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Conserved domains on  [gi|1704623754|gb|QDM06785.1|]
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serine acetyltransferase [Escherichia coli]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 40-128 4.51e-35

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: 119.03  E-value: 4.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDEDK-YPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:COG1045    80 IDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                          90
                  ....*....|
gi 1704623754 119 VKGSPAVVIR 128
Cdd:COG1045   160 VVGVPARIVK 169
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 40-128 4.51e-35

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: 119.03  E-value: 4.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDEDK-YPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:COG1045    80 IDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                          90
                  ....*....|
gi 1704623754 119 VKGSPAVVIR 128
Cdd:COG1045   160 VVGVPARIVK 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 40-123 1.75e-31

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: 107.53  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNND-EDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:cd03354    17 IDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGgGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANST 96


                  ....*
gi 1704623754 119 VKGSP 123
Cdd:cd03354    97 VVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 36-129 5.23e-20

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 83.55  E-value: 5.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  36 KKTLIPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDE-DKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:PLN02739  216 KGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETgDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVP 295

                          90
                  ....*....|....*
gi 1704623754 115 DNAIVKGSPAVVIRF 129
Cdd:PLN02739  296 SHSMVAGNPAKLIGF 310
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 45-124 3.47e-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: 65.59  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTI--GVRnndedkypvLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGS 122
Cdd:TIGR03570 129 GAIVEHDCVIGDFVHIAPGVTLsgGVV---------IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGV 199


                  ..
gi 1704623754 123 PA 124
Cdd:TIGR03570 200 PA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
77-105 1.32e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 1704623754  77 PVLGDNVIVYANACIIGDVKVGSNVIIGS 105
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 40-128 4.51e-35

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: 119.03  E-value: 4.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDEDK-YPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:COG1045    80 IDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKrHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                          90
                  ....*....|
gi 1704623754 119 VKGSPAVVIR 128
Cdd:COG1045   160 VVGVPARIVK 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 40-123 1.75e-31

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: 107.53  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNND-EDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:cd03354    17 IDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGgGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANST 96


                  ....*
gi 1704623754 119 VKGSP 123
Cdd:cd03354    97 VVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 36-129 5.23e-20

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 83.55  E-value: 5.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  36 KKTLIPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDE-DKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:PLN02739  216 KGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETgDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVP 295

                          90
                  ....*....|....*
gi 1704623754 115 DNAIVKGSPAVVIRF 129
Cdd:PLN02739  296 SHSMVAGNPAKLIGF 310
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
38-128 8.21e-19

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 76.45  E-value: 8.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  38 TLIPHPVGIVIGKNVVLGNRCTIYqNVTIGVRNNDEDKYP----VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDI 113
Cdd:COG0110    40 VTIDDPGGITIGDNVLIGPGVTIL-TGNHPIDDPATFPLRtgpvTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDV 118

                          90
                  ....*....|....*
gi 1704623754 114 PDNAIVKGSPAVVIR 128
Cdd:COG0110   119 PPYAIVAGNPARVIR 133
PRK10191 PRK10191
putative acyl transferase; Provisional
 40-126 2.78e-18

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 75.31  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  40 IPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:PRK10191   56 IHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALV 135


                  ....*..
gi 1704623754 120 KGSPAVV 126
Cdd:PRK10191  136 VGEKARV 142
PLN02357 PLN02357
serine acetyltransferase
 39-127 1.65e-17

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 76.84  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  39 LIPHPVGIVIGKNVVLGNRCTIYQNVTIG-VRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNA 117
Cdd:PLN02357  240 LLDHATGVVIGETAVVGNNVSILHNVTLGgTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRT 319

                          90
                  ....*....|
gi 1704623754 118 IVKGSPAVVI 127
Cdd:PLN02357  320 TAVGNPARLI 329
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 45-127 1.87e-17

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: 72.10  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTI------YQNVTIGVRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:cd04647    21 GITIGDNVLIGPNVTIydhnhdIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSI 100


                  ....*....
gi 1704623754 119 VKGSPAVVI 127
Cdd:cd04647   101 VAGNPAKVI 109
PLN02694 PLN02694
serine O-acetyltransferase
 36-127 3.71e-17

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 75.06  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  36 KKTLIPHPVGIVIGKNVVLGNRCTIYQNVTIG-VRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:PLN02694  171 KGILFDHATGVVIGETAVIGNNVSILHHVTLGgTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVP 250

                          90
                  ....*....|...
gi 1704623754 115 DNAIVKGSPAVVI 127
Cdd:PLN02694  251 PRTTAVGNPARLV 263
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 46-127 9.92e-17

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: 71.68  E-value: 9.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  46 IVIGKNVVLGNRCTIYQN---VTIGVRNND-EDKYPV-LGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVK 120
Cdd:cd03357    83 VTIGDNVLIGPNVQIYTAghpLDPEERNRGlEYAKPItIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAA 162


                  ....*..
gi 1704623754 121 GSPAVVI 127
Cdd:cd03357   163 GNPARVI 169
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 45-124 3.47e-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: 65.59  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTI--GVRnndedkypvLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGS 122
Cdd:TIGR03570 129 GAIVEHDCVIGDFVHIAPGVTLsgGVV---------IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGV 199


                  ..
gi 1704623754 123 PA 124
Cdd:TIGR03570 200 PA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 45-123 2.49e-12

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: 60.58  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTI--GVRnndedkypvLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGS 122
Cdd:cd03360   126 GAVIGHDCVIGDFVHIAPGVVLsgGVT---------IGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGN 196


                  .
gi 1704623754 123 P 123
Cdd:cd03360   197 P 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 45-128 3.69e-12

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: 58.67  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTI------YQNVTIG--------------------VRNNDEDKYPVLGDNVIVYANACIIGDVKVG 98
Cdd:cd03358    10 NVFIENDVKIGDNVKIqsnvsiYEGVTIEddvfigpnvvftndlyprskIYRKWELKGTTVKRGASIGANATILPGVTIG 89

                          90       100       110
                  ....*....|....*....|....*....|
gi 1704623754  99 SNVIIGSGSLVNKDIPDNAIVKGSPAVVIR 128
Cdd:cd03358    90 EYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 47-107 7.39e-11

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: 57.72  E-value: 7.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIGvrnndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGS 107
Cdd:COG1044   122 VIGAGVVIGDGVVIGPGVVIG-------DGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGA 175
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 46-128 8.30e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 56.94  E-value: 8.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  46 IVIGKNVVLGNRCTIYQNVTIGV----------RNNDEDKYPV-LGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:PRK09527   90 IVDDYTVTIGDNVLIAPNVTLSVtghpvhhelrKNGEMYSFPItIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIP 169

                          90
                  ....*....|....
gi 1704623754 115 DNAIVKGSPAVVIR 128
Cdd:PRK09527  170 PNVVAAGVPCRVIR 183
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 42-128 9.29e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.19  E-value: 9.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  42 HPVGIVIGkNVVLGNRCTIYQNV---------TIGVRNNDED--------KYPV-LGDNVIVYANA----CIIGD----- 94
Cdd:COG0663    20 APTAVVIG-DVTIGEDVSVWPGAvlrgdvgpiRIGEGSNIQDgvvlhvdpGYPLtIGDDVTIGHGAilhgCTIGDnvlig 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1704623754  95 --------VKVGSNVIIGSGSLV--NKDIPDNAIVKGSPAVVIR 128
Cdd:COG0663    99 mgaivldgAVIGDGSIVGAGALVteGKVVPPGSLVVGSPAKVVR 142
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 47-128 2.36e-10

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: 54.73  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  47 VIGkNVVLGNRCTI---------YQNVTIGVRNNDED--------KYPV-LGDNVIVYANA----CIIGD---------- 94
Cdd:cd04645    14 VIG-DVTLGEGSSVwfgavlrgdVNPIRIGERTNIQDgsvlhvdpGYPTiIGDNVTVGHGAvlhgCTIGDncligmgaii 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1704623754  95 ---VKVGSNVIIGSGSLV--NKDIPDNAIVKGSPAVVIR 128
Cdd:cd04645    93 ldgAVIGKGSIVAAGSLVppGKVIPPGSLVAGSPAKVVR 131
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 38-129 5.48e-10

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: 53.70  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  38 TLIPHPVGIVIGKNVVLGNRCTIYQNVTIGVRNN----------------------DEDKYP-----VLGDNVIVYANAC 90
Cdd:cd03349     8 SYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGNhptdwvstypfyifggeweddaKFDDWPskgdvIIGNDVWIGHGAT 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1704623754  91 IIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGSPAVVIRF 129
Cdd:cd03349    88 ILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 48-128 6.86e-10

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 54.34  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  48 IGKNVVLGNRCTIYQNVTIGvrnndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGSPAVVI 127
Cdd:cd03352   129 IAHNVRIGENCLIAAQVGIA-------GSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPH 201


                  .
gi 1704623754 128 R 128
Cdd:cd03352   202 R 202
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 47-125 7.63e-10

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.02  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIGvRNNdedkypV------------LGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:COG1044   224 VIGDGTKIDNLVQIAHNVRIG-EHT------AiaaqvgiagstkIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIP 296

                          90
                  ....*....|.
gi 1704623754 115 DNAIVKGSPAV 125
Cdd:COG1044   297 EGGVYSGSPAQ 307
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 46-128 9.33e-10

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 53.66  E-value: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  46 IVIGKNVVLGNRCTIY---QNVTIGVRNND-EDKYPV-LGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVK 120
Cdd:PRK10092   94 IRIGDNCMLAPGVHIYtatHPLDPVARNSGaELGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVG 173


                  ....*...
gi 1704623754 121 GSPAVVIR 128
Cdd:PRK10092  174 GNPARIIK 181
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 52-127 1.30e-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: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  52 VVLGNRCTIYQNVTI--GVRNNDEDKYP------VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGSP 123
Cdd:cd05825    24 VTIGSDACISQGAYLctGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNP 103


                  ....
gi 1704623754 124 AVVI 127
Cdd:cd05825   104 AVPV 107
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 47-107 1.75e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 1.75e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIGvrnndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGS 107
Cdd:PRK00892  126 VIGAGVVIGDGVVIGAGAVIG-------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSGA 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 47-109 2.41e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 52.80  E-value: 2.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIGvrnndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLV 109
Cdd:cd03352    15 VIGEGVVIGDGVVIGPGVVIG-------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 78-129 1.23e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 50.64  E-value: 1.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGSPAVVIRF 129
Cdd:PRK09677  132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
PRK10502 PRK10502
putative acyl transferase; Provisional
 46-128 6.47e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 48.79  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  46 IVIGKNVVLGNRCTI------YQNVTIGVRNndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:PRK10502   92 ITIGAHCVISQKSYLctgshdYSDPHFDLNT----APIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTIC 167


                  ....*....
gi 1704623754 120 KGSPAVVIR 128
Cdd:PRK10502  168 RGNPAVPIR 176
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 45-107 6.93e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTI--GVRnndedkypvLGDNVIVYANACI-------------------IGDVKVGSNVII 103
Cdd:PRK00892  142 GAVIGDGVKIGADCRLHANVTIyhAVR---------IGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGDDVEI 212


                  ....
gi 1704623754 104 GSGS 107
Cdd:PRK00892  213 GANT 216
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 42-128 1.09e-07

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: 47.56  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  42 HPVGIVIGkNVVLGNRCTIY---------QNVTIGVRNNDEDK--------YPV------------------LGDNVIVY 86
Cdd:cd04650    10 HPTSYVIG-DVVIGELTSVWhyavirgdnDSIYIGKYSNVQENvsihtdhgYPTeigdyvtighnavvhgakVGNYVIVG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1704623754  87 ANACIIGDVKVGSNVIIGSGSLV--NKDIPDNAIVKGSPAVVIR 128
Cdd:cd04650    89 MGAILLNGAKIGDHVIIGAGAVVtpGKEIPDYSLVLGVPAKVVR 132
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
48-126 7.75e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.24  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  48 IGKNVVLGNRCTIYQNVTIG--VrnndedkypVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKGSPAV 125
Cdd:PRK05289  120 VAHDCVVGNHVILANNATLAghV---------EVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPAR 190


                  .
gi 1704623754 126 V 126
Cdd:PRK05289  191 L 191
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 41-106 8.55e-07

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: 8.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  41 PHPVGI----VIGKNVVLGNRCTIYQNVTIGvrnndedKYPVLGDNVIVYANACIIGDVKVGSNVIIGSG 106
Cdd:COG1044    94 APAPGIhpsaVIDPSAKIGEGVSIGPFAVIG-------AGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPN 156
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 47-125 9.42e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIGvrnndedKYPV------------LGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIP 114
Cdd:PRK00892  227 VIGEGVKIDNLVQIAHNVVIG-------RHTAiaaqvgiagstkIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIP 299

                          90
                  ....*....|..
gi 1704623754 115 D-NAIVKGSPAV 125
Cdd:PRK00892  300 EpGEYSSGIPAQ 311
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 45-107 1.11e-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: 45.48  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTIGVRNndedkypVLGDNVIVYANACI-------------------IGDVKVGSNVIIGS 105
Cdd:cd03352    31 GVVIGDGVVIGDDCVIHPNVTIYEGC-------IIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVIIGDDVEIGA 103


                  ..
gi 1704623754 106 GS 107
Cdd:cd03352   104 NT 105
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 45-110 2.86e-06

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: 42.24  E-value: 2.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704623754  45 GIVIGKNVVLGNRCTIYQNVTIG-VRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVN 110
Cdd:cd00208    12 KAVIRGPVVIGDNVNIGPGAVIGaATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 59-119 6.04e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 43.76  E-value: 6.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704623754  59 TIYQNVTIG----VRNND-EDKYP-VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:PRK14360  367 TLGEQVNIGagtiTANYDgVKKHRtVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLA 433
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 47-118 6.84e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.98  E-value: 6.84e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704623754  47 VIGKNVVLGNRctiyqnvTIGVRNNDEDKYP-VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:PRK14357  360 TVGKNVNIGAG-------TITCNYDGKKKNPtFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSL 425
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 78-119 6.91e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.18  E-value: 6.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-121 1.19e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.93  E-value: 1.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIVKG 121
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 52-126 2.06e-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: 42.31  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  52 VVLGNRCTIYQNVTIGvRNNDEDKYP-------------------VLGDNVIVyANA------CIIGD------------ 94
Cdd:COG1043    80 LEIGDNNTIREFVTIH-RGTVQGGGVtrigddnllmayvhvahdcVVGNNVIL-ANNatlaghVEVGDhaiigglsavhq 157

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1704623754  95 -VKVGSNVIIGSGSLVNKDIPDNAIVKGSPAVV 126
Cdd:COG1043   158 fVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 47-106 2.60e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 2.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  47 VIGKNVVLGNRCTIYQNVTIgvrnndedkypvlGDNVIVYANaCIIGD-VKVGSNVIIGSG 106
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVI-------------GDGVVIGAG-AVIGDgVKIGADCRLHAN 160
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 58-119 1.14e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.36  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704623754  58 CTIYQNVTIGVR----NND-EDKYP-VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:PRK14359  343 CEIDEGTNIGAGtitcNYDgKKKHKtIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLA 410
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 79-128 1.27e-04

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: 39.27  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704623754  79 LGDNVIVYANACIIGDVKVGSNVIIGSGSLV--NKDIPDNAIVKGSPAVVIR 128
Cdd:cd04745    81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVkaGTVIPPRSLIAGSPAKVIR 132
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 52-126 1.83e-04

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: 39.34  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  52 VVLGNRCTIYQNVTIGvRNNDEDKYP-------------------VLGDNVIVYANACIIGDVKVGSNVIIGS------- 105
Cdd:cd03351    78 LEIGDNNTIREFVTIH-RGTAQGGGVtrignnnllmayvhvahdcVIGNNVILANNATLAGHVEIGDYAIIGGlsavhqf 156

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1704623754 106 -----------GSLVNKDIPDNAIVKGSPAVV 126
Cdd:cd03351   157 crigrhamvggGSGVVQDVPPYVIAAGNRARL 188
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 48-118 1.83e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.73  E-value: 1.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704623754  48 IGKNVVLGnrC-TIYQNVTiGVRNNDEdkypVLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:PRK14355  375 IGRNVNIG--CgTITCNYD-GVKKHRT----VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSL 439
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 48-118 2.27e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.43  E-value: 2.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704623754  48 IGKNVVLGnrCTiyqnvTIGVRNNDEDKYP-VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAI 118
Cdd:PRK14354  371 VGENVNIG--CG-----TITVNYDGKNKFKtIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-119 2.52e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 39.24  E-value: 2.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDNAIV 119
Cdd:PRK09451  396 IIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 50-119 2.54e-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: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  50 KNVVLGNR-----------CTIYQNVTIG----VRNND-EDKYP-VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKD 112
Cdd:COG1207   351 KNSTIGEGskvnhlsyigdAEIGEGVNIGagtiTCNYDgVNKHRtVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKD 430


                  ....*..
gi 1704623754 113 IPDNAIV 119
Cdd:COG1207   431 VPAGALA 437
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 51-106 2.84e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.54  E-value: 2.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704623754  51 NVVLGNRCTIYQNVTIGVRNndedkypVLGDNVIVYANACIIGDVKVGSNVIIGSG 106
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGV-------VIGDGVVIGPGVVIGDGVVIGDDCVIHPN 49
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 52-125 3.51e-04

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 38.78  E-value: 3.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704623754  52 VVLGNRCTIYQNVTIGVRNNDEDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSGSLV--NKDIPDNAIVKGSPAV 125
Cdd:TIGR01852  77 LIIGDNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLagHVEVGDYAIIGGLVAV 152
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 78-129 4.65e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 4.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKD--IPDNAIVKgsPAVVIRF 129
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGvkIGADCRLH--ANVTIYH 165
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 78-122 5.13e-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: 38.47  E-value: 5.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGS-LVNKDIPDNAIVKGS 122
Cdd:COG1207   268 EIGRDVVIDPNVILEGKTVIGEGVVIGPNCtLKDSTIGDGVVIKYS 313
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 43-119 5.50e-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: 37.78  E-value: 5.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704623754  43 PVGIVIGKNVVLGNRCTIYQNVTIGVRNndedkypVLGDNVIVYANaCIIGDVKVGSNVIIGSGSLV-NKDIPDNAIV 119
Cdd:cd03353     7 PETTYIDGDVEIGVDVVIDPGVILEGKT-------VIGEDCVIGPN-CVIKDSTIGDGVVIKASSVIeGAVIGNGATV 76
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-121 7.19e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.17  E-value: 7.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKDIPDN--AIVKG 121
Cdd:PRK14356  400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGslAIARG 445
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 44-104 1.22e-03

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: 37.31  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  44 VGIVIGKNVVLGNRCTIYQNVTIgvRNNdedkypVLGDNVIVyaNACIIGDVKVGSNVIIG 104
Cdd:COG1207   277 PNVILEGKTVIGEGVVIGPNCTL--KDS------TIGDGVVI--KYSVIEDAVVGAGATVG 327
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-104 1.30e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704623754  36 KKTLIpHPvGIVIGKNVVLGNRCTIYQNVTIgvrnndedKYPVLGDNVIVYANAcIIGDVKVGSNVIIG 104
Cdd:PRK14355  273 RDTTI-YP-GVCISGDTRIGEGCTIEQGVVI--------KGCRIGDDVTVKAGS-VLEDSVVGDDVAIG 330
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
77-105 1.32e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 1704623754  77 PVLGDNVIVYANACIIGDVKVGSNVIIGS 105
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PLN02296 PLN02296
carbonate dehydratase
 74-119 1.39e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.03  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  74 DKYPVLGDNVIVYANACIIGDVKVG---------------SNVIIGSGSlvnkDIPDNAIV 119
Cdd:PLN02296   50 DKAPVVDKDAFVAPSASVIGDVQVGrgssiwygcvlrgdvNSISVGSGT----NIQDNSLV 106
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 42-107 1.85e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 36.53  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704623754  42 HPVGIV-----IGKNVVLGNRCTIYQNVTIgvrnndedkypvlGDNVIVYANACIIGDVKVGSNVIIGSGS 107
Cdd:COG1043     5 HPTAIVdpgakLGENVEIGPFCVIGPDVEI-------------GDGTVIGSHVVIEGPTTIGKNNRIFPFA 62
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 27-126 1.93e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.54  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704623754  27 TVGIKYLFLKKTLIPHPVgiVIGKNVVLGNRCTIYQNVTIgvrnndedkypvlGDNVIVYANACIIGDVKVGSNVIIGSG 106
Cdd:PRK12461  103 RIGNDNLLMAYSHVAHDC--QIGNNVILVNGALLAGHVTV-------------GDRAIISGNCLVHQFCRIGALAMMAGG 167

                          90       100
                  ....*....|....*....|
gi 1704623754 107 SLVNKDIPDNAIVKGSPAVV 126
Cdd:PRK12461  168 SRISKDVPPYCMMAGHPTNV 187
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 78-128 2.08e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.53  E-value: 2.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGSLVNKD--IPDNAIVKgsPAVVIR 128
Cdd:COG1044   110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGvvIGDDCVLH--PNVTIY 160
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 80-127 2.67e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 36.16  E-value: 2.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1704623754  80 GDNVIVYANACIIGDVKVGSNVIIGSGS-LVNKDIPDNAIVkgSPAVVI 127
Cdd:PRK09451  269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCvLKNCVIGDDCEI--SPYSVV 315
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-122 3.67e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 35.96  E-value: 3.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGS-LVNKDIPDNAIVKGS 122
Cdd:PRK14354  267 EIGSDTVIEPGVVIKGNTVIGEDCVIGPGSrIVDSTIGDGVTITNS 312
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 50-110 5.35e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 33.71  E-value: 5.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704623754  50 KNVVLGNRCTIYQNVTIgvrnndEDKYpvLGDNVIVYANA----CIIGD-VKVGSNVIIGSGSLVN 110
Cdd:cd05787    15 KNSVIGRNCKIGKNVVI------DNSY--IWDDVTIEDGCtihhSIVADgAVIGKGCTIPPGSLIS 72
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 78-122 7.24e-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: 34.70  E-value: 7.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1704623754  78 VLGDNVIVYANACIIGDVKVGSNVIIGSGS-LVNKDIPDNAIVKGS 122
Cdd:cd03353    17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCvIKDSTIGDGVVIKAS 62
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 73-106 7.99e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 34.23  E-value: 7.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1704623754  73 EDKYPVLGDNVIVYANACIIGDVKVGSNVIIGSG 106
Cdd:COG0663     7 DGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPG 40
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 46-120 9.06e-03

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: 34.11  E-value: 9.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704623754  46 IVIGKNVVLGNRCTIYQNVTIgvRNNDEDKYPVL-GDNVIVYANaCIIGDVKVGSNVIIGSGSLVNK--DIPDNAIVK 120
Cdd:cd03359    43 VSIGRYCILSEGCVIRPPFKK--FSKGVAFFPLHiGDYVFIGEN-CVVNAAQIGSYVHIGKNCVIGRrcIIKDCVKIL 117
 
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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