----GGRAIVGKNSHVGAGAVLAGViepa 157
Cdd:COG0663   16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGC---- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994759 158 saepvRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQD--VPENVVVAGVPARVIKTIDEK 218
Cdd:COG0663   90 -----TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEE 147
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 80-212 1.91e-24

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


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 95.18  E-value: 1.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  80 LLDKRDINARIEPGAIIR--DQVEIGDNAVIMMGAVINIGAE--IGAGTMIdmgailggraivGKN------SH-VGAGA 148
Cdd:cd03357   41 LFGSVGENVYIEPPFHCDygYNIHIGDNFYANFNCTILDVAPvtIGDNVLI------------GPNvqiytaGHpLDPEE 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488994759 149 VLAGviePASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVI 212
Cdd:cd03357  109 RNRG---LEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 87-218 4.01e-24

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 93.63  E-value: 4.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVI-----NIgaEIGAGTMIDMGAIL----GGRAIVGKNSHVGAGAVLAGViepa 157
Cdd:cd04645    5 SAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGC---- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994759 158 saepvRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQD--VPENVVVAGVPARVIKTIDEK 218
Cdd:cd04645   79 -----TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDE 136
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 100-212 2.22e-23

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: 90.59  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 100 VEIGDNAVIMMGAVINIGA--EIGAGTMIdmgailGGRAIVGKNSHvGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVI 177
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGgiTIGDNVLI------GPNVTIYDHNH-DIDDPERPIEQGVTSAPIVIGDDVWIGANVVIL 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488994759 178 EGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVI 212
Cdd:cd04647   75 PGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 114-218 3.59e-23

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: 91.68  E-value: 3.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 114 INIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:COG1045   68 IHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGAN 147

                         90       100
                 ....*....|....*....|....*..
gi 488994759 192 AIVTQDVPENVVVAGVPARVIKTIDEK 218
Cdd:COG1045  148 SVVLKDVPPGSTVVGVPARIVKRKGSK 174
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 102-213 1.07e-22

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: 89.10  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 102 IGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAE-------PVRVGDNVLIGANA 174
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIyrkwelkGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488994759 175 VVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIK 213
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 111-208 7.88e-21

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: 83.64  E-value: 7.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 111 GAVINIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVV 188
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                         90       100
                 ....*....|....*....|
gi 488994759 189 AAGAIVTQDVPENVVVAGVP 208
Cdd:cd03354   82 GANAVVTKDVPANSTVVGVP 101
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 108-210 1.16e-18

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 79.64  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  108 IMMGAVINIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGV-IEPASAEPvRVGDNVLIGANAVVIEGVQIGS 184
Cdd:TIGR01172  58 VLTGVDIHPGARIGRGVFIDhgTGVVIGETAVIGDDVTIYHGVTLGGTgKEKGKRHP-TIGEGVMIGAGAKVLGNIEVGE 136

                          90       100
                  ....*....|....*....|....*.
gi 488994759  185 GSVVAAGAIVTQDVPENVVVAGVPAR 210
Cdd:TIGR01172 137 NAKIGANSVVLKDVPPGATVVGVPAR 162
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 159-215 1.55e-18

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 79.86  E-value: 1.55e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488994759 159 AEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTI 215
Cdd:PRK10092 127 GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
PLN02739 PLN02739
serine acetyltransferase
 109-230 1.94e-18

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 82.78  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 109 MMGAVINIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGS 186
Cdd:PLN02739 203 VFGIDIHPAARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGA 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488994759 187 VVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQQKTALEDALR 230
Cdd:PLN02739 283 MVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYDATR 326
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 95-213 3.26e-18

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: 77.97  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  95 IIRDQVEIGDNAVIMMGAVINIGAE---IGAGTMIDMGAILGGRAIVGKNSHVGAGavlagviepasaePVRVGDNVLIG 171
Cdd:cd03349   17 VGGDKLSIGKFCSIAPGVKIGLGGNhptDWVSTYPFYIFGGEWEDDAKFDDWPSKG-------------DVIIGNDVWIG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488994759 172 ANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIK 213
Cdd:cd03349   84 HGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 161-221 1.52e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 77.74  E-value: 1.52e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994759 161 PVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQQ 221
Cdd:PRK09527 131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQ 191
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 87-211 2.08e-17

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: 78.52  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGG------------RAIVGKN------------- 141
Cdd:COG1043   19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptRLEIGDNntirefvtihrgt 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 142 ------------------SHVG------------AGAVLAGviepasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:COG1043   99 vqgggvtrigddnllmayVHVAhdcvvgnnvilaNNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGG 170

                        170       180
                 ....*....|....*....|
gi 488994759 192 AIVTQDVPENVVVAGVPARV 211
Cdd:COG1043  171 SGVVKDVPPYVLAAGNPARL 190
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 87-210 3.76e-17

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: 76.68  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVI------------------NIGA-------EIGAGTMIDMGAIlgGRAIVGK- 140
Cdd:cd03352   43 DCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgggwvkipQLGGviigddvEIGANTTIDRGAL--GDTVIGDg 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 141 -----------NSHVGAGAVLAG--VIepasAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGV 207
Cdd:cd03352  121 tkidnlvqiahNVRIGENCLIAAqvGI----AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGT 196


                 ...
gi 488994759 208 PAR 210
Cdd:cd03352  197 PAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 87-210 7.82e-17

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: 77.75  E-value: 7.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVIniGA----------------------------EIGAGTMIDMGAIlgGRAIV 138
Cdd:COG1044  150 DCVLHPNVTIYERCVIGDRVIIHSGAVI--GAdgfgfapdedggwvkipqlgrvvigddvEIGANTTIDRGAL--GDTVI 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 139 GK------------NSHVGAGAVLAG--VIepasAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVV 204
Cdd:COG1044  226 GDgtkidnlvqiahNVRIGEHTAIAAqvGI----AGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVY 301


                 ....*.
gi 488994759 205 AGVPAR 210
Cdd:COG1044  302 SGSPAQ 307
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 90-224 2.69e-16

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: 73.17  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQVEIGDNAVIMMGAVI--NIGA-EIGAGTMIDMGAILGGR----AIVGKNSHVGAGAVLAGViepasaepv 162
Cdd:cd04745    9 VHPTAVLIGDVIIGKNCYIGPHASLrgDFGRiVIRDGANVQDNCVIHGFpgqdTVLEENGHIGHGAILHGC--------- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994759 163 RVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQ--DVPENVVVAGVPARVIKTI-DEKTQQKTA 224
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELsDEEVAWKTR 144
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 87-211 1.07e-15

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: 73.62  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGG------------RAIVGKN------------- 141
Cdd:cd03351   17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptRLEIGDNntirefvtihrgt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 142 ------------------SHVG------------AGAVLAGviepasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:cd03351   97 aqgggvtrignnnllmayVHVAhdcvignnvilaNNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                        170       180
                 ....*....|....*....|
gi 488994759 192 AIVTQDVPENVVVAGVPARV 211
Cdd:cd03351  169 SGVVQDVPPYVIAAGNRARL 188
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 156-220 9.55e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 69.90  E-value: 9.55e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488994759 156 PASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKTIDEKTQ 220
Cdd:PRK09677 125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETK 189
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
87-211 1.77e-14

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 70.51  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGG------------RAIVGKN------------- 141
Cdd:PRK05289  20 NVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEdpqdlkykgeptRLVIGDNntirefvtinrgt 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 142 ------------------SHVG------------AGAVLAGviepasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:PRK05289 100 vqgggvtrigdnnllmayVHVAhdcvvgnhvilaNNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGM 171

                        170       180
                 ....*....|....*....|
gi 488994759 192 AIVTQDVPENVVVAGVPARV 211
Cdd:PRK05289 172 SGVSQDVPPYVLAEGNPARL 191
PLN02694 PLN02694
serine O-acetyltransferase
 114-212 3.15e-14

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 70.06  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 114 INIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:PLN02694 163 IHPAAKIGKGILFDhaTGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAG 242

                         90       100
                 ....*....|....*....|.
gi 488994759 192 AIVTQDVPENVVVAGVPARVI 212
Cdd:PLN02694 243 SVVLIDVPPRTTAVGNPARLV 263
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-232 2.57e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.86  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVI------------------NIGA-------EIGAGTMIDMGAIlgGRAIVGK- 140
Cdd:PRK00892 154 DCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandrggwvkipQLGRviigddvEIGANTTIDRGAL--DDTVIGEg 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 141 -----------NSHVGAGAVLAG-VIEPASAepvRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPE-NVVVAGV 207
Cdd:PRK00892 232 vkidnlvqiahNVVIGRHTAIAAqVGIAGST---KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSSGI 308

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488994759 208 PAR----------VIKTIDEKTQQKTALEDALRTL 232
Cdd:PRK00892 309 PAQpnkewlrtaaRLRRLDELRKRLKALEKKVEQL 343
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 118-195 2.65e-13

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: 63.04  E-value: 2.65e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488994759 118 AEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVT 195
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
PLN02357 PLN02357
serine acetyltransferase
 114-212 2.96e-13

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 67.98  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 114 INIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:PLN02357 229 IHPGAKIGQGILLDhaTGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAG 308

                         90       100
                 ....*....|....*....|.
gi 488994759 192 AIVTQDVPENVVVAGVPARVI 212
Cdd:PLN02357 309 SVVLKDVPPRTTAVGNPARLI 329
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 90-213 3.50e-13

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: 67.74  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQVEIGDNAVIMMGAVInIGAEIGAGTMIDM----GAILGGRAIVG-----------------------KNS 142
Cdd:COG1207  275 IDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKYsvieDAVVGAGATVGpfarlrpgtvlgegvkignfvevKNS 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 143 HVGAGA------------------VLAGVI----EPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPE 200
Cdd:COG1207  354 TIGEGSkvnhlsyigdaeigegvnIGAGTItcnyDGVNKHRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPA 433

                        170
                 ....*....|....
gi 488994759 201 N-VVVAGVPARVIK 213
Cdd:COG1207  434 GaLAIARARQRNIE 447
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 90-176 4.67e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 67.09  E-value: 4.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLagviepasAEPVRVGDNVL 169
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI--------YHAVRIGNRVI 174


                 ....*..
gi 488994759 170 IGANAVV 176
Cdd:PRK00892 175 IHSGAVI 181
PRK10502 PRK10502
putative acyl transferase; Provisional
 88-214 6.82e-13

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 64.59  E-value: 6.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQV--------EIGDNAVIMMGAVINIGAEIgagtmidmgailggraIVGKNSHVGAGAVL-AGVIEPAS 158
Cdd:PRK10502  52 AKIGKGVVIRPSVritypwklTIGDYAWIGDDVWLYNLGEI----------------TIGAHCVISQKSYLcTGSHDYSD 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994759 159 ------AEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKT 214
Cdd:PRK10502 116 phfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-193 1.41e-12

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: 65.81  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLagviepasAEPVRVGDN 167
Cdd:COG1044   97 PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI--------YERCVIGDR 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488994759 168 VLIGANA-------------------------VVIE-GVQIGSGSVVAAGAI 193
Cdd:COG1044  169 VIIHSGAvigadgfgfapdedggwvkipqlgrVVIGdDVEIGANTTIDRGAL 220
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-213 1.67e-12

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 66.10  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVImmGAVINI-GAEIGAGTMIDMGAILGGrAIVGKNSHVGAGAVLA---GViepaSAEPV 162
Cdd:PRK14360 319 GVKIGPYAHLRPEAQIGSNCRI--GNFVEIkKSQLGEGSKVNHLSYIGD-ATLGEQVNIGAGTITAnydGV----KKHRT 391

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488994759 163 RVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIK 213
Cdd:PRK14360 392 VIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 90-201 4.28e-12

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: 62.82  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQVEIGDNAVIMMGAVIN-----IGAEIGAGTMIDmGAILGGRAIVG-----------------------KN 141
Cdd:cd03353   24 IDPGVILEGKTVIGEDCVIGPNCVIKdstigDGVVIKASSVIE-GAVIGNGATVGpfahlrpgtvlgegvhignfveiKK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 142 SHVGAGA------------------VLAGVI----EPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVP 199
Cdd:cd03353  103 STIGEGSkanhlsylgdaeigegvnIGAGTItcnyDGVNKHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVP 182


                 ..
gi 488994759 200 EN 201
Cdd:cd03353  183 PG 184
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 87-232 7.80e-12

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 63.05  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759   87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGG------------RAIVGKN------------- 141
Cdd:TIGR01852  16 NVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGvpqdlkykgektRLIIGDNntirefvtinrgt 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  142 ------------------SHVG------------AGAVLAGVIEpasaepvrVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:TIGR01852  96 asgggvtrignnnllmaySHIAhdcvvgnhvilaNNATLAGHVE--------VGDYAIIGGLVAVHQFVRIGRYAMIGGL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488994759  192 AIVTQDVPENVVVAGVPARVI---------KTIDEKtqQKTALEDALRTL 232
Cdd:TIGR01852 168 SAVSKDVPPYCLAEGNRARLRglnivglrrRGFSRE--EITAIKRAYRTL 215
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 159-212 7.83e-12

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: 59.93  E-value: 7.83e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488994759 159 AEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVI 212
Cdd:cd05825   54 TAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-203 4.80e-11

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 61.66  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGdNAVIMMGAVINIGAEIGAGTMIdmgailgGRAIVGKNSHVGAGAVLAGViEPASAEPVRVGDN 167
Cdd:PRK14356 334 ARLRPGAVLEEGARVG-NFVEMKKAVLGKGAKANHLTYL-------GDAEIGAGANIGAGTITCNY-DGVNKHRTVIGEG 404

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488994759 168 VLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVV 203
Cdd:PRK14356 405 AFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
PLN02296 PLN02296
carbonate dehydratase
 78-219 9.21e-11

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 60.14  E-value: 9.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  78 VPLLDKrdiNARIEPGAIIRDQVEIGDNAVIMMGAVI-----NIgaEIGAGTMIDMGAI-------LGGR---AIVGKNS 142
Cdd:PLN02296  52 APVVDK---DAFVAPSASVIGDVQVGRGSSIWYGCVLrgdvnSI--SVGSGTNIQDNSLvhvaktnLSGKvlpTIIGDNV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 143 HVGAGAVLAGVIepasaepvrVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQD--VPENVVVAGVPARVIK--TIDEK 218
Cdd:PLN02296 127 TIGHSAVLHGCT---------VEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRklTEEEI 197


                 .
gi 488994759 219 T 219
Cdd:PLN02296 198 A 198
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 87-195 1.34e-10

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: 57.81  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDmGAILGGrAIVGKNSHVGAGAVLAGVIEPASAEPVRVGD 166
Cdd:cd04649    1 GVRIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVE-GRISSG-VIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                         90       100
                 ....*....|....*....|....*....
gi 488994759 167 NVLIGANAVVieGVQIGSGSVVAAGAIVT 195
Cdd:cd04649   79 RCLLGANSGI--GISLGDNCIVEAGLYVT 105
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 87-211 2.08e-10

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 58.88  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILG------------GRAIVGK-------------- 140
Cdd:PRK12461  17 GVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGdepqdftykgeeSRLEIGDrnviregvtihrgt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 141 ----------------NSHVGAGAVLAG----VIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPE 200
Cdd:PRK12461  97 kgggvtrigndnllmaYSHVAHDCQIGNnvilVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPP 176

                        170
                 ....*....|.
gi 488994759 201 NVVVAGVPARV 211
Cdd:PRK12461 177 YCMMAGHPTNV 187
cysE PRK11132
serine acetyltransferase; Provisional
 114-212 2.85e-10

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 58.55  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 114 INIGAEIGAGTMID--MGAILGGRAIVGKNSHVGAGAVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAG 191
Cdd:PRK11132 144 IHPAAKIGRGIMLDhaTGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223

                         90       100
                 ....*....|....*....|.
gi 488994759 192 AIVTQDVPENVVVAGVPARVI 212
Cdd:PRK11132 224 SVVLQPVPPHTTAAGVPARIV 244
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 88-217 2.85e-10

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 56.81  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGDNAVIMMGAV-------INIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLAGViepasae 160
Cdd:cd04650    7 AYVHPTSYVIGDVVIGELTSVWHYAVirgdndsIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGA------- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488994759 161 pvRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQ--DVPENVVVAGVPARVIKTIDE 217
Cdd:cd04650   80 --KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPgkEIPDYSLVLGVPAKVVRKLTE 136
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 85-218 3.78e-10

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 57.51  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  85 DINARIEPGAIIRDQVEIGdnAVIMMGAVINIGAEIG-----AGTMIDMGAILGGRA----IVGKNSHVGAGAVLAGVIe 155
Cdd:PRK13627  14 HPTAFVHPSAVLIGDVIVG--AGVYIGPLASLRGDYGrlivqAGANLQDGCIMHGYCdtdtIVGENGHIGHGAILHGCV- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488994759 156 pasaepvrVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVT---QDVPENVVVaGVPARVIKTIDEK 218
Cdd:PRK13627  91 --------IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKagfQGEKRQLLM-GTPARAVRSVSDD 147
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 43-222 4.25e-10

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 58.88  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  43 LGNVLFGDWEEIKPllanleenktYVVEQDAR---NSAV-PLldkrdinARIEPGAIIRDQVEIGdNAVIMMGAVINIGA 118
Cdd:PRK09451 298 LKNCVIGDDCEISP----------YSVVEDANlgaACTIgPF-------ARLRPGAELAEGAHVG-NFVEMKKARLGKGS 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 119 EIGAGTMIdmgailgGRAIVGKNSHVGAGAVLAGViEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDV 198
Cdd:PRK09451 360 KAGHLTYL-------GDAEIGDNVNIGAGTITCNY-DGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDV 431

                        170       180
                 ....*....|....*....|....*
gi 488994759 199 PEN-VVVAGVPARVIKTIDEKTQQK 222
Cdd:PRK09451 432 AENeLVISRVPQRHIQGWQRPVKKK 456
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 83-195 5.02e-10

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: 56.44  E-value: 5.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  83 KRDINARIEPGAIIRDQVEIGDNAVIMMGAVIN----IG--AEIGAGTMIDMGAILG----------------------- 133
Cdd:cd05636    1 KDEIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEgpviIGkgCEIGPNAYIRGYTVLGdgcvvgnsvevknsiimdgtkvp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 134 -----GRAIVGKNSHVGAGAVLAGVIEPASAEPVRV----------------GDNVLIGANAVVIEGVQIGSGSVVAAGA 192
Cdd:cd05636   81 hlnyvGDSVLGENVNLGAGTITANLRFDDKPVKVRLkgervdtgrrklgaiiGDGVKTGINVSLNPGVKIGPGSWVYPGC 160


                 ...
gi 488994759 193 IVT 195
Cdd:cd05636  161 VVR 163
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-201 9.64e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.92  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDQVEIGdNAVIMMGAVINIGAEIGAGTMIdmgailgGRAIVGKNSHVGAGAVLA---GViepaSAEPVR 163
Cdd:PRK14354 328 FAHLRPGSVIGEEVKIG-NFVEIKKSTIGEGTKVSHLTYI-------GDAEVGENVNIGCGTITVnydGK----NKFKTI 395

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488994759 164 VGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPEN 201
Cdd:PRK14354 396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-214 1.41e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 57.18  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGdNAVIMMGAVINIGAEIGAGTMIdmgailgGRAIVGKNSHVGAGAVLA---GViepaSAEPVRV 164
Cdd:PRK14353 316 ARLRPGAELGEGAKVG-NFVEVKNAKLGEGAKVNHLTYI-------GDATIGAGANIGAGTITCnydGF----NKHRTEI 383

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488994759 165 GDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIKT 214
Cdd:PRK14353 384 GAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-213 4.42e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 55.92  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  93 GAIIRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAI----------LGGRAIVGKNSHVGAGAVLAGvIEPASAEPV 162
Cdd:PRK14357 306 KSVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIgentkaqhltYLGDATVGKNVNIGAGTITCN-YDGKKKNPT 384

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488994759 163 RVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPENVVVAGVPARVIK 213
Cdd:PRK14357 385 FIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 90-221 6.80e-09

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 53.37  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAIIRDQ---VEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNShvgagavlagVIEPASaepvrVGD 166
Cdd:cd03359   30 IQSDVIIRGDlatVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENC----------VVNAAQ-----IGS 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488994759 167 NVLIGANAVVIEGVQIGSGSVVAAGAIVTQD--VPENVVVAGVPARVIKTIDEKTQQ 221
Cdd:cd03359   95 YVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQE 151
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 126-204 9.20e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.76  E-value: 9.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 126 IDMGAILGGRAIVGKNSHVGAGAVlagvIEPAsaepVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVP--ENVV 203
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAV----IGAG----VVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRigNRVI 174


                 .
gi 488994759 204 V 204
Cdd:PRK00892 175 I 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 100-176 1.66e-08

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: 52.80  E-value: 1.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488994759 100 VEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGRAIVGKNSHVGAGAVLagviepasAEPVRVGDNVLIGANAVV 176
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI--------YEGCIIGDRVIIHSGAVI 70
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 88-200 1.69e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 51.13  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGDnavimmgAVINIGAEIGAGTMIDMGAILGGRAIvGKNSHVGAGAVLAGvIEPASAEPVRVGDN 167
Cdd:PRK14358 335 ARLRPGTVLGEGVHIGN-------FVETKNARLDAGVKAGHLAYLGDVTI-GAETNVGAGTIVAN-FDGVNKHQSKVGAG 405

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994759 168 VLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPE 200
Cdd:PRK14358 406 VFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPE 438
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 85-194 8.94e-07

Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 47.24  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  85 DINARIEPGAIIRDQVEIGDNAVIMMGAVIN----IGAEIGAGTMIDMGAIL----GGRAIVGKNSHVGAGAVLAGviep 156
Cdd:cd00710    6 DPSAYVHPTAVVIGDVIIGDNVFVGPGASIRadegTPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHG---- 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488994759 157 asaePVRVGDNVLIGANAVVIEGVqIGSGSVVAAGAIV 194
Cdd:cd00710   82 ----PAYIGDNCFIGFRSVVFNAK-VGDNCVIGHNAVV 114
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-212 1.20e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 45.70  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRDqVEIGDNAVIM----MGAVINIGAEIGAGTMIDMGAILG----------------------------G 134
Cdd:PRK14352 295 DAVVGPDTTLTD-VTVGEGASVVrthgSESEIGAGATVGPFTYLRPGTVLGeegklgafvetknatigrgtkvphltyvG 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 135 RAIVGKNSHVGAGAVLA---GViepaSAEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPEN-VVVAGVPAR 210
Cdd:PRK14352 374 DADIGEHSNIGASSVFVnydGV----NKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGaLAVSEGPQR 449


                 ..
gi 488994759 211 VI 212
Cdd:PRK14352 450 NI 451
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-201 1.24e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.50  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  88 ARIEPGAIIRDQVEIGdNAVIMMGAVINIGAEIGAGTMIdmgailgGRAIVGKNSHVGAGAVLA---GVIEPASAepvrV 164
Cdd:PRK14355 333 AHLRPGTELSAHVKIG-NFVETKKIVMGEGSKASHLTYL-------GDATIGRNVNIGCGTITCnydGVKKHRTV----I 400

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488994759 165 GDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPEN 201
Cdd:PRK14355 401 EDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPD 437
PRK10191 PRK10191
putative acyl transferase; Provisional
 117-211 1.84e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 43.34  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 117 GAEIGAGTMIDMG-AILGGRAIVgKNSHVGAG-------AVLAGVIEPASAEPVRVGDNVLIGANAVVIEGVQIGSGSVV 188
Cdd:PRK10191  41 GYEIQAAATIGRRfTIHHGYAVV-INKNVVAGddftirhGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTV 119

                         90       100
                 ....*....|....*....|...
gi 488994759 189 AAGAIVTQDVPENVVVAGVPARV 211
Cdd:PRK10191 120 GAGSVVLDSVPDNALVVGEKARV 142
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 94-226 2.25e-05

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 43.47  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  94 AIIRDQVEIGDNAVIMMGAVINIGAE---IGAGTMIDMGAILGGR----AIVGKNSHVGAGavlaGVIEPAS-AEPVRVG 165
Cdd:cd04646   12 SEIRGDVTIGPGTVVHPRATIIAEAGpiiIGENNIIEEQVTIVNKkpkdPAEPKPMIIGSN----NVFEVGCkCEALKIG 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488994759 166 DNVLIGANAVVIEGVQIGSGSVVAAGAIVTQD--VPENVVVAGVPARVIKTIDEKTQQKTALE 226
Cdd:cd04646   88 NNNVFESKSFVGKNVIITDGCIIGAGCKLPSSeiLPENTVIYGADCLRRTQTDRPKPQTLQLD 150
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 125-212 3.61e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.47  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 125 MIDMGAILGGRAIVGKNSHVGAGAVLAGviepasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDvPENVVV 204
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGA--------NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE-PQDFTY 71


                 ....*...
gi 488994759 205 AGVPARVI 212
Cdd:PRK12461  72 KGEESRLE 79
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
124-197 3.71e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.55  E-value: 3.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488994759 124 TMIDMGAILGGRAIVGKNSHVGAGAVlagvIEPasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIV---TQD 197
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCV----IGP----NVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedPQD 71
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
162-196 5.46e-05

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 39.35  E-value: 5.46e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 488994759  162 VRVGDNVLIGANAVVieGVQIGSGSVVAAGAIVTQ 196
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 151-198 5.65e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.08  E-value: 5.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488994759 151 AGVIEPAS-AEPVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDV 198
Cdd:COG1044   97 PGIHPSAViDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
161-190 2.18e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 2.18e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 488994759  161 PVRVGDNVLIGANAVVIEGVQIGSGSVVAA 190
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 100-209 3.38e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 41.27  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  100 VEIGDNAVIMmGAVINIGA--EIGAGTMIDMGAILGGRAIVGKNSHVGagavlagviepasaePVRVGDNVLIGANAVVI 177
Cdd:TIGR02353 113 AKIGKGVDIG-SLPPVCTDllTIGAGTIVRKEVMLLGYRAERGRLHTG---------------PVTLGRDAFIGTRSTLD 176

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488994759  178 EGVQIGSGSVVAAGAIVT--QDVPENVVVAGVPA 209
Cdd:TIGR02353 177 IDTSIGDGAQLGHGSALQggQSIPDGERWHGSPA 210
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 162-198 6.38e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.70  E-value: 6.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488994759 162 VRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDV 198
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
PLN02472 PLN02472
uncharacterized protein
 78-232 8.29e-04

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 39.56  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  78 VPL---LDKRDINARIEPGAIIRDQVEIGDNAVIMMGAV-------INIG--AEIGAGTMIDMGAI----LGGRAIVGKN 141
Cdd:PLN02472  53 IPLgqwVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVlrgdlnkITVGfcSNVQERCVLHAAWNsptgLPAETLIDRY 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 142 SHVGAGAVL-AGVIEPasaepvrvgdNVLIGANAVVIEGVQIGSGSVVAAGAIVT--QDVPENVVVAGVPARVIKTI-DE 217
Cdd:PLN02472 133 VTIGAYSLLrSCTIEP----------ECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLtNE 202

                        170
                 ....*....|....*
gi 488994759 218 KTQQKTALEDALRTL 232
Cdd:PLN02472 203 ETLEIPKLAVAINDL 217
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 116-209 9.65e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 39.73  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  116 IGAEIGAGTMIDmGAILGGRAIV--GKNSHVGAGAVLA------GVIepaSAEPVRVGDNVLIGANAVVIEGVQIGSGSV 187
Cdd:TIGR02353 596 LGVKIGRGVYID-GTDLTERDLVtiGDDSTLNEGSVIQthlfedRVM---KSDTVTIGDGATLGPGAIVLYGVVMGEGSV 671

                          90       100
                  ....*....|....*....|....
gi 488994759  188 VAAGAIVT--QDVPENVVVAGVPA 209
Cdd:TIGR02353 672 LGPDSLVMkgEEVPAHTRWRGNPA 695
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 125-197 1.71e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 38.57  E-value: 1.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488994759 125 MIDMGAILGGRAIVGKNSHVGAGAVlagvIEPasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIV---TQD 197
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCV----IGP----NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeaPQD 68
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 87-196 2.58e-03

Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 37.22  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  87 NARIEPGAIIRD----QVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILggraivgKNShvgagavlagviepasaepv 162
Cdd:cd00710   48 NVNIQDGVVIHAlegySVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVV-------FNA-------------------- 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488994759 163 RVGDNVLIGANAVVIeGVQIGSGSVVAAGAIVTQ 196
Cdd:cd00710  101 KVGDNCVIGHNAVVD-GVEIPPGRYVPAGAVITS 133
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 86-176 2.59e-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: 36.29  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  86 INARIEPGAIIRDqveigdnaVIMMGAVinigaEIGAGTMIDmgailggRAIVGKNSHVGAGAVLAGVIEPASAEPVRVG 165
Cdd:cd04651   33 RGVRVGSGSVVED--------SVIMPNV-----GIGRNAVIR-------RAIIDKNVVIPDGVVIGGDPEEDRARFYVTE 92

                         90
                 ....*....|..
gi 488994759 166 DN-VLIGANAVV 176
Cdd:cd04651   93 DGiVVVGKGMVI 104
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-193 3.84e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  69 VEQDARNSAVPLLDKRD---INARI---EPGAIIRDQVeigdNAVIMMGAVINIGAEigaGTMIDMGAIlggraiVGKNS 142
Cdd:PRK14355 209 AAEGLRCLAFPVADPDEimgVNDRAqlaEAARVLRRRI----NRELMLAGVTLIDPE---TTYIDRGVV------IGRDT 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488994759 143 HVGAGAVLAGviepasaePVRVGDNVLIGANaVVIEGVQIGSGSVVAAGAI 193
Cdd:PRK14355 276 TIYPGVCISG--------DTRIGEGCTIEQG-VVIKGCRIGDDVTVKAGSV 317
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 136-194 4.25e-03

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: 37.69  E-value: 4.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488994759 136 AIVGKNSHVGAGavlagviepasaepVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIV 194
Cdd:COG1044  103 AVIDPSAKIGEG--------------VSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVI 147
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 120-198 5.85e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.91  E-value: 5.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488994759 120 IGAGTMIDMGAILGgRAIVGKNSHVGAGAVlagVIEPASAEPVRVGDNVLIgANAVVIEGVQIGSGSVVAAGAIVTQDV 198
Cdd:cd03356    2 IGESTVIGENAIIK-NSVIGDNVRIGDGVT---ITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDV 75
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 113-198 6.81e-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: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 113 VINIGAEIGAGTMIdMGAILGGRAIVGKNSHVGAGAVLAGVIepasaepvrVGDNVLIGaNAVVIEGVQIGSGSVVAAGA 192
Cdd:cd05787    1 VIGRGTSIGEGTTI-KNSVIGRNCKIGKNVVIDNSYIWDDVT---------IEDGCTIH-HSIVADGAVIGKGCTIPPGS 69


                 ....*.
gi 488994759 193 IVTQDV 198
Cdd:cd05787   70 LISFGV 75
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 65-213 7.86e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  65 KTYVVEQDA--RNSAV-PLldkrdinARIEPGAIIRDqVEIGdNAVIMMGAVIN---------IG-AEIGAGTMIDMGAI 131
Cdd:PRK14359 286 KAHSVIEESiiENSDVgPL-------AHIRPKSEIKN-THIG-NFVETKNAKLNgvkaghlsyLGdCEIDEGTNIGAGTI 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759 132 LGGRAivGKNSHvgagavlagviepasaePVRVGDNVLIGANAVVIEGVQIGSGSVVAAGAIVTQDVPE-NVVVAGVPAR 210
Cdd:PRK14359 357 TCNYD--GKKKH-----------------KTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKgSLAISRAPQK 417


                 ...
gi 488994759 211 VIK 213
Cdd:PRK14359 418 NIK 420
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-174 8.82e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994759  90 IEPGAI-IRDQVEIGDNAVIMMGAVINIGAEIGAGTMIDMGAILGGrAIVGKNSHVGAGAVLagviepasaEPVRVGDNV 168
Cdd:PRK14355 258 IDPETTyIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAGSVL---------EDSVVGDDV 327


                 ....*.
gi 488994759 169 LIGANA 174
Cdd:PRK14355 328 AIGPMA 333
 
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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