NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1430660611|gb|AXE61687|]
View 

hypothetical protein CRN91_03220 [Candidatus Thioglobus sp. NP1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
21-139 1.29e-23

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 89.16  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  21 YHPLVWINGNPKIGKNVVIAGFSEINANHvNVTIGDNCDIASFVSINAAdSHKKCLGLSDEIERKDITIGDHVFIGSHCV 100
Cdd:COG0110    18 GPGVRIYGGNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTG-NHPIDDPATFPLRTGPVTIGDDVWIGAGAT 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1430660611 101 VKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPM-IIKK 139
Cdd:COG0110    96 ILPGVTIGDGAVVGAGSVVTK-DVPPYAIVAGNPArVIRK 134
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
21-139 1.29e-23

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 89.16  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  21 YHPLVWINGNPKIGKNVVIAGFSEINANHvNVTIGDNCDIASFVSINAAdSHKKCLGLSDEIERKDITIGDHVFIGSHCV 100
Cdd:COG0110    18 GPGVRIYGGNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTG-NHPIDDPATFPLRTGPVTIGDDVWIGAGAT 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1430660611 101 VKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPM-IIKK 139
Cdd:COG0110    96 ILPGVTIGDGAVVGAGSVVTK-DVPPYAIVAGNPArVIRK 134
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 32-134 7.90e-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: 80.96  E-value: 7.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINAnHVNVTIGDNCDIASFVSINAA--DSHKKCLGLSDEIERKDITIGDHVFIGSHCVVKGGANIGN 109
Cdd:cd04647     3 SIGDNVYIGPGCVISA-GGGITIGDNVLIGPNVTIYDHnhDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*
gi 1430660611 110 YCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd04647    82 GAVVGAGSVVTK-DVPPNSIVAGNP 105
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 22-134 1.03e-14

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: 67.52  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINAN-------HVN--------VTIGDNCDIASFVSINAadshkkclglsdeierkD 86
Cdd:TIGR03570  91 HPSAIVSPSASIGEGTVIMAGAVINPDvrigdnvIINtgaivehdCVIGDFVHIAPGVTLSG-----------------G 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  87 ITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:TIGR03570 154 VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTK-DIPDGGVVVGVP 200
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 2-143 1.99e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 58.86  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611   2 FNKIIQKIFTKFTTFKANPY-HPLVWIN--GNPKIGKNVViAGFSEINANHVNVTIGDNCDIASFVSINAADS--HKKcL 76
Cdd:PRK09527   44 VEKRESLIKEMFATVGENAWvEPPVYFSygSNIHIGRNFY-ANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHpvHHE-L 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430660611  77 GLSDEIERKDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPMII--------KKGYYR 143
Cdd:PRK09527  122 RKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTK-DIPPNVVAAGVPCRVireindrdKQYYFK 195
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
86-115 7.78e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1430660611  86 DITIGDHVFIGSHCVVKGGANIGNYCVIGA 115
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
21-139 1.29e-23

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 89.16  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  21 YHPLVWINGNPKIGKNVVIAGFSEINANHvNVTIGDNCDIASFVSINAAdSHKKCLGLSDEIERKDITIGDHVFIGSHCV 100
Cdd:COG0110    18 GPGVRIYGGNITIGDNVYIGPGVTIDDPG-GITIGDNVLIGPGVTILTG-NHPIDDPATFPLRTGPVTIGDDVWIGAGAT 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1430660611 101 VKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPM-IIKK 139
Cdd:COG0110    96 ILPGVTIGDGAVVGAGSVVTK-DVPPYAIVAGNPArVIRK 134
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 32-134 7.90e-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: 80.96  E-value: 7.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINAnHVNVTIGDNCDIASFVSINAA--DSHKKCLGLSDEIERKDITIGDHVFIGSHCVVKGGANIGN 109
Cdd:cd04647     3 SIGDNVYIGPGCVISA-GGGITIGDNVLIGPNVTIYDHnhDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*
gi 1430660611 110 YCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd04647    82 GAVVGAGSVVTK-DVPPNSIVAGNP 105
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 30-134 8.43e-15

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: 67.06  E-value: 8.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  30 NPKIGKNVVIagfseiNANHV-----NVTIGDNCDIASFVSINAADSHkkclglSDEIERKD-------ITIGDHVFIGS 97
Cdd:cd03357    62 NIHIGDNFYA------NFNCTildvaPVTIGDNVLIGPNVQIYTAGHP------LDPEERNRgleyakpITIGDNVWIGG 129

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1430660611  98 HCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd03357   130 GVIILPGVTIGDNSVIGAGSVVTK-DIPANVVAAGNP 165
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 22-134 1.03e-14

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: 67.52  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINAN-------HVN--------VTIGDNCDIASFVSINAadshkkclglsdeierkD 86
Cdd:TIGR03570  91 HPSAIVSPSASIGEGTVIMAGAVINPDvrigdnvIINtgaivehdCVIGDFVHIAPGVTLSG-----------------G 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  87 ITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:TIGR03570 154 VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTK-DIPDGGVVVGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 3-134 1.52e-14

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: 67.12  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611   3 NKIIQKIFTKFTTFKANPY---HPLVWINGNPKIGKNVVIAGFSEINA-----NHV----NVTIGDNCDIASFVSINaad 70
Cdd:cd03360    66 NKLRRKLAEKLLAAGYRFAtliHPSAVVSPSAVIGEGCVIMAGAVINPdarigDNViintGAVIGHDCVIGDFVHIA--- 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430660611  71 SHKKCLGlsdeierkDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd03360   143 PGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTK-DVPDGSVVVGNP 197
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 46-134 1.63e-13

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: 63.33  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  46 NANHVNVTIGDNCDIASFVSINAADSHK-----------------KCLGLSDEIERKDITIGDHVFIGSHCVVKGGANIG 108
Cdd:cd03349    16 DVGGDKLSIGKFCSIAPGVKIGLGGNHPtdwvstypfyifggeweDDAKFDDWPSKGDVIIGNDVWIGHGATILPGVTIG 95

                          90       100
                  ....*....|....*....|....*.
gi 1430660611 109 NYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd03349    96 DGAVIAAGAVVTK-DVPPYAIVGGNP 120
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 33-139 1.06e-11

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 57.90  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  33 IGKNVVIAGFSEINANhvnVTIGDNCDIASFVSI--------------NAA---DSHKKCLGLSDEiERKDITIGDHVFI 95
Cdd:cd03358     1 IGDNCIIGTNVFIEND---VKIGDNVKIQSNVSIyegvtieddvfigpNVVftnDLYPRSKIYRKW-ELKGTTVKRGASI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1430660611  96 GSHCVVKGGANIGNYCVIGAGTIVEgVDIPEYSLVIGNPMIIKK 139
Cdd:cd03358    77 GANATILPGVTIGEYALVGAGAVVT-KDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 25-134 1.44e-11

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: 57.06  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  25 VWINGNPKIGKNVVIAGFSEINANHvNVTIGDNCDIASFVSINaadshkkclGLSDEIERKDITIGDHVFIGSHCVVKGG 104
Cdd:cd03354     3 IDIHPGAKIGPGLFIDHGTGIVIGE-TAVIGDNCTIYQGVTLG---------GKGKGGGKRHPTIGDNVVIGAGAKILGN 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1430660611 105 ANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:cd03354    73 ITIGDNVKIGANAVVTK-DVPANSTVVGVP 101
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 2-143 1.99e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 58.86  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611   2 FNKIIQKIFTKFTTFKANPY-HPLVWIN--GNPKIGKNVViAGFSEINANHVNVTIGDNCDIASFVSINAADS--HKKcL 76
Cdd:PRK09527   44 VEKRESLIKEMFATVGENAWvEPPVYFSygSNIHIGRNFY-ANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHpvHHE-L 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430660611  77 GLSDEIERKDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPMII--------KKGYYR 143
Cdd:PRK09527  122 RKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTK-DIPPNVVAAGVPCRVireindrdKQYYFK 195
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 88-134 2.81e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 57.73  E-value: 2.81e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  88 TIGDHVFIGSHCVVKGGANIGNYCVIGAGTIV-EGVDIPEYSLVIGNP 134
Cdd:COG0663    90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVtEGKVVPPGSLVVGSP 137
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 32-134 3.05e-11

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: 57.42  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINANHVN-VTIGDNCDIASFVSINAAdshkkclglsdeierkdiTIGDHVFIGSHCVVKGGANIGNY 110
Cdd:cd04645    40 RIGERTNIQDGSVLHVDPGYpTIIGDNVTVGHGAVLHGC------------------TIGDNCLIGMGAIILDGAVIGKG 101

                          90       100
                  ....*....|....*....|....*
gi 1430660611 111 CVIGAGTIV-EGVDIPEYSLVIGNP 134
Cdd:cd04645   102 SIVAAGSLVpPGKVIPPGSLVAGSP 126
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 22-119 1.18e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.02  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSInaadshkkclGlsdeierKDITIGDHVFIGSHCVV 101
Cdd:COG1044   100 HPSAVIDPSAKIGEGVSIGPFAVIGAG---VVIGDGVVIGPGVVI----------G-------DGVVIGDDCVLHPNVTI 159

                          90
                  ....*....|....*...
gi 1430660611 102 KGGANIGNYCVIGAGTIV 119
Cdd:COG1044   160 YERCVIGDRVIIHSGAVI 177
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 33-135 1.58e-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: 51.84  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  33 IGKNVVIAgfseinaNHVNVTIGDNCDIASFVSInaadshkkCLGLSD------EIERKDITIGDHVFIGSHCVVKGGAN 106
Cdd:cd05825    12 IGEGVWIY-------NLAPVTIGSDACISQGAYL--------CTGSHDyrspafPLITAPIVIGDGAWVAAEAFVGPGVT 76

                          90       100
                  ....*....|....*....|....*....
gi 1430660611 107 IGNYCVIGAGTIVEGvDIPEYSLVIGNPM 135
Cdd:cd05825    77 IGEGAVVGARSVVVR-DLPAWTVYAGNPA 104
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 32-139 4.48e-09

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: 52.01  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIagfseinanHVNVTIGdncdiasfvsinaadshkkclGLSDEIERKDITIGDHVFIGSHCVVKGGANIGNYC 111
Cdd:COG1045    93 VIGDNVTI---------YQGVTLG---------------------GTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNA 142

                          90       100
                  ....*....|....*....|....*...
gi 1430660611 112 VIGAGTIVEGvDIPEYSLVIGNPMIIKK 139
Cdd:COG1045   143 KIGANSVVLK-DVPPGSTVVGVPARIVK 169
PRK10502 PRK10502
putative acyl transferase; Provisional
 33-139 7.58e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 51.49  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  33 IGKNVVIAgfseinaNHVNVTIGDNCDIASFV-----SINAADSHKKclglsdeIERKDITIGDHVFIGSHCVVKGGANI 107
Cdd:PRK10502   80 IGDDVWLY-------NLGEITIGAHCVISQKSylctgSHDYSDPHFD-------LNTAPIVIGEGCWLAADVFVAPGVTI 145

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1430660611 108 GNYCVIGAGTIVEGvDIPEYSLVIGNPMIIKK 139
Cdd:PRK10502  146 GSGAVVGARSSVFK-SLPANTICRGNPAVPIR 176
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 29-141 1.63e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 51.03  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  29 GNPKI--GKNVVIAGFSEInANHVNVTIGDNCDIASFVSINaaDSHKKCLGLSDE------------IERKDITIGDHVF 94
Cdd:PRK09677   62 GRGKLffGDNVQVNDYVHI-ACIESITIGRDTLIASKVFIT--DHNHGSFKHSDDfsspnlppdmrtLESSAVVIGQRVW 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1430660611  95 IGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNPMIIKKGY 141
Cdd:PRK09677  139 IGENVTILPGVSIGNGCIVGANSVVTK-SIPENTVIAGNPAKIIKKY 184
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 22-134 2.06e-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: 49.88  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINANHVNVTIGDNCDIASFVSINAADSHKKCLGLSDEIERKDIT----IGDHVFIGS 97
Cdd:cd04650    10 HPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVhgakVGNYVIVGM 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1430660611  98 HCVVKGGANIGNYCVIGAGTIV-EGVDIPEYSLVIGNP 134
Cdd:cd04650    90 GAILLNGAKIGDHVIIGAGAVVtPGKEIPDYSLVLGVP 127
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 22-144 1.46e-07

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: 48.87  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEInanhVNVTIGDNCDIASFVSINA---------------------ADSH-------K 73
Cdd:COG1207   276 DPNVILEGKTVIGEGVVIGPNCTL----KDSTIGDGVVIKYSVIEDAvvgagatvgpfarlrpgtvlgEGVKignfvevK 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  74 KC-LG-------LS---D-EI-ERKDI-----------------TIGDHVFIGSHCV----VKgganIGNYCVIGAG-TI 118
Cdd:COG1207   352 NStIGegskvnhLSyigDaEIgEGVNIgagtitcnydgvnkhrtVIGDGAFIGSNTNlvapVT----IGDGATIGAGsTI 427

                         170       180
                  ....*....|....*....|....*..
gi 1430660611 119 VEgvDIPEYSLVIG-NPMIIKKGYYRK 144
Cdd:COG1207   428 TK--DVPAGALAIArARQRNIEGWVRP 452
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 32-119 2.42e-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: 47.79  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSInaadshkkclglsdeieRKDITIGDHVFIGSHCVVKGGANIGNYC 111
Cdd:cd03352     3 KIGENVSIGPNAVIGEG---VVIGDGVVIGPGVVI-----------------GDGVVIGDDCVIHPNVTIYEGCIIGDRV 62


                  ....*...
gi 1430660611 112 VIGAGTIV 119
Cdd:cd03352    63 IIHSGAVI 70
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 32-119 2.85e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 45.32  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSINAADShkkclglsdEIERKDITIGDHVFIGSHCVVKGGANIGNYC 111
Cdd:cd00208     2 FIGEGVKIHPKAVIRGP---VVIGDNVNIGPGAVIGAATG---------PNEKNPTIIGDNVEIGANAVIHGGVKIGDNA 69


                  ....*...
gi 1430660611 112 VIGAGTIV 119
Cdd:cd00208    70 VIGAGAVV 77
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 23-134 3.80e-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: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  23 PLVWINGNP-----------KIGKNVVIagFSEINANHVNVTIGDNCDIASFVSINAADSHkkclglSDEIERKDITIGD 91
Cdd:TIGR02353  94 PTVLLSGSPlyslylralgaKIGKGVDI--GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAE------RGRLHTGPVTLGR 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1430660611  92 HVFIGSHCVVKGGANIGNYCVIGAGTIVE-GVDIPEYSLVIGNP 134
Cdd:TIGR02353 166 DAFIGTRSTLDIDTSIGDGAQLGHGSALQgGQSIPDGERWHGSP 209
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-119 4.59e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.44  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611   2 FNKIIQKIFTKFTTFKANPYHPLVWINGNPKIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSINAadshkkclglsde 81
Cdd:PRK00892   84 FARLAQLFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAG---VVIGDGVVIGAGAVIGD------------- 147

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1430660611  82 ierkDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIV 119
Cdd:PRK00892  148 ----GVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 36-139 5.60e-07

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: 46.05  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  36 NVVIAGFSEINANHV------NVTIGDNCDIASFVSINAAdshkkCLGLSDEIERKDITIGDHVFIGSHCVVKgGANIGN 109
Cdd:cd03359    21 NIVLNGKTIIQSDVIirgdlaTVSIGRYCILSEGCVIRPP-----FKKFSKGVAFFPLHIGDYVFIGENCVVN-AAQIGS 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1430660611 110 YCVIGAGTIV-------------------EGVDIPEYSLVIGNPMIIKK 139
Cdd:cd03359    95 YVHIGKNCVIgrrciikdcvkildgtvvpPDTVIPPYSVVSGRPARFIG 143
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 33-131 6.82e-07

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: 47.03  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  33 IGKNVVI-AGFSEINAnHVN--------------VTIGDNCDIASFVSINaadshkkclGLSDEIERKDITIGDHVFIGS 97
Cdd:COG2171   112 LAPGVVLmPSFVNIGA-YVDegtmvdtwatvgscAQIGKNVHLSGGAGIG---------GVLEPLQAAPVIIEDNCFIGA 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  98 HCVVKGGANIGNYCVIGAGTIVEG----VD----------IPEYSLVI 131
Cdd:COG2171   182 RSGVVEGVIVGEGAVLGAGVYLTAstkiYDrvtgevyygrVPAGSVVV 229
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 22-119 7.01e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.13  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEInanhVNVTIGDNCDIASFVsINAADSHKKC-LGLSDEIeRKDITIGDHVFIGSHCV 100
Cdd:PRK14354  275 EPGVVIKGNTVIGEDCVIGPGSRI----VDSTIGDGVTITNSV-IEESKVGDNVtVGPFAHL-RPGSVIGEEVKIGNFVE 348

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1430660611 101 VK----------------GGANIGNYCVIGAGTIV 119
Cdd:PRK14354  349 IKkstigegtkvshltyiGDAEVGENVNIGCGTIT 383
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 22-125 7.48e-07

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 46.08  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINANHVN-VTIGDNCDIASFVSINAADSHKKCLGLSDEIERKDI-----TIGDHVFI 95
Cdd:cd00710    12 HPTAVVIGDVIIGDNVFVGPGASIRADEGTpIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIvhgpaYIGDNCFI 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 1430660611  96 GSHCVVKGgANIGNYCVIGAGTIVEGVDIP 125
Cdd:cd00710    92 GFRSVVFN-AKVGDNCVIGHNAVVDGVEIP 120
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 49-137 8.44e-07

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: 46.66  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  49 HV--NVTIGDNCDIASFVSINAadsHkkclglsdeierkdITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPE 126
Cdd:cd03351   116 HVahDCVIGNNVILANNATLAG---H--------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQ-DVPP 177

                          90
                  ....*....|.
gi 1430660611 127 YSLVIGNPMII 137
Cdd:cd03351   178 YVIAAGNRARL 188
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 48-136 1.06e-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: 45.86  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  48 NHV----NVTIGDNCDIASFVSInaADShkkclglsdeierkdITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvD 123
Cdd:cd03352   125 NLVqiahNVRIGENCLIAAQVGI--AGS---------------TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTS-I 186

                          90
                  ....*....|...
gi 1430660611 124 IPEYSLVIGNPMI 136
Cdd:cd03352   187 VPPGEYVSGTPAQ 199
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 21-124 1.26e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  21 YHPLVWINGNPKIGKNVVIagfseinanHVNVTIGDNCDIASFVSINAadshkkclglsdeierkDITIGDHVFIGSHCV 100
Cdd:PRK00892   91 FDPPATPSPAAGIHPSAVI---------DPSAKIGEGVSIGPNAVIGA-----------------GVVIGDGVVIGAGAV 144

                          90       100
                  ....*....|....*....|....*
gi 1430660611 101 VKGGANIGNYCVIGAG-TIVEGVDI 124
Cdd:PRK00892  145 IGDGVKIGADCRLHANvTIYHAVRI 169
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 49-133 1.31e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.16  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  49 HVNVTIGDNCDIASFVSINAadshkkclglsdeierkDITIGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEGVdipey 127
Cdd:COG1044   106 DPSAKIGEGVSIGPFAVIGA-----------------GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNvTIYERC----- 163


                  ....*.
gi 1430660611 128 slVIGN 133
Cdd:COG1044   164 --VIGD 167
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 16-134 8.64e-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: 43.97  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  16 FKANPYHPLVWINGNPKIGKNVVIAGFseinanhvNVTIGDNCDIASFVSINAAdSHKKCLGLSDEIERKD-ITIGDHVF 94
Cdd:TIGR02353 583 FRGTPFLPAILRLLGVKIGRGVYIDGT--------DLTERDLVTIGDDSTLNEG-SVIQTHLFEDRVMKSDtVTIGDGAT 653

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1430660611  95 IGSHCVVKGGANIGNYCVIGAGTIV-EGVDIPEYSLVIGNP 134
Cdd:TIGR02353 654 LGPGAIVLYGVVMGEGSVLGPDSLVmKGEEVPAHTRWRGNP 694
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 51-124 1.61e-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: 42.78  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430660611  51 NVTIGDNCDIASFVSInaadshkkclglsdeieRKDITIGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEGVDI 124
Cdd:cd03352     1 SAKIGENVSIGPNAVI-----------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNvTIYEGCII 58
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 22-118 1.62e-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: 42.41  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEInanhVNVTIGDNCDIASFVSINAADSHKKC-------LglsdeieRKDITIGDHVF 94
Cdd:cd03353    25 DPGVILEGKTVIGEDCVIGPNCVI----KDSTIGDGVVIKASSVIEGAVIGNGAtvgpfahL-------RPGTVLGEGVH 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1430660611  95 IGSHCVVK----------------GGANIGNYCVIGAGTI 118
Cdd:cd03353    94 IGNFVEIKkstigegskanhlsylGDAEIGEGVNIGAGTI 133
PLN02694 PLN02694
serine O-acetyltransferase
 32-134 1.72e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.09  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  32 KIGKNVVIAGFSEINANHVNVtIGDNCDIASFVSIN-----AADSHKKclglsdeierkditIGDHVFIGSHCVVKGGAN 106
Cdd:PLN02694  168 KIGKGILFDHATGVVIGETAV-IGNNVSILHHVTLGgtgkaCGDRHPK--------------IGDGVLIGAGATILGNVK 232

                          90       100
                  ....*....|....*....|....*...
gi 1430660611 107 IGNYCVIGAGTIVEgVDIPEYSLVIGNP 134
Cdd:PLN02694  233 IGEGAKIGAGSVVL-IDVPPRTTAVGNP 259
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 48-136 3.27e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.31  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  48 NHV----NVTIGDNCDIASFVSInaADShkkclglsdeierkdITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvD 123
Cdd:COG1044   233 NLVqiahNVRIGEHTAIAAQVGI--AGS---------------TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTK-S 294

                          90
                  ....*....|...
gi 1430660611 124 IPEYSLVIGNPMI 136
Cdd:COG1044   295 IPEGGVYSGSPAQ 307
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 22-134 3.55e-05

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.20  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINAN------HVNVTIGDNCDIASFVSINAADSHKKCLGLSDEIErkDITIGDHVFI 95
Cdd:cd04745    10 HPTAVLIGDVIIGKNCYIGPHASLRGDfgriviRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILH--GCTIGRNALV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1430660611  96 GSHCVVKGGANIGNYCVIGAGTIVE-GVDIPEYSLVIGNP 134
Cdd:cd04745    88 GMNAVVMDGAVIGEESIVGAMAFVKaGTVIPPRSLIAGSP 127
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 22-124 3.88e-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: 41.65  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSINaadshkkclglsdeierkditigDHVFIGSHCVV 101
Cdd:cd03351     3 HPTAIVDPGAKIGENVEIGPFCVIGPN---VEIGDGTVIGSHVVID-----------------------GPTTIGKNNRI 56

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1430660611 102 KGGANIGN------------YCVIGAG-TIVEGVDI 124
Cdd:cd03351    57 FPFASIGEapqdlkykgeptRLEIGDNnTIREFVTI 92
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
22-113 4.52e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINAnhvNVTIGDNCDIASFVSINAadshkkclglsdeierkDITIGDHVFIGSHCVV 101
Cdd:PRK05289    6 HPTAIVEPGAKIGENVEIGPFCVIGP---NVVIGDGTVIGSHVVIDG-----------------HTTIGKNNRIFPFASI 65

                          90       100
                  ....*....|....*....|....*
gi 1430660611 102 kGGAN-------------IGNYCVI 113
Cdd:PRK05289   66 -GEDPqdlkykgeptrlvIGDNNTI 89
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 27-134 5.52e-05

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: 41.16  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  27 INGNPKIGKNVVIAGFSEINAN---------HVNVTIGDNCDIASFVSINAADSHKK--------CL------------- 76
Cdd:COG1043    46 IEGPTTIGKNNRIFPFASIGEEpqdlkykgePTRLEIGDNNTIREFVTIHRGTVQGGgvtrigddNLlmayvhvahdcvv 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430660611  77 ----------GLSDEIErkditIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:COG1043   126 gnnvilannaTLAGHVE-----VGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVK-DVPPYVLAAGNP 187
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 27-133 5.81e-05

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 40.77  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  27 INGNPKIGKNVVIAGFSEINANHVNVTIGDNCDIASFVSInaadSHKKclgLSDEIERKDITIGDH-VF----------- 94
Cdd:cd04646    14 IRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTI----VNKK---PKDPAEPKPMIIGSNnVFevgckcealki 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1430660611  95 -----IGSHCVVKGGANIGNYCVIGAGTIV-EGVDIPEYSLVIGN 133
Cdd:cd04646    87 gnnnvFESKSFVGKNVIITDGCIIGAGCKLpSSEILPENTVIYGA 131
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 22-113 6.44e-05

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: 41.16  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGFSEINAnhvNVTIGDNCDIASFVSINAadshkkclglsdeierkDITIGDHVFIGSHCVV 101
Cdd:COG1043     5 HPTAIVDPGAKLGENVEIGPFCVIGP---DVEIGDGTVIGSHVVIEG-----------------PTTIGKNNRIFPFASI 64

                          90       100
                  ....*....|....*....|....*
gi 1430660611 102 kGGAN-------------IGNYCVI 113
Cdd:COG1043    65 -GEEPqdlkykgeptrleIGDNNTI 88
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-144 9.99e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.74  E-value: 9.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1430660611  88 TIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGN-PMIIKKGYYRK 144
Cdd:PRK14359  369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTK-DVPKGSLAISRaPQKNIKNFYYK 425
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 47-131 1.03e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.78  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  47 ANHV----NVTIGDNCDI-ASFVSIN--AADSHKKclglsdeierkdiTIGDHVFIGSHCVVKGGANIGNYCVIGAGTIV 119
Cdd:PRK09451  361 AGHLtylgDAEIGDNVNIgAGTITCNydGANKFKT-------------IIGDDVFVGSDTQLVAPVTVGKGATIGAGTTV 427

                          90
                  ....*....|..
gi 1430660611 120 EGvDIPEYSLVI 131
Cdd:PRK09451  428 TR-DVAENELVI 438
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-118 1.08e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.78  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  25 VWINGNPKIGKNVVIAGFSEINanhvNVTIGDNCDIASFVSINAADSHKKC-LG----------LSDE------IERKDI 87
Cdd:PRK09451  278 VIIEGNVTLGNRVKIGAGCVLK----NCVIGDDCEISPYSVVEDANLGAACtIGpfarlrpgaeLAEGahvgnfVEMKKA 353

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1430660611  88 TIGDhvfiGS---HCVVKGGANIGNYCVIGAGTI 118
Cdd:PRK09451  354 RLGK----GSkagHLTYLGDAEIGDNVNIGAGTI 383
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 51-126 1.33e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 1.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430660611  51 NVTIGDNCDIASFVSInaADShkkclglsdeierkdITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPE 126
Cdd:PRK00892  243 NVVIGRHTAIAAQVGI--AGS---------------TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTK-SIPE 300
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 85-119 1.44e-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: 1.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1430660611  85 KDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIV 119
Cdd:COG1043    30 PDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 30-144 1.47e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.30  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  30 NPKIGKNVVIAGFSEINANhvnVTIGDNCDIASFVSI---------NAA------DSHkkcLGLSDEIERKDIT------ 88
Cdd:PRK14360  313 DSQIGDGVKIGPYAHLRPE---AQIGSNCRIGNFVEIkksqlgegsKVNhlsyigDAT---LGEQVNIGAGTITanydgv 386

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430660611  89 ------IGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEgvDIPEYSLVIGNP-MIIKKGYYRK 144
Cdd:PRK14360  387 kkhrtvIGDRSKTGANSVLVAPITLGEDVTVAAGsTITK--DVPDNSLAIARSrQVIKENWKKK 448
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 88-132 1.72e-04

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 39.71  E-value: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1430660611  88 TIGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEgvDIPEYSLVIG 132
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGsTITK--DVPPGALAIA 189
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 25-114 3.10e-04

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: 39.24  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  25 VWINGNPKIGKNVVIAGFSEInanHVNVTIGDNCDIASFVSInaadshkkclglsdeierKDITIGDHVFIgSHCVVKgG 104
Cdd:COG1207   261 TYIDGDVEIGRDVVIDPNVIL---EGKTVIGEGVVIGPNCTL------------------KDSTIGDGVVI-KYSVIE-D 317

                          90
                  ....*....|
gi 1430660611 105 ANIGNYCVIG 114
Cdd:COG1207   318 AVVGAGATVG 327
PLN02739 PLN02739
serine acetyltransferase
 27-134 3.83e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 39.25  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  27 INGNPKIGKNVVIagfseinaNH-VNVTIGDNCDIASFVSInaadSHKKCLG-LSDEIERKDITIGDHVFIGSHCVVKGG 104
Cdd:PLN02739  208 IHPAARIGKGILL--------DHgTGVVIGETAVIGDRVSI----LHGVTLGgTGKETGDRHPKIGDGALLGACVTILGN 275

                          90       100       110
                  ....*....|....*....|....*....|
gi 1430660611 105 ANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:PLN02739  276 ISIGAGAMVAAGSLVLK-DVPSHSMVAGNP 304
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
86-115 7.78e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1430660611  86 DITIGDHVFIGSHCVVKGGANIGNYCVIGA 115
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 22-121 1.21e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.43  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIA----------GFSEINANHV------NVTIGDNCDIASFVSINAAdshkkclGLSDEIERK 85
Cdd:PRK00892  158 HANVTIYHAVRIGNRVIIHsgavigsdgfGFANDRGGWVkipqlgRVIIGDDVEIGANTTIDRG-------ALDDTVIGE 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  86 D------ITIGDHVFIGSHCV------VKGGANIGNYCVIGAGTIVEG 121
Cdd:PRK00892  231 GvkidnlVQIAHNVVIGRHTAiaaqvgIAGSTKIGRYCMIGGQVGIAG 278
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 25-114 1.32e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 37.01  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  25 VWINGNPKIGKNVVIAGFSEINAnhvNVTIGDNCDIASFVSInaadshkkclglsdeierKDITIGDHVFIGSHCVVKgG 104
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVILEG---KTVIGEDCVIGPNCVI------------------KDSTIGDGVVIKASSVIE-G 67

                          90
                  ....*....|
gi 1430660611 105 ANIGNYCVIG 114
Cdd:cd03353    68 AVIGNGATVG 77
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-144 1.68e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.44  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1430660611  89 IGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEgvDIPEYSLVIGNP-MIIKKGYYRK 144
Cdd:PRK14357  386 IEDGAFIGSNSSLVAPVRIGKGALIGAGsVITE--DVPPYSLALGRArQIVKEGWVLK 441
ligA PRK07956
NAD-dependent DNA ligase LigA; Validated
 80-95 2.35e-03

NAD-dependent DNA ligase LigA; Validated


Pssm-ID: 236137 [Multi-domain]  Cd Length: 665  Bit Score: 37.02  E-value: 2.35e-03
                          10
                  ....*....|....*.
gi 1430660611  80 DEIERKDITIGDHVFI 95
Cdd:PRK07956  361 DEIERKDIRIGDTVVV 376
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 89-131 2.59e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 36.71  E-value: 2.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1430660611  89 IGDHVFIGSHCVVKGGANIGNYCVIGAGTI----------VEGV----DIPEYSLVI 131
Cdd:PRK11830  179 IEDNCFIGARSEVVEGVIVEEGSVLGMGVFlgqstkiydrETGEvhygRVPAGSVVV 235
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-114 3.06e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.44  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  27 INGNPKIGKNVVIAGFSEINanhvNVTIGDNCDIA-SFVSinaadshkkclglsdeierkDITIGDHVFIGSHCVVKGGA 105
Cdd:PRK14360  277 LRGNTVIGSGCRIGPGSLIE----NSQIGENVTVLySVVS--------------------DSQIGDGVKIGPYAHLRPEA 332


                  ....*....
gi 1430660611 106 NIGNYCVIG 114
Cdd:PRK14360  333 QIGSNCRIG 341
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
80-95 3.29e-03

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 36.54  E-value: 3.29e-03
                          10
                  ....*....|....*.
gi 1430660611  80 DEIERKDITIGDHVFI 95
Cdd:COG0272   362 DEIERKDVRIGDTVVV 377
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
80-133 3.84e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 35.23  E-value: 3.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1430660611  80 DEIERKDITIGDHVFIGSHCVVKGG-ANIGNYCVIGAGTIVEGVDipeySLVIGN 133
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPG----GITIGD 52
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 52-131 5.21e-03

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: 35.05  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  52 VTIGDNCDIASFVSINaadshkkclGLSDEIERKDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGV--------- 122
Cdd:cd03350    50 AQIGKNVHLSAGAVIG---------GVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQStpiydretg 120

                          90
                  ....*....|....
gi 1430660611 123 -----DIPEYSLVI 131
Cdd:cd03350   121 eiyygRVPPGSVVV 134
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 22-118 5.45e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 35.87  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  22 HPLVWINGNPKIGKNVVIAGfseinanhvNVTIGDnCDIASFVSINAADShkkclgLSDEIERKDITIG----------- 90
Cdd:PRK14355  278 YPGVCISGDTRIGEGCTIEQ---------GVVIKG-CRIGDDVTVKAGSV------LEDSVVGDDVAIGpmahlrpgtel 341

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1430660611  91 -DHVFIG----------------SHCVVKGGANIGNYCVIGAGTI 118
Cdd:PRK14355  342 sAHVKIGnfvetkkivmgegskaSHLTYLGDATIGRNVNIGCGTI 386
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 89-130 5.92e-03

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: 35.26  E-value: 5.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1430660611  89 IGDHVFIGSHCVVKGGANIGNYCVIGAGT------IVEGVDIPEYSLV 130
Cdd:cd05636    38 IGKGCEIGPNAYIRGYTVLGDGCVVGNSVevknsiIMDGTKVPHLNYV 85
PLN02357 PLN02357
serine acetyltransferase
 25-134 6.79e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 35.63  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  25 VWINGNPKIGKNVVIAGFSEINANHVNVtIGDNCDIASFVSIN-----AADSHKKclglsdeierkditIGDHVFIGSHC 99
Cdd:PLN02357  227 VDIHPGAKIGQGILLDHATGVVIGETAV-VGNNVSILHNVTLGgtgkqSGDRHPK--------------IGDGVLIGAGT 291

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1430660611 100 VVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIGNP 134
Cdd:PLN02357  292 CILGNITIGEGAKIGAGSVVLK-DVPPRTTAVGNP 325
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-144 6.96e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 35.61  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  23 PLVWINGNPKIGKNVVIAGFSEINANHV--NVTIG------------DNCDIASFVSINAAD-------SHKKCLGLSDE 81
Cdd:PRK14353  279 PNVVFGPGVTVASGAVIHAFSHLEGAHVgeGAEVGpyarlrpgaelgEGAKVGNFVEVKNAKlgegakvNHLTYIGDATI 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430660611  82 IERKDI-----------------TIGDHVFIGSHCVVKGGANIGNYCVIGAG-TIVEgvDIPEYSLVIG-NPMIIKKGYY 142
Cdd:PRK14353  359 GAGANIgagtitcnydgfnkhrtEIGAGAFIGSNSALVAPVTIGDGAYIASGsVITE--DVPDDALALGrARQETKPGWA 436


                  ..
gi 1430660611 143 RK 144
Cdd:PRK14353  437 KK 438
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 80-141 9.52e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 35.10  E-value: 9.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430660611  80 DEIERKDITIGDHVFIGSHCVVKGGANIGNYCVIGAGTIVEGvDIPEYSLVIG-NPMIIKKGY 141
Cdd:PRK14355  391 DGVKKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTK-DVPPDSLAIArSPQVNKEGW 452
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 86-119 9.53e-03

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: 33.97  E-value: 9.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1430660611  86 DITIGDHVFIGSHCVV--KGGANIGNYCVIGAGTIV 119
Cdd:cd04647     1 NISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTI 36
 
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