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Conserved domains on  [gi|1222444041|ref|WP_090495455|]
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acyltransferase [Pseudoalteromonas sp. DSM 26666]

Protein Classification

WbbJ family protein( domain architecture ID 11414744)

WbbJ family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
89-234 8.99e-40

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 133.84  E-value: 8.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041  89 KLKIECKNDVRISGISTLCGrvsnerePLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGFpGHPIDcerranS 168
Cdd:COG0110     6 LFGARIGDGVVIGPGVRIYG-------GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPID------D 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 169 ESDDESQIGDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNIAE 234
Cdd:COG0110    72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
89-234 8.99e-40

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 133.84  E-value: 8.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041  89 KLKIECKNDVRISGISTLCGrvsnerePLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGFpGHPIDcerranS 168
Cdd:COG0110     6 LFGARIGDGVVIGPGVRIYG-------GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPID------D 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 169 ESDDESQIGDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNIAE 234
Cdd:COG0110    72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 118-229 3.67e-38

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: 128.73  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 118 LSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGFpGHPIDCERRANsesDDESQIGDIIIKRGAWIGTGVTVLAGV 197
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDH-NHDIDDPERPI---EQGVTSAPIVIGDDVWIGANVVILPGV 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1222444041 198 TIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:cd04647    78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 120-226 1.58e-18

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: 80.23  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIgWQNAfSVGRKIILEDDVRLAGRVFLAGfpghpidcerransesddesqigDIIIKRGAWIGTGVTVLAGVTI 199
Cdd:TIGR03570 120 IGDNVII-NTGA-IVEHDCVIGDFVHIAPGVTLSG-----------------------GVVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 1222444041 200 GTGAIIGAGSVVTKDIPDFTIAAGNPA 226
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 116-230 1.73e-18

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.92  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 116 PLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLA----GFPGHPIDCERRANSESDDESQIGDIIIKRGAWIGTGV 191
Cdd:PRK09677   64 GKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITdhnhGSFKHSDDFSSPNLPPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1222444041 192 TVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
178-207 1.42e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.09  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1222444041 178 DIIIKRGAWIGTGVTVLAGVTIGTGAIIGA 207
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
89-234 8.99e-40

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 133.84  E-value: 8.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041  89 KLKIECKNDVRISGISTLCGrvsnerePLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGFpGHPIDcerranS 168
Cdd:COG0110     6 LFGARIGDGVVIGPGVRIYG-------GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTG-NHPID------D 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 169 ESDDESQIGDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNIAE 234
Cdd:COG0110    72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 118-229 3.67e-38

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: 128.73  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 118 LSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGFpGHPIDCERRANsesDDESQIGDIIIKRGAWIGTGVTVLAGV 197
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDH-NHDIDDPERPI---EQGVTSAPIVIGDDVWIGANVVILPGV 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1222444041 198 TIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:cd04647    78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 118-229 2.68e-30

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: 110.20  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 118 LSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRV-FLAgfPGHPIDCERRAnsesdDESQIGD-IIIKRGAWIGTGVTVLA 195
Cdd:cd03357    63 IHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVqIYT--AGHPLDPEERN-----RGLEYAKpITIGDNVWIGGGVIILP 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1222444041 196 GVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:cd03357   136 GVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 108-230 3.70e-30

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 109.17  E-value: 3.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 108 GRVSNEREPLLSIGNNVDIGwqnafsVGRKIILEDDVRLagrVFLAGFPGHPIDCERRANSESDDESQIGDIIIKRGAWI 187
Cdd:cd03349    12 GPDCDVGGDKLSIGKFCSIA------PGVKIGLGGNHPT---DWVSTYPFYIFGGEWEDDAKFDDWPSKGDVIIGNDVWI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1222444041 188 GTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:cd03349    83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 120-230 4.32e-27

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: 100.27  E-value: 4.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIgwQNAFSVGRKIILEDDVRLAGRVFLAG--FPGHPIDcerransesdDESQIGDIIIKRGAWIGTGVTVLAGV 197
Cdd:cd03358    19 IGDNVKI--QSNVSIYEGVTIEDDVFIGPNVVFTNdlYPRSKIY----------RKWELKGTTVKRGASIGANATILPGV 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444041 198 TIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:cd03358    87 TIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 120-226 1.58e-18

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: 80.23  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIgWQNAfSVGRKIILEDDVRLAGRVFLAGfpghpidcerransesddesqigDIIIKRGAWIGTGVTVLAGVTI 199
Cdd:TIGR03570 120 IGDNVII-NTGA-IVEHDCVIGDFVHIAPGVTLSG-----------------------GVVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 1222444041 200 GTGAIIGAGSVVTKDIPDFTIAAGNPA 226
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 116-230 1.73e-18

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 79.92  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 116 PLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLA----GFPGHPIDCERRANSESDDESQIGDIIIKRGAWIGTGV 191
Cdd:PRK09677   64 GKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITdhnhGSFKHSDDFSSPNLPPDMRTLESSAVVIGQRVWIGENV 143

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1222444041 192 TVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK09677  144 TILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
PRK10502 PRK10502
putative acyl transferase; Provisional
 179-230 1.36e-17

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 77.30  E-value: 1.36e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1222444041 179 IIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK10502  125 IVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 120-225 3.72e-17

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: 76.37  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIgWQNAfSVGRKIILEDDVRLAGRVFLAGfpghpidcerransesddesqigDIIIKRGAWIGTGVTVLAGVTI 199
Cdd:cd03360   117 IGDNVII-NTGA-VIGHDCVIGDFVHIAPGVVLSG-----------------------GVTIGEGAFIGAGATIIQGVTI 171

                          90       100
                  ....*....|....*....|....*.
gi 1222444041 200 GTGAIIGAGSVVTKDIPDFTIAAGNP 225
Cdd:cd03360   172 GAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 179-229 5.65e-17

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: 73.79  E-value: 5.65e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1222444041 179 IIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:cd05825    57 IVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 118-234 1.10e-16

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 75.43  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 118 LSIGNNVDIGwqNAFSVGRKIILEDD--VRLAGRVFLA-----GFPGHPIDCERRANSESDDESqigdIIIKRGAWIGTG 190
Cdd:PRK09527   70 FSYGSNIHIG--RNFYANFNLTIVDDytVTIGDNVLIApnvtlSVTGHPVHHELRKNGEMYSFP----ITIGNNVWIGSH 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1222444041 191 VTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNIAE 234
Cdd:PRK09527  144 VVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREIND 187
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 180-231 1.44e-16

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 74.35  E-value: 1.44e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKN 231
Cdd:COG1045   119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 120-225 9.57e-15

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: 67.47  E-value: 9.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIGWQNAFSVGRKIILEDDVRLA-----GRVFLAGFPGHPIdcerransesddesqIGDiiikrGAWIGTGVTVL 194
Cdd:cd03354    11 IGPGLFIDHGTGIVIGETAVIGDNCTIYqgvtlGGKGKGGGKRHPT---------------IGD-----NVVIGAGAKIL 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1222444041 195 AGVTIGTGAIIGAGSVVTKDIPDFTIAAGNP 225
Cdd:cd03354    71 GNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 181-234 5.71e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 67.36  E-value: 5.71e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 181 IKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVT--KDIPDFTIAAGNPAKVVKNIAE 234
Cdd:COG0663    91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTE 146
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 158-232 5.51e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 65.22  E-value: 5.51e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 158 HPIDC-ERRANSESDDESQIGDiiikrGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNI 232
Cdd:PRK10092  113 HPLDPvARNSGAELGKPVTIGN-----NVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 181-234 1.13e-12

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: 63.58  E-value: 1.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1222444041 181 IKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVT--KDIPDFTIAAGNPAKVVKNIAE 234
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRELTD 135
PLN02739 PLN02739
serine acetyltransferase
 116-234 7.91e-12

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 63.90  E-value: 7.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 116 PLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGfpghpidcerRANSESDDESQIGDiiikrGAWIGTGVTVLA 195
Cdd:PLN02739  210 PAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGG----------TGKETGDRHPKIGD-----GALLGACVTILG 274

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1222444041 196 GVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVKNIAE 234
Cdd:PLN02739  275 NISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
PLN02694 PLN02694
serine O-acetyltransferase
 116-229 1.03e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 63.12  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 116 PLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGfpghpidcerRANSESDDESQIGDiiikrGAWIGTGVTVLA 195
Cdd:PLN02694  165 PAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGG----------TGKACGDRHPKIGD-----GVLIGAGATILG 229

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1222444041 196 GVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:PLN02694  230 NVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PLN02357 PLN02357
serine acetyltransferase
 116-229 8.10e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 60.67  E-value: 8.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 116 PLLSIGNNVDIGWQNAFSVGRKIILEDDVRLAGRVFLAGfpghpidcerRANSESDDESQIGDiiikrGAWIGTGVTVLA 195
Cdd:PLN02357  231 PGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGG----------TGKQSGDRHPKIGD-----GVLIGAGTCILG 295

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1222444041 196 GVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:PLN02357  296 NITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
cysE PRK11132
serine acetyltransferase; Provisional
 181-229 1.13e-10

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 59.71  E-value: 1.13e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1222444041 181 IKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:PRK11132  196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 177-229 1.13e-09

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: 56.95  E-value: 1.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1222444041 177 GDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:COG1043   139 GHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLR 191
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-221 2.70e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 56.66  E-value: 2.70e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIA 221
Cdd:PRK14356  400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLA 441
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 173-230 5.87e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 55.64  E-value: 5.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1222444041 173 ESQIGDiiikrGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK14353  380 RTEIGA-----GAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 177-229 8.52e-09

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: 54.36  E-value: 8.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1222444041 177 GDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVV 229
Cdd:cd03351   137 GHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLR 189
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-230 1.43e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.38  E-value: 1.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK14357  385 FIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 180-217 1.57e-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: 52.81  E-value: 1.57e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPD 217
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPP 183
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 187-234 4.85e-08

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 50.65  E-value: 4.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222444041 187 IGTGVTVLAGVTIGTGAIIGAGSVVT--KDIPDFTIAAGNPAKVVKNIAE 234
Cdd:cd04650    87 VGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTE 136
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 180-217 6.41e-08

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: 52.34  E-value: 6.41e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPD 217
Cdd:COG1207   396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPA 433
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 137-234 1.36e-07

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: 49.67  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 137 KIILEDDVRLAGRVFLAGFPGhpIDCERRANSESDDESQIGDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTK--D 214
Cdd:cd04745    39 RIVIRDGANVQDNCVIHGFPG--QDTVLEENGHIGHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtV 116

                          90       100
                  ....*....|....*....|
gi 1222444041 215 IPDFTIAAGNPAKVVKNIAE 234
Cdd:cd04745   117 IPPRSLIAGSPAKVIRELSD 136
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 177-227 1.54e-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: 50.10  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1222444041 177 GDIIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAK 227
Cdd:cd03352   149 GSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
PLN02296 PLN02296
carbonate dehydratase
 185-234 2.38e-07

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 50.12  E-value: 2.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1222444041 185 AWIGTGVTVLAGVTIGTGAIIGAGSVVTKD--IPDFTIAAGNPAKVVKNIAE 234
Cdd:PLN02296  143 AFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTE 194
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-221 3.11e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.22  E-value: 3.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIA 221
Cdd:PRK14354  395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
197-228 2.82e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.02  E-value: 2.82e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1222444041 197 VTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKV 228
Cdd:PRK05289  160 VRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 120-229 4.79e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 47.05  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIG-----WQNAFSVGRKIILEDDVRLAGRvflagfpghpidcerRANSesdDESQIGDIIIKRGAWIGTGVTVL 194
Cdd:TIGR02353 115 IGKGVDIGslppvCTDLLTIGAGTIVRKEVMLLGY---------------RAER---GRLHTGPVTLGRDAFIGTRSTLD 176

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1222444041 195 AGVTIGTGAIIGAGSVVTKD--IPDFTIAAGNPAKVV 229
Cdd:TIGR02353 177 IDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPAQKT 213
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 179-226 8.14e-06

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 46.28  E-value: 8.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222444041 179 IIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTK--DIPDFTIAAGNPA 226
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
PRK10191 PRK10191
putative acyl transferase; Provisional
 180-228 2.27e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 42.95  E-value: 2.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKV 228
Cdd:PRK10191   94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-230 7.63e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.19  E-value: 7.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK14355  399 VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNK 449
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-217 1.31e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.32  E-value: 1.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPD 217
Cdd:PRK09451  396 IIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAE 433
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
178-207 1.42e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.09  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1222444041 178 DIIIKRGAWIGTGVTVLAGVTIGTGAIIGA 207
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 187-227 1.64e-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: 41.93  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1222444041 187 IGTGVtVLAG-------VTIGTGAIIGAGSVVTKDIPDFTIAAGNPAK 227
Cdd:COG1044   261 IGDNV-VIGGqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 120-212 2.84e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.38  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIgwQNAFSVGRKIILEDDVRLAGRVFLAGFPGhpidcerransesddESQIGDIIIKRGAWIGTGVTVLAGVTI 199
Cdd:cd00208     3 IGEGVKI--HPKAVIRGPVVIGDNVNIGPGAVIGAATG---------------PNEKNPTIIGDNVEIGANAVIHGGVKI 65

                          90
                  ....*....|...
gi 1222444041 200 GTGAIIGAGSVVT 212
Cdd:cd00208    66 GDNAVIGAGAVVT 78
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 179-223 2.93e-04

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: 39.67  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1222444041 179 IIIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIAAG 223
Cdd:cd03350    76 VIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETG 120
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 187-231 4.73e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 4.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1222444041 187 IGTGVTVLAGVTIGTGAIIGAGSVVTKDIPDFTIA-AGNPAKVVKN 231
Cdd:PRK14352  408 TGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAvSEGPQRNIEG 453
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 192-230 5.42e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.68  E-value: 5.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1222444041 192 TVL-AGVTIGTGAIIGAGSVVTKDIPDFTIAAGNPAKVVK 230
Cdd:PRK14360  403 SVLvAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 180-231 1.71e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.82  E-value: 1.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVVTKDIP--DFTIAAGnPAKVVKN 231
Cdd:PRK14359  369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPkgSLAISRA-PQKNIKN 421
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 171-211 2.35e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.46  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1222444041 171 DDESQIGDiiikrGAWIGTGVTVLAGVTIGTGAIIGAGSVV 211
Cdd:COG1044   106 DPSAKIGE-----GVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 120-211 5.63e-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: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 120 IGNNVDIGwqnAFSVgrkiiLEDDVRLAGRVFLagFPGHPIDcerransesdDESQIGDiiikrGAWIGTGVTVLAGVTI 199
Cdd:cd03352     4 IGENVSIG---PNAV-----IGEGVVIGDGVVI--GPGVVIG----------DGVVIGD-----DCVIHPNVTIYEGCII 58

                          90
                  ....*....|..
gi 1222444041 200 GTGAIIGAGSVV 211
Cdd:cd03352    59 GDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 119-211 6.57e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.92  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 119 SIGNNVDIGwqnAFSV-GRKIILEDDVRLAGRVFLAgfpghpidcerransesdDESQIGDiiikrGAWIGTGVTVLAGV 197
Cdd:COG1044   110 KIGEGVSIG---PFAViGAGVVIGDGVVIGPGVVIG------------------DGVVIGD-----DCVLHPNVTIYERC 163

                          90
                  ....*....|....
gi 1222444041 198 TIGTGAIIGAGSVV 211
Cdd:COG1044   164 VIGDRVIIHSGAVI 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 180-211 7.72e-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: 36.23  E-value: 7.72e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1222444041 180 IIKRGAWIGTGVTVLAGVTIGTGAIIGAGSVV 211
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVI 34
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 161-228 7.76e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.54  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444041 161 DCERRANSESDDESQIGD-IIIKRGAWIGTGVTV-----LAG-------VTIGTGAIIGAGSVVTKDIPDFTIAAGNPAK 227
Cdd:PRK12461  107 DNLLMAYSHVAHDCQIGNnVILVNGALLAGHVTVgdraiISGnclvhqfCRIGALAMMAGGSRISKDVPPYCMMAGHPTN 186


                  .
gi 1222444041 228 V 228
Cdd:PRK12461  187 V 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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