NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1221676970|ref|WP_089805232|]
View 

acetyltransferase [Chitinophaga sp. YR627]

Protein Classification

acetyltransferase( domain architecture ID 10129737)

acetyltransferase similar to Escherichia coli GDP-perosamine N-acetyltransferase that catalyzes the transfer of an acetyl residue from acetyl-CoA onto GDP-perosamine to form GDP-N-acetyl-perosamine; belongs to the transferase hexapeptide repeat family

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-181 2.27e-48

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: 155.72  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970   6 IYGKGGHA-LTIEALARKSDYEIVAFFDDNADVNDRYRGREVLRYETALMREYP----LFIAIGNNVVRKKIV-SFVAHK 79
Cdd:cd03360     1 IIGAGGHArVVADILEADSGYEVVGFLDDDPELKGTEGLGLPVGLDELLLLYPPpddeFVVAIGDNKLRRKLAeKLLAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  80 YC--TFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIG 157
Cdd:cd03360    81 YRfaTLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIG 160

                         170       180
                  ....*....|....*....|....
gi 1221676970 158 AGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVT 184
 
Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-181 2.27e-48

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: 155.72  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970   6 IYGKGGHA-LTIEALARKSDYEIVAFFDDNADVNDRYRGREVLRYETALMREYP----LFIAIGNNVVRKKIV-SFVAHK 79
Cdd:cd03360     1 IIGAGGHArVVADILEADSGYEVVGFLDDDPELKGTEGLGLPVGLDELLLLYPPpddeFVVAIGDNKLRRKLAeKLLAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  80 YC--TFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIG 157
Cdd:cd03360    81 YRfaTLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIG 160

                         170       180
                  ....*....|....*....|....
gi 1221676970 158 AGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVT 184
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-174 1.01e-47

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: 154.19  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970   5 LIYGKGGHALTIEALARKSDYEIVAFFDDN-ADVNDRYRGREVLRYETALMR----EYPLFIAIGNNVVRKKIVSFVAHK 79
Cdd:TIGR03570   3 VIIGAGGHGRVVADILERSGWEVVGFLDDNpALQGTEVDGLPVLGGDEDLLRyppdEVDLVVAIGDNKLRRRLVEKLKAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  80 YCTF---IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATI 156
Cdd:TIGR03570  83 GYRFatlIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFI 162

                         170
                  ....*....|....*...
gi 1221676970 157 GAGSVIMRNAKIADWTNI 174
Cdd:TIGR03570 163 GAGATIIQGVTIGAGAIV 180
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 84-162 2.00e-13

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 66.96  E-value: 2.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 77-162 3.13e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 63.62  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  77 AHKYCTFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATI 156
Cdd:PRK00892   96 TPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175


                  ....*.
gi 1221676970 157 GAGSVI 162
Cdd:PRK00892  176 HSGAVI 181
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 5-73 2.35e-11

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 56.80  E-value: 2.35e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221676970   5 LIYGKGGHALTIEALARKS-DYEIVAFFDDNADVND---RYRGREVLRYETALMREYPLFIAIGNNVVRKKIV 73
Cdd:pfam17836   3 IIIGAGGHGKVVADIIEAMgEYEIIGFLDDNKKTEVngyPVLGGDIDLLASLSPDEYDVVIAIGNNKVRKKIA 75
 
Name Accession Description Interval E-value
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-181 2.27e-48

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: 155.72  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970   6 IYGKGGHA-LTIEALARKSDYEIVAFFDDNADVNDRYRGREVLRYETALMREYP----LFIAIGNNVVRKKIV-SFVAHK 79
Cdd:cd03360     1 IIGAGGHArVVADILEADSGYEVVGFLDDDPELKGTEGLGLPVGLDELLLLYPPpddeFVVAIGDNKLRRKLAeKLLAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  80 YC--TFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIG 157
Cdd:cd03360    81 YRfaTLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIG 160

                         170       180
                  ....*....|....*....|....
gi 1221676970 158 AGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVT 184
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-174 1.01e-47

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: 154.19  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970   5 LIYGKGGHALTIEALARKSDYEIVAFFDDN-ADVNDRYRGREVLRYETALMR----EYPLFIAIGNNVVRKKIVSFVAHK 79
Cdd:TIGR03570   3 VIIGAGGHGRVVADILERSGWEVVGFLDDNpALQGTEVDGLPVLGGDEDLLRyppdEVDLVVAIGDNKLRRRLVEKLKAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  80 YCTF---IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATI 156
Cdd:TIGR03570  83 GYRFatlIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFI 162

                         170
                  ....*....|....*...
gi 1221676970 157 GAGSVIMRNAKIADWTNI 174
Cdd:TIGR03570 163 GAGATIIQGVTIGAGAIV 180
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 84-162 2.00e-13

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 66.96  E-value: 2.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 77-162 3.13e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 63.62  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  77 AHKYCTFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATI 156
Cdd:PRK00892   96 TPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175


                  ....*.
gi 1221676970 157 GAGSVI 162
Cdd:PRK00892  176 HSGAVI 181
PglD_N pfam17836
PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as ...
 5-73 2.35e-11

PglD N-terminal domain; This alpha/beta domain is found at the N-terminus of proteins such as PglD. This domain binds a UDP-sugar substrate.


Pssm-ID: 436081  Cd Length: 78  Bit Score: 56.80  E-value: 2.35e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221676970   5 LIYGKGGHALTIEALARKS-DYEIVAFFDDNADVND---RYRGREVLRYETALMREYPLFIAIGNNVVRKKIV 73
Cdd:pfam17836   3 IIIGAGGHGKVVADIIEAMgEYEIIGFLDDNKKTEVngyPVLGGDIDLLASLSPDEYDVVIAIGNNKVRKKIA 75
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
79-172 1.61e-10

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 56.42  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  79 KYCTFIDNTAFITQDVRIGEGTVVMPGAIVQAGAD--IGRHVILNIGC---AVDHE-------------VSIGDFAHIGP 140
Cdd:COG0110    13 DGVVIGPGVRIYGGNITIGDNVYIGPGVTIDDPGGitIGDNVLIGPGVtilTGNHPiddpatfplrtgpVTIGDDVWIGA 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1221676970 141 KCYIGGGAVIGEGATIGAGSVIMRNakIADWT 172
Cdd:COG0110    93 GATILPGVTIGDGAVVGAGSVVTKD--VPPYA 122
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-174 3.16e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 57.84  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIG-------------------GGA 148
Cdd:PRK00892  125 AVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGsdgfgfandrggwvkipqlGRV 204

                          90       100       110
                  ....*....|....*....|....*....|
gi 1221676970 149 VIGEGATIGAGSVI----MRNAKIADWTNI 174
Cdd:PRK00892  205 IIGDDVEIGANTTIdrgaLDDTVIGEGVKI 234
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 83-181 4.37e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.80  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQDVRIGEGTVVMPGAIVQAGAD---IGRHVilNI--GCAV----DHEVSIGDFAHIGPK-----CYIGGGA 148
Cdd:COG0663    18 FVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGpirIGEGS--NIqdGVVLhvdpGYPLTIGDDVTIGHGailhgCTIGDNV 95

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1221676970 149 VIG------EGATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:COG0663    96 LIGmgaivlDGAVIGDGSIVGAGALVTEGKVVPPGSLVV 134
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 93-162 5.24e-10

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: 55.88  E-value: 5.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-170 7.71e-10

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 56.56  E-value: 7.71e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIAD 170
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGD 149
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 82-180 1.07e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 56.38  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFID-NTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVIL---------NIG--CAVDHEV----SIGDFAHIGPKCYIG 145
Cdd:PRK14354  253 TIIDpESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIgpgsrivdsTIGdgVTITNSVieesKVGDNVTVGPFAHLR 332

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1221676970 146 GGAVIGEGATIGaGSVIMRNAKIADWTNIPPLSVI 180
Cdd:PRK14354  333 PGSVIGEEVKIG-NFVEIKKSTIGEGTKVSHLTYI 366
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 91-180 3.01e-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: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  91 TQDVRIGEGTVVMPGAIVQ---AGADIGRHVILNIGCAV-------DHEVS-----IGDFAHIGPKC-----YIGGGAVI 150
Cdd:cd03359    19 SQNIVLNGKTIIQSDVIIRgdlATVSIGRYCILSEGCVIrppfkkfSKGVAffplhIGDYVFIGENCvvnaaQIGSYVHI 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 1221676970 151 GEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:cd03359    99 GKNCVIGRRCIIKDCVKILDGTVVPPDTVI 128
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 82-181 3.73e-09

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 52.80  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPGAIVQAGAD---IGRHVilNIG------CAVDHEVSIGDFAHIGPKCYIGGgAVIGE 152
Cdd:cd04645     6 AFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNpirIGERT--NIQdgsvlhVDPGYPTIIGDNVTVGHGAVLHG-CTIGD 82

                          90       100
                  ....*....|....*....|....*....
gi 1221676970 153 GATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd04645    83 NCLIGMGAIILDGAVIGKGSIVAAGSLVP 111
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 126-180 6.52e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 6.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 82-178 7.60e-09

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: 53.88  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFID-NTAFITQDVRIGEGTVVMPGAI------VQAGADIGRHVILN---IG--CAVDH----EVSIGDFAHIGPKCYIG 145
Cdd:COG1207   254 TIIDpATTYIDGDVEIGRDVVIDPNVIlegktvIGEGVVIGPNCTLKdstIGdgVVIKYsvieDAVVGAGATVGPFARLR 333

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1221676970 146 GGAVIGEGATIGAgSVIMRNAKIADWTNIPPLS 178
Cdd:COG1207   334 PGTVLGEGVKIGN-FVEVKNSTIGEGSKVNHLS 365
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 83-164 9.79e-09

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: 52.41  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIG----------------- 145
Cdd:cd03352     9 SIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGsdgfgfapdgggwvkip 88

                          90       100
                  ....*....|....*....|.
gi 1221676970 146 --GGAVIGEGATIGAGSVIMR 164
Cdd:cd03352    89 qlGGVIIGDDVEIGANTTIDR 109
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-151 1.14e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 53.10  E-value: 1.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGcavdheVSIGDFAHIGPKCYIGGGAVIG 151
Cdd:COG1044   121 AVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPN------VTIYERCVIGDRVIIHSGAVIG 178
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 84-168 1.66e-08

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 52.98  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRhvilniGCavdhevsigdfaHIGPKCYIGGGAVIGEGATIGAG---- 159
Cdd:TIGR03992 239 VEENVTIKGPVVIGEGAVIRSGTYIEGPVYIGK------NC------------DIGPNAYIRPYTVIGNNVHIGNAveik 300

                          90
                  ....*....|
gi 1221676970 160 -SVIMRNAKI 168
Cdd:TIGR03992 301 nSIIMEGTKI 310
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 82-160 2.61e-08

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: 51.27  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPG-----AIVQAGADIGRHVILNiGCAVDHEVSIGDFAHIGPKCYIGGGAVIG----- 151
Cdd:cd03353    22 VVIDPGVILEGKTVIGEDCVIGPNcvikdSTIGDGVVIKASSVIE-GAVIGNGATVGPFAHLRPGTVLGEGVHIGnfvei 100


                  ....*....
gi 1221676970 152 EGATIGAGS 160
Cdd:cd03353   101 KKSTIGEGS 109
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 82-180 5.49e-08

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: 49.93  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPGAIVQA----GADIGRHVILNIGcAVDH-----EVSIGDFAHIGPKCYIGGGAVIGE 152
Cdd:cd00710     9 AYVHPTAVVIGDVIIGDNVFVGPGASIRAdegtPIIIGANVNIQDG-VVIHalegySVWIGKNVSIAHGAIVHGPAYIGD 87

                          90       100
                  ....*....|....*....|....*...
gi 1221676970 153 GATIGAGSVIMrNAKIADWTNIPPLSVI 180
Cdd:cd00710    88 NCFIGFRSVVF-NAKVGDNCVIGHNAVV 114
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 123-174 2.93e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.56  E-value: 2.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1221676970 123 GCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNI 174
Cdd:cd03352     7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII 58
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 82-176 3.33e-07

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: 48.19  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFID-NTAFITQDVRIGEGTVVMPGAIVQAGadigrhvilnigcavdheVSIGDFAHIGPKCYIGGGaVIGEGATIGAGS 160
Cdd:cd03353     3 TLIDpETTYIDGDVEIGVDVVIDPGVILEGK------------------TVIGEDCVIGPNCVIKDS-TIGDGVVIKASS 63

                          90
                  ....*....|....*.
gi 1221676970 161 VImRNAKIADWTNIPP 176
Cdd:cd03353    64 VI-EGAVIGNGATVGP 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 96-181 5.89e-07

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 46.34  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  96 IGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKC------YIGG---------GAVIGEGATIGAGS 160
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVvftndlYPRSkiyrkwelkGTTVKRGASIGANA 80

                          90       100
                  ....*....|....*....|.
gi 1221676970 161 VIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVT 101
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 98-180 7.39e-07

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 47.88  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  98 EGTVVMPGAIVQAGADIGRHVIL-----NIGCAVDHE------------------------VSIG--------------D 134
Cdd:PRK11830  102 AGVRVVPGAVVRRGAYIAPNVVLmpsyvNIGAYVDEGtmvdtwatvgscaqigknvhlsggVGIGgvleplqanpviieD 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1221676970 135 FAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTN-------IPPLSVI 180
Cdd:PRK11830  182 NCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETgevhygrVPAGSVV 234
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 114-165 7.47e-07

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 45.67  E-value: 7.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1221676970 114 IGRHVILNIG---CAVDH------------EVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRN 165
Cdd:cd05825    26 IGSDACISQGaylCTGSHdyrspafplitaPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRD 92
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 83-172 9.22e-07

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: 47.82  E-value: 9.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQD-VRIGEGTVVMPGAIVQAgadigrHVILNIGCAVDHeVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSV 161
Cdd:TIGR02353 605 YIDGTDLTERDlVTIGDDSTLNEGSVIQT------HLFEDRVMKSDT-VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677

                          90
                  ....*....|.
gi 1221676970 162 IMRNAKIADWT 172
Cdd:TIGR02353 678 VMKGEEVPAHT 688
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 88-181 1.06e-06

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: 45.83  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRhvilniGCAVDHEVSIGDFAHIGPKCYIGGGAVIG---------------- 151
Cdd:cd03350     8 AIIRDGAFIGPGAVLMMPSYVNIGAYVDE------GTMVDSWATVGSCAQIGKNVHLSAGAVIGgvleplqatpviiedd 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1221676970 152 ----------------EGATIGAGSVIMRNAKIADWTN-------IPPLSVIT 181
Cdd:cd03350    82 vfigancevvegvivgKGAVLAAGVVLTQSTPIYDRETgeiyygrVPPGSVVV 134
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 130-180 1.14e-06

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: 46.63  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1221676970 130 VSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 90-180 1.27e-06

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: 46.16  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  90 ITQDVRIGEGTVVMPGAIVQAGAD-------------------------------IGRHVILNIGCAVDhEVSIGDFAHI 138
Cdd:cd04646    14 IRGDVTIGPGTVVHPRATIIAEAGpiiigenniieeqvtivnkkpkdpaepkpmiIGSNNVFEVGCKCE-ALKIGNNNVF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1221676970 139 GPKCYIGGGAVIGEGATIGAGSVIMRNakiadwTNIPPLSVI 180
Cdd:cd04646    93 ESKSFVGKNVIITDGCIIGAGCKLPSS------EILPENTVI 128
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 82-178 1.34e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 47.24  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFID-NTAFITQDVRIGEGTVVMPGA------IVQAGADIG-----RHVILNIGCAVDH----EVSIGDFAHIGPKCYIG 145
Cdd:PRK14352  259 TIVDpATTWIDVDVTIGRDVVIHPGTqllgrtTIGEDAVVGpdttlTDVTVGEGASVVRthgsESEIGAGATVGPFTYLR 338

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1221676970 146 GGAVIGEGATIGAgSVIMRNAKIADWTNIPPLS 178
Cdd:PRK14352  339 PGTVLGEEGKLGA-FVETKNATIGRGTKVPHLT 370
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 56-180 1.46e-06

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: 45.88  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  56 EYPLFIAIGNNVvrkkivsFVAHKyCTFIDNTAfitqdVRIGEGTVVMPGaiVQagadigrhvILNIGCAVDHEVSIGD- 134
Cdd:cd03357    58 DYGYNIHIGDNF-------YANFN-CTILDVAP-----VTIGDNVLIGPN--VQ---------IYTAGHPLDPEERNRGl 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1221676970 135 -FA---HIGPKCYIGGGAV------IGEGATIGAGSVIMRnakiadwtNIPPLSVI 180
Cdd:cd03357   114 eYAkpiTIGDNVWIGGGVIilpgvtIGDNSVIGAGSVVTK--------DIPANVVA 161
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 93-169 1.75e-06

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 45.66  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVMPGAIVQAGADIGRHVIlnigcavdhevsIGDFAHIGPKCYIGGGAVIGEGATIGAG-----SVIMRNAK 167
Cdd:cd05636    11 GVTIKGPVWIGEGAIVRSGAYIEGPVI------------IGKGCEIGPNAYIRGYTVLGDGCVVGNSvevknSIIMDGTK 78


                  ..
gi 1221676970 168 IA 169
Cdd:cd05636    79 VP 80
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 83-181 2.20e-06

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: 45.44  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQDVRIGEGTVVMPGA---------IVQAGADI----------GRHVILNIGCAVDHEvSIGDFAHIGPKCY 143
Cdd:cd04745     8 FVHPTAVLIGDVIIGKNCYIGPHAslrgdfgriVIRDGANVqdncvihgfpGQDTVLEENGHIGHG-AILHGCTIGRNAL 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1221676970 144 IGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd04745    87 VGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIA 124
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 83-181 2.31e-06

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: 45.25  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQDVRIGEGTVVMPGAIVQAGAD---IGRHVILNIGCAVD----HEVSIGDFAHIGPKCYIgGGAVIGEGAT 155
Cdd:cd04650     8 YVHPTSYVIGDVVIGELTSVWHYAVIRGDNDsiyIGKYSNVQENVSIHtdhgYPTEIGDYVTIGHNAVV-HGAKVGNYVI 86

                          90       100
                  ....*....|....*....|....*.
gi 1221676970 156 IGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd04650    87 VGMGAILLNGAKIGDHVIIGAGAVVT 112
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 99-157 3.65e-06

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: 44.29  E-value: 3.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970  99 GTVVMPGAIVQAGADIGRHVIL------NIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIG 157
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLmmpsyvNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIG 65
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 93-172 3.94e-06

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 43.60  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVMPGAIVQAGA--DIGRHVILNIGC---AVDH----------------EVSIGDFAHIGPKCYIGGGAVIG 151
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVtiyDHNHdiddperpieqgvtsaPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|.
gi 1221676970 152 EGATIGAGSVIMRNakIADWT 172
Cdd:cd04647    81 DGAVVGAGSVVTKD--VPPNS 99
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 126-180 4.17e-06

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 45.50  E-value: 4.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:cd03351     8 VDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 104-162 6.10e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 6.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970 104 PGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:PRK12461    4 PTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 126-180 6.43e-06

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: 45.01  E-value: 6.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:COG1043    10 VDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 96-179 8.01e-06

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: 44.72  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  96 IGEGTVVMPG-----------------AIVQAGADIGRHVILNIGCAV--------DHEVSIGDFAHIGPKCYIGGGAVI 150
Cdd:COG2171   112 LAPGVVLMPSfvnigayvdegtmvdtwATVGSCAQIGKNVHLSGGAGIggvleplqAAPVIIEDNCFIGARSGVVEGVIV 191

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1221676970 151 GEGATIGAGSVIMRNAKIADWTN-------IPPLSV 179
Cdd:COG2171   192 GEGAVLGAGVYLTASTKIYDRVTgevyygrVPAGSV 227
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 90-170 8.76e-06

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: 42.18  E-value: 8.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  90 ITQDVRIGEGTVVMpGAIVQAGADIGRHVILNiGCAVDHEVSIGDFAHIGpKCYIGGGAVIGEGATIGAGSVIMRNAKIA 169
Cdd:cd05787     2 IGRGTSIGEGTTIK-NSVIGRNCKIGKNVVID-NSYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGVVIG 78


                  .
gi 1221676970 170 D 170
Cdd:cd05787    79 D 79
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
126-180 1.29e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.93  E-value: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:PRK05289   11 VEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 126-180 1.37e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 1.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVImRNAKIADWTNIPPLSVI 180
Cdd:PRK14355  265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVL 318
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 94-163 1.37e-05

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: 41.47  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1221676970  94 VRIGEGTVVMPGAIVQAGADIGRHVILNIGCAV--------DHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIM 163
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIgaatgpneKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 124-180 1.40e-05

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.56  E-value: 1.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1221676970 124 CAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVImRNAKIADWTNIPPLSVI 180
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVI 65
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 82-178 1.43e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFID-NTAFITQDVRIGEGTVVMPGAIVQAGADIGRhvilniGCAVDHEVSIgdfahigpkcyigGGAVIGEGATIGAGS 160
Cdd:PRK14355  256 TLIDpETTYIDRGVVIGRDTTIYPGVCISGDTRIGE------GCTIEQGVVI-------------KGCRIGDDVTVKAGS 316

                          90
                  ....*....|....*...
gi 1221676970 161 ViMRNAKIADWTNIPPLS 178
Cdd:PRK14355  317 V-LEDSVVGDDVAIGPMA 333
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 82-161 1.73e-05

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.86  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPG-----AIVQAGADIGRHVIlnIGCAVDHEVSIGDFAH------IGPKCYIG----- 145
Cdd:COG1207   273 VVIDPNVILEGKTVIGEGVVIGPNctlkdSTIGDGVVIKYSVI--EDAVVGAGATVGPFARlrpgtvLGEGVKIGnfvev 350

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1221676970 146 -----------------GGAVIGEGATIGAGSV 161
Cdd:COG1207   351 knstigegskvnhlsyiGDAEIGEGVNIGAGTI 383
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 112-166 1.79e-05

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.86  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221676970 112 ADIGRHVilNIGCAV-----D----HEVSIGDFAHIG-------PkcyigggAVIGEGATIGAGSVIMRNA 166
Cdd:COG1207   370 AEIGEGV--NIGAGTitcnyDgvnkHRTVIGDGAFIGsntnlvaP-------VTIGDGATIGAGSTITKDV 431
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 56-176 2.28e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 43.07  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  56 EYPLFIAIGNNVVRKKivSFVAHKYCTFIDNTAfitqdVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDF 135
Cdd:PRK09527   65 EPPVYFSYGSNIHIGR--NFYANFNLTIVDDYT-----VTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNN 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1221676970 136 AHIGPKCYIGGGAVIGEGATIGAGSVIMRnakiadwtNIPP 176
Cdd:PRK09527  138 VWIGSHVVINPGVTIGDNSVIGAGSVVTK--------DIPP 170
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 84-152 2.69e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.09  E-value: 2.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRhvilniGCAVDHEVSIGDFAHIGPKCYIGGGAVIGE 152
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGD------GTWIGPHAVILGPTRIGKNNKIHQGAVVGD 64
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 104-162 3.87e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.80  E-value: 3.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221676970 104 PGAIVQAGADIGRHVIlnIG--CAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:cd03351     4 PTAIVDPGAKIGENVE--IGpfCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 84-162 5.11e-05

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.42  E-value: 5.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVsIGDFAHIGPKCYIgGGAVIGEGATIGAGSVI 162
Cdd:cd05636    26 VRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI-IMDGTKVPHLNYV-GDSVLGENVNLGAGTIT 102
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 135-170 5.97e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 41.62  E-value: 5.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1221676970 135 FAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIAD 170
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGD 36
PRK10502 PRK10502
putative acyl transferase; Provisional
 52-165 6.02e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.47  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  52 ALMReypLFIA-IGNNVVRKKIVSFvahKYCTFIDntafITQDVRIGEGTVVMPGAIVQagadIGRHVILNIG---CAVD 127
Cdd:PRK10502   45 FLLR---LFGAkIGKGVVIRPSVRI---TYPWKLT----IGDYAWIGDDVWLYNLGEIT----IGAHCVISQKsylCTGS 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1221676970 128 HE------------VSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRN 165
Cdd:PRK10502  111 HDysdphfdlntapIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS 160
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 84-165 6.75e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVIlnigcavdhevsigdfahIGPKCYIGGGAVIGEGATIGAGSVIM 163
Cdd:PRK00892  234 IDNLVQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCM------------------IGGQVGIAGHLEIGDGVTITAMSGVT 295


                  ..
gi 1221676970 164 RN 165
Cdd:PRK00892  296 KS 297
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-180 7.07e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.22  E-value: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  73 VSFVAHKYCTfIDNTAFITQDV------------RIGEGTVVMPGAIVQaGADIGRHV-ILN---IGCAVDHEVSIGDFA 136
Cdd:PRK14360  249 VTFIDPASCT-ISETVELGPDViiepqthlrgntVIGSGCRIGPGSLIE-NSQIGENVtVLYsvvSDSQIGDGVKIGPYA 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1221676970 137 HIGPKCYIGGGAVIGEgatigagSVIMRNAKIADWTNIPPLSVI 180
Cdd:PRK14360  327 HLRPEAQIGSNCRIGN-------FVEIKKSQLGEGSKVNHLSYI 363
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
82-152 7.32e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 7.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPGAIvqagadIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGE 152
Cdd:PRK05289    3 AKIHPTAIVEPGAKIGENVEIGPFCV------IGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGE 67
PLN02694 PLN02694
serine O-acetyltransferase
 99-163 9.71e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 41.55  E-value: 9.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1221676970  99 GTVVMPGAIVQAGADIGRHVILN-IGCAV-DHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIM 163
Cdd:PLN02694  180 GVVIGETAVIGNNVSILHHVTLGgTGKACgDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVL 246
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-167 1.10e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 41.63  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221676970 106 AIVQAGADIGRHVILnigCAVD----HEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAK 167
Cdd:PRK14356  374 AEIGAGANIGAGTIT---CNYDgvnkHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVP 436
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 138-180 1.11e-04

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: 41.54  E-value: 1.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1221676970 138 IGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 61-165 1.38e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.55  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  61 IAIGNNVvrkKIVSFVAHKYCTFIDNTAF----ITQDVRIGEGTVV------MPGAIVQAGADIGRHV-----ILNIGCA 125
Cdd:PRK09451  284 VTLGNRV---KIGAGCVLKNCVIGDDCEIspysVVEDANLGAACTIgpfarlRPGAELAEGAHVGNFVemkkaRLGKGSK 360

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221676970 126 VDHEVSIGDfAHIGPKCYIGGGAV-------------------------------IGEGATIGAGSVIMRN 165
Cdd:PRK09451  361 AGHLTYLGD-AEIGDNVNIGAGTItcnydgankfktiigddvfvgsdtqlvapvtVGKGATIGAGTTVTRD 430
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 126-180 1.68e-04

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: 40.71  E-value: 1.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970 126 VDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:TIGR01852   7 IEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVI 61
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 94-165 1.90e-04

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 38.96  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  94 VRIGEGTVVM--PGAIVQAGADIGRHVILNIGCAV--DHEVSIGDFAHIGPKCYIGGGAV------IGEGATIGAGSVIM 163
Cdd:cd03354     9 AKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLggKGKGGGKRHPTIGDNVVIGAGAKilgnitIGDNVKIGANAVVT 88


                  ..
gi 1221676970 164 RN 165
Cdd:cd03354    89 KD 90
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 88-161 2.71e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.00  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRHVIlnigcavdhevsIGDFAHIG------------PKCYIGGGAVIGEGAT 155
Cdd:COG1043    26 CVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNR------------IFPFASIGeepqdlkykgepTRLEIGDNNTIREFVT 93


                  ....*.
gi 1221676970 156 IGAGSV 161
Cdd:COG1043    94 IHRGTV 99
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-165 3.05e-04

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: 40.00  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRHVILN------------------------------------IGC--AVD-- 127
Cdd:COG1044   139 VVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHsgavigadgfgfapdedggwvkipqlgrvvigddveIGAntTIDrg 218

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221676970 128 --------------------HEVSIGDF------------AHIGPKCYIGGGAV------IGEGATIGAGSVIMRN 165
Cdd:COG1044   219 algdtvigdgtkidnlvqiaHNVRIGEHtaiaaqvgiagsTKIGDNVVIGGQVGiaghltIGDGVIIGAQSGVTKS 294
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-181 3.10e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.48  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  94 VRIGEGTVV------MPGAIVQAGADIGRHV-----ILNIGCAVDHEVSIGDfAHIGPKCYIGGGA-------------V 149
Cdd:PRK14356  322 AEVGDGCSVgpyarlRPGAVLEEGARVGNFVemkkaVLGKGAKANHLTYLGD-AEIGAGANIGAGTitcnydgvnkhrtV 400

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1221676970 150 IGEGATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVIT 432
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 84-167 3.98e-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: 39.31  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  84 IDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVIlnigcavdhevsigdfahIGPKCYIGGGAVIGEGATIGAGSVIM 163
Cdd:cd03352   123 IDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVI------------------IGGQVGIAGHLTIGDGVVIGAGSGVT 184


                  ....
gi 1221676970 164 RNAK 167
Cdd:cd03352   185 SIVP 188
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 83-170 4.06e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 39.41  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  83 FIDNTAFITQDVRIGEGTVVMPGA---------IVQAGADIGRHVILNIGCAVDheVSIGDFAHIGPKCyIGGGAVIGEG 153
Cdd:PRK13627   18 FVHPSAVLIGDVIVGAGVYIGPLAslrgdygrlIVQAGANLQDGCIMHGYCDTD--TIVGENGHIGHGA-ILHGCVIGRD 94

                          90
                  ....*....|....*..
gi 1221676970 154 ATIGAGSVIMRNAKIAD 170
Cdd:PRK13627   95 ALVGMNSVIMDGAVIGE 111
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 88-160 4.97e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.24  E-value: 4.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSigDFAHIGPKCY--IGGGAVIGEGATIGAGS 160
Cdd:PRK12461   24 AVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQ--DFTYKGEESRleIGDRNVIREGVTIHRGT 96
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 114-181 7.38e-04

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: 36.84  E-value: 7.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221676970 114 IGRHVILNIGCAVDHEVsIGDFAHIGPK-----CYIGGGAVIGEGATIgAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03356     2 IGESTVIGENAIIKNSV-IGDNVRIGDGvtitnSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIG 72
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
130-158 7.44e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 7.44e-04
                          10        20
                  ....*....|....*....|....*....
gi 1221676970 130 VSIGDFAHIGPKCYIGGGAVIGEGATIGA 158
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
93-175 7.69e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.93  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVMPGAIVQ-AGADIGRHVILNIGCAVD--HEVSIGDFAHIGPkcyigggavigeGATIGAGSVIMRNAKIA 169
Cdd:COG0110     8 GARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDdpGGITIGDNVLIGP------------GVTILTGNHPIDDPATF 75


                  ....*.
gi 1221676970 170 DWTNIP 175
Cdd:COG0110    76 PLRTGP 81
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 96-181 8.86e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.07  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  96 IGEGTVV------MPGAIVQAGADIGRHV-----ILNIGCAVDHEVSIGDfAHIGPKCYIGGGA-------------VIG 151
Cdd:PRK14353  306 VGEGAEVgpyarlRPGAELGEGAKVGNFVevknaKLGEGAKVNHLTYIGD-ATIGAGANIGAGTitcnydgfnkhrtEIG 384

                          90       100       110
                  ....*....|....*....|....*....|
gi 1221676970 152 EGATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:PRK14353  385 AGAFIGSNSALVAPVTIGDGAYIASGSVIT 414
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-161 1.29e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 38.38  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVM----PGAIVQAGADIGRHVILNIGCAVDHEVSIGDF-----AHIG-----PKCYIGGGAVIGEGATIGA 158
Cdd:PRK14352  306 DVTVGEGASVVrthgSESEIGAGATVGPFTYLRPGTVLGEEGKLGAFvetknATIGrgtkvPHLTYVGDADIGEHSNIGA 385


                  ...
gi 1221676970 159 GSV 161
Cdd:PRK14352  386 SSV 388
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 88-161 1.51e-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: 37.80  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGRhvilniGCAVDHEVSIG----DFAHIG--PKCYIGGGAVIGEGATIGAGSV 161
Cdd:cd03351    24 CVIGPNVEIGDGTVIGSHVVIDGPTTIGK------NNRIFPFASIGeapqDLKYKGepTRLEIGDNNTIREFVTIHRGTA 97
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 135-180 1.55e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1221676970 135 FAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVI 180
Cdd:PRK00892  100 AAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI 145
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 63-134 1.59e-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: 36.02  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1221676970  63 IGNNVVrkkivsfvahkyctfIDNtAFITQDVRIGEGTVVMpGAIVQAGADIGRHVILNIGCAVDHEVSIGD 134
Cdd:cd05787    25 IGKNVV---------------IDN-SYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-162 2.45e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.61  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFI-TQDVRIGEGTVVmPGAIVQAGADIGRHVilNIGCAV---------DHEVSIGDFAHIGPKCYIGGGAVIGEGATIG 157
Cdd:PRK14352  351 AFVeTKNATIGRGTKV-PHLTYVGDADIGEHS--NIGASSvfvnydgvnKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTG 427


                  ....*
gi 1221676970 158 AGSVI 162
Cdd:PRK14352  428 AGTVI 432
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 90-162 2.82e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.65  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  90 ITQDVRIGEGTVVMP-----GAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHI-----------GPKCYIgGGAVIGEG 153
Cdd:PRK14358  302 VVTDSVLHEGAVIKPhsvleGAEVGAGSDVGPFARLRPGTVLGEGVHIGNFVETknarldagvkaGHLAYL-GDVTIGAE 380


                  ....*....
gi 1221676970 154 ATIGAGSVI 162
Cdd:PRK14358  381 TNVGAGTIV 389
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 90-174 2.85e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.54  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  90 ITQDVRIGEGT-----VVMPGAIvqagadIGRHVILNigcavdhevsigdfahigpKCYIGGGAVIGEGATIGAG----S 160
Cdd:PRK05293  311 LFQGVQVGEGSvvkdsVIMPGAK------IGENVVIE-------------------RAIIGENAVIGDGVIIGGGkeviT 365

                          90
                  ....*....|....
gi 1221676970 161 VIMRNAKIADWTNI 174
Cdd:PRK05293  366 VIGENEVIGVGTVI 379
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-161 3.35e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 37.40  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  93 DVRIGEGTVVMP-----GAIVQAGADIGRHVILNIGCAVDHEVSIGDF-----AHIGPKCYIG-----GGAVIGEGATIG 157
Cdd:PRK14356  304 DAVVSSGATIHSfshleGAEVGDGCSVGPYARLRPGAVLEEGARVGNFvemkkAVLGKGAKANhltylGDAEIGAGANIG 383


                  ....
gi 1221676970 158 AGSV 161
Cdd:PRK14356  384 AGTI 387
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 82-181 3.44e-03

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: 36.62  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  82 TFIDNTAFITQDVRIGEGTVVMPGAIVQAGADIGRHVILNIGC---------AVDHE----------VSIGDFA------ 136
Cdd:cd03352    26 VVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAvigsdgfgfAPDGGgwvkipqlggVIIGDDVeigant 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970 137 ----------------------HIGPKCYIG------------GGAVIGEGATIGAGSVIMRNAKIADWTNIPPLSVIT 181
Cdd:cd03352   106 tidrgalgdtvigdgtkidnlvQIAHNVRIGencliaaqvgiaGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVT 184
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 71-165 4.98e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 36.66  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  71 KIVSFVAHKYCTFIDNT----------AFITQDVRIGEGTvvmpgaivqagadigrhvilnIGCAVD----HEVSIGDFA 136
Cdd:PRK14357  332 KIGNFVEIKKSTIGENTkaqhltylgdATVGKNVNIGAGT---------------------ITCNYDgkkkNPTFIEDGA 390

                          90       100
                  ....*....|....*....|....*....
gi 1221676970 137 HIGPKCYIGGGAVIGEGATIGAGSVIMRN 165
Cdd:PRK14357  391 FIGSNSSLVAPVRIGKGALIGAGSVITED 419
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 95-165 5.79e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.15  E-value: 5.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221676970  95 RIGEGTVVMPGAIVQAGADIGRHVILNIGCAVDHEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRN 165
Cdd:PRK12461  103 RIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKD 173
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 84-162 7.28e-03

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: 35.76  E-value: 7.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221676970  84 IDNTAFITQDVRIGegtvvmPGAIVQAGadigrhvilnigcavdheVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:COG1043    10 VDPGAKLGENVEIG------PFCVIGPD------------------VEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
136-162 7.74e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 7.74e-03
                          10        20
                  ....*....|....*....|....*..
gi 1221676970 136 AHIGPKCYIGGGAVIGEGATIGAGSVI 162
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVII 28
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
88-180 7.77e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 35.84  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  88 AFITQDVRIGEGTVVMPGAIVQAGADIGR------------------------------------HVILNIGCAVDHEVS 131
Cdd:PRK05289   27 CVIGPNVVIGDGTVIGSHVVIDGHTTIGKnnrifpfasigedpqdlkykgeptrlvigdnntireFVTINRGTVQGGGVT 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1221676970 132 -IGD------FAHIGPKCYIGGGAVIGEGATIgAGSVImrnakIADWTNIPPLSVI 180
Cdd:PRK05289  107 rIGDnnllmaYVHVAHDCVVGNHVILANNATL-AGHVE-----VGDYAIIGGLTAV 156
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 90-175 9.10e-03

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: 36.27  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221676970  90 ITQDVRIGEGTVVMPGA-IVQAGADIGRhviLNIGcavdhEVSIGDFAHIGPKCYIGGGAVIGEGATIGAGSVIMRNAKI 168
Cdd:TIGR02353 128 CTDLLTIGAGTIVRKEVmLLGYRAERGR---LHTG-----PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSI 199

                          90
                  ....*....|
gi 1221676970 169 AD---WTNIP 175
Cdd:TIGR02353 200 PDgerWHGSP 209
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH