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Conserved domains on  [gi|1209319062|ref|WP_088360873|]
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MULTISPECIES: acyltransferase [Bacillus cereus group]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

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];
36-174 2.70e-25

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 94.94  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFCILSG-KITIGSYSHIAAYTALFGGEmGIEMHDFANISSKTIVYAAIDDFSGNTLMgptiphqykNVK 114
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTGNHPIDDPATF---------PLR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062 115 AGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKN 174
Cdd:COG0110    79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-174 2.70e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 94.94  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFCILSG-KITIGSYSHIAAYTALFGGEmGIEMHDFANISSKTIVYAAIDDFSGNTLMgptiphqykNVK 114
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTGNHPIDDPATF---------PLR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062 115 AGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKN 174
Cdd:COG0110    79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 36-168 4.59e-21

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: 83.27  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFCILS--GKITIGSYSHIAAYTALFGGemgieMHDFANISsktivyaaiddfsgntlmgptiPHQYKNV 113
Cdd:cd04647     2 ISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDH-----NHDIDDPE----------------------RPIEQGV 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1209319062 114 KAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKI 168
Cdd:cd04647    55 TSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10502 PRK10502
putative acyl transferase; Provisional
 17-174 2.03e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.88  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLISKKTSIYNPGAISVGNNVRI-DDFCILS-GKITIGSYSHIAAYTALFGGEmgiemHDFANissktivyaaiD 94
Cdd:PRK10502   53 KIGKGVVIRPSVRITYPWKLTIGDYAWIgDDVWLYNlGEITIGAHCVISQKSYLCTGS-----HDYSD-----------P 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  95 DFsgntlmgptiphqykNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKN 174
Cdd:PRK10502  117 HF---------------DLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRVET 181
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 17-164 5.51e-07

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: 47.87  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLIskktsiyNPGAIsVGNNVRIDDFCILSGKITIGSYSHIAaytalfggemgiemhDFANISSKTIVyaaiddf 96
Cdd:TIGR03570 101 SIGEGTVI-------MAGAV-INPDVRIGDNVIINTGAIVEHDCVIG---------------DFVHIAPGVTL------- 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209319062  97 sgntlmgptiphqyknvkAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVP 164
Cdd:TIGR03570 151 ------------------SGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-174 2.70e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 94.94  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFCILSG-KITIGSYSHIAAYTALFGGEmGIEMHDFANISSKTIVYAAIDDFSGNTLMgptiphqykNVK 114
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTGNHPIDDPATF---------PLR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062 115 AGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKN 174
Cdd:COG0110    79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 36-168 4.59e-21

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: 83.27  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFCILS--GKITIGSYSHIAAYTALFGGemgieMHDFANISsktivyaaiddfsgntlmgptiPHQYKNV 113
Cdd:cd04647     2 ISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDH-----NHDIDDPE----------------------RPIEQGV 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1209319062 114 KAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKI 168
Cdd:cd04647    55 TSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10502 PRK10502
putative acyl transferase; Provisional
 17-174 2.03e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.88  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLISKKTSIYNPGAISVGNNVRI-DDFCILS-GKITIGSYSHIAAYTALFGGEmgiemHDFANissktivyaaiD 94
Cdd:PRK10502   53 KIGKGVVIRPSVRITYPWKLTIGDYAWIgDDVWLYNlGEITIGAHCVISQKSYLCTGS-----HDYSD-----------P 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  95 DFsgntlmgptiphqykNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKN 174
Cdd:PRK10502  117 HF---------------DLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRVET 181
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 17-169 4.39e-10

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: 54.81  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLISKKTSIynpgaisvGNNVRIDDFCILSGKITIGSYSHIAAYTAlfggemgiemhdFANissktivyaaiDDF 96
Cdd:cd03358     6 IIGTNVFIENDVKI--------GDNVKIQSNVSIYEGVTIEDDVFIGPNVV------------FTN-----------DLY 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209319062  97 SGNTlmgptiphQYKNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIK 169
Cdd:cd03358    55 PRSK--------IYRKWELKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 33-168 2.26e-09

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: 52.61  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  33 PGAISVGNNVRI-DDFCILS-GKITIGSYSHIAAYTALFGGEmgiemHDFANissktivyaaiDDFsgntlmgptiphqy 110
Cdd:cd05825     1 PWNLTIGDNSWIgEGVWIYNlAPVTIGSDACISQGAYLCTGS-----HDYRS-----------PAF-------------- 50

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209319062 111 kNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKI 168
Cdd:cd05825    51 -PLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 30-169 6.88e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 52.72  E-value: 6.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  30 IYNPGAIS--VGNNVRIDDFCILSGKITIGSYSHIAAYTALFGGEMGIEMHDFANISSKTIVYAAiDDFSgnTLMGP--T 105
Cdd:COG0663     3 IYSFDGKTpqIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-PGYP--LTIGDdvT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209319062 106 IPHQyknvkagkVVL-----KKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKE--SLDDWYMYVGVPVRKIK 169
Cdd:COG0663    80 IGHG--------AILhgctiGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPGSLVVGSPAKVVR 142
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 49-177 2.86e-08

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: 50.83  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  49 ILSGKITIGSYSHIAAYTALFGGEMGIEMHDFANISSKTIVYAaiddFSGNTlmgpTIPHQYKNVKAGKVV----LKKHA 124
Cdd:cd04745    14 VLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHG----FPGQD----TVLEENGHIGHGAILhgctIGRNA 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1209319062 125 IVGAHSIIFPNVVIGEGAAVGAMSMVKES--LDDWYMYVGVPVRKIKARKKNIVE 177
Cdd:cd04745    86 LVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSDEEVA 140
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 17-164 1.50e-07

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: 49.41  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLIskktsiyNPGAIsVGNNVRIDDFCILSGKITIGSYSHIaaytalfggemgiemHDFANISSKTIVyaaiddf 96
Cdd:cd03360    98 VIGEGCVI-------MAGAV-INPDARIGDNVIINTGAVIGHDCVI---------------GDFVHIAPGVVL------- 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209319062  97 sgntlmgptiphqyknvkAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVP 164
Cdd:cd03360   148 ------------------SGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 17-164 5.51e-07

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: 47.87  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  17 SVGENVLIskktsiyNPGAIsVGNNVRIDDFCILSGKITIGSYSHIAaytalfggemgiemhDFANISSKTIVyaaiddf 96
Cdd:TIGR03570 101 SIGEGTVI-------MAGAV-INPDVRIGDNVIINTGAIVEHDCVIG---------------DFVHIAPGVTL------- 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209319062  97 sgntlmgptiphqyknvkAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVP 164
Cdd:TIGR03570 151 ------------------SGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 30-171 1.40e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 46.41  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  30 IYNPGAISVGNNVRIDDF----CILSgkITIGSYSHIAAytalfggEMGIEMHDFANISSKtivyaaiDDFSGntlmgPT 105
Cdd:PRK09677   60 AFGRGKLFFGDNVQVNDYvhiaCIES--ITIGRDTLIAS-------KVFITDHNHGSFKHS-------DDFSS-----PN 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209319062 106 IPHQYKNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKAR 171
Cdd:PRK09677  119 LPPDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 37-169 1.94e-06

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 45.48  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  37 SVGNNVRIDDFCILSGKITIGSYSHIAAYTALFGGEMGIEMHDFANISSKTIVYAAIDdfsgntlmGPTIPHQYKNVKAG 116
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPG--------YPTIIGDNVTVGHG 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1209319062 117 KVV----LKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKE--SLDDWYMYVGVPVRKIK 169
Cdd:cd04645    73 AVLhgctIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPgkVIPPGSLVAGSPAKVVR 131
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 105-164 2.18e-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: 2.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062 105 TIPHQYKNVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVP 164
Cdd:cd03354    42 TLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 49-169 3.36e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 39.79  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  49 ILSGKITIGSYSHIAAYTALFGGEMGIEMHDFANISSKTIV--YAAIDdfsgntlmgpTIPHQYKNVKAGKV----VLKK 122
Cdd:PRK13627   24 VLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMhgYCDTD----------TIVGENGHIGHGAIlhgcVIGR 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1209319062 123 HAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDW--YMYVGVPVRKIK 169
Cdd:PRK13627   94 DALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEkrQLLMGTPARAVR 142
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 36-171 5.23e-04

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: 38.68  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  36 ISVGNNVRIDDFC--ILSGKITIGSYSHIAAYTALFGGE----MGIEMHDFANISSKTIVYAAIDDFsgntlmgptiphq 109
Cdd:cd03349     2 ISVGDYSYGSGPDcdVGGDKLSIGKFCSIAPGVKIGLGGnhptDWVSTYPFYIFGGEWEDDAKFDDW------------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209319062 110 yknVKAGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKAR 171
Cdd:cd03349    69 ---PSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 115-180 6.11e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 6.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209319062 115 AGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYV-GVPVRKIKARKKNIVELEN 180
Cdd:PRK00892  259 AGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSsGIPAQPNKEWLRTAARLRR 325
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 118-146 6.17e-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: 39.23  E-value: 6.17e-04
                          10        20
                  ....*....|....*....|....*....
gi 1209319062 118 VVLKKHAIVGAHSIIFPNVVIGEGAAVGA 146
Cdd:COG1044   121 AVIGAGVVIGDGVVIGPGVVIGDGVVIGD 149
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 2-173 1.34e-03

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 38.06  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062   2 NSFYSQEELSEIGFLSVGENVLISKktsiynPGAISVGNNVRIDDFCILSGKITIgsyshIAAYTALFGGemgiemhdfa 81
Cdd:PRK09527   42 SEVEKRESLIKEMFATVGENAWVEP------PVYFSYGSNIHIGRNFYANFNLTI-----VDDYTVTIGD---------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209319062  82 nissktivyaaiddfsgNTLMGPTI-------PHQYKNVKAGK-----VVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSM 149
Cdd:PRK09527  101 -----------------NVLIAPNVtlsvtghPVHHELRKNGEmysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSV 163

                         170       180
                  ....*....|....*....|....*..
gi 1209319062 150 VKESLDDWYMYVGVP---VRKIKARKK 173
Cdd:PRK09527  164 VTKDIPPNVVAAGVPcrvIREINDRDK 190
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 126-168 1.62e-03

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: 37.40  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1209319062 126 VGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKI 168
Cdd:cd03357   127 IGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 115-180 1.64e-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: 38.07  E-value: 1.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209319062 115 AGKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMVKESLDDWYMYVGVPVRKIKARKKNIVELEN 180
Cdd:COG1044   256 AGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREWLRNAAALRR 321
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 118-146 1.68e-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: 37.77  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|....*....
gi 1209319062 118 VVLKKHAIVGAHSIIFPNVVIGEGAAVGA 146
Cdd:cd03352    14 AVIGEGVVIGDGVVIGPGVVIGDGVVIGD 42
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 116-150 3.27e-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: 37.42  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1209319062 116 GKVVLKKHAIVGAHSIIFPNVVIGEGAAVGAMSMV 150
Cdd:TIGR02353 159 GPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSAL 193
 
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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