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Conserved domains on  [gi|1186663102|ref|WP_085448390|]
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MULTISPECIES: serine O-acetyltransferase [Enterobacteriaceae]

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 ...
 62-155 5.03e-32

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: 112.10  E-value: 5.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSK-LEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:COG1045    76 RGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVP 155

                          90
                  ....*....|....*
gi 1186663102 141 DNCIAIGNPAKIIPK 155
Cdd:COG1045   156 PGSTVVGVPARIVKR 170
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 62-155 5.03e-32

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: 112.10  E-value: 5.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSK-LEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:COG1045    76 RGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVP 155

                          90
                  ....*....|....*
gi 1186663102 141 DNCIAIGNPAKIIPK 155
Cdd:COG1045   156 PGSTVVGVPARIVKR 170
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 62-149 1.54e-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: 108.68  E-value: 1.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSK-LEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:cd03354    13 PGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKgKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVP 92


                  ....*....
gi 1186663102 141 DNCIAIGNP 149
Cdd:cd03354    93 ANSTVVGVP 101
PRK10191 PRK10191
putative acyl transferase; Provisional
 62-152 9.56e-18

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 74.93  E-value: 9.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPD 141
Cdd:PRK10191   52 RRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPD 131

                          90
                  ....*....|.
gi 1186663102 142 NCIAIGNPAKI 152
Cdd:PRK10191  132 NALVVGEKARV 142
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 71-150 2.14e-13

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: 64.44  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTI--GSKLEDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGN 148
Cdd:TIGR03570 123 NVIINTGAIVEHDCVIGDFVHIapGVTLSGGV---VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGV 199


                  ..
gi 1186663102 149 PA 150
Cdd:TIGR03570 200 PA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
103-131 4.84e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.47  E-value: 4.84e-05
                          10        20
                  ....*....|....*....|....*....
gi 1186663102 103 PKLGDNVTIYANSVIVGGVSVGNNVTIGA 131
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 62-155 5.03e-32

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: 112.10  E-value: 5.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSK-LEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:COG1045    76 RGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVP 155

                          90
                  ....*....|....*
gi 1186663102 141 DNCIAIGNPAKIIPK 155
Cdd:COG1045   156 PGSTVVGVPARIVKR 170
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 62-149 1.54e-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: 108.68  E-value: 1.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSK-LEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:cd03354    13 PGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKgKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVP 92


                  ....*....
gi 1186663102 141 DNCIAIGNP 149
Cdd:cd03354    93 ANSTVVGVP 101
PRK10191 PRK10191
putative acyl transferase; Provisional
 62-152 9.56e-18

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 74.93  E-value: 9.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPD 141
Cdd:PRK10191   52 RRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPD 131

                          90
                  ....*....|.
gi 1186663102 142 NCIAIGNPAKI 152
Cdd:PRK10191  132 NALVVGEKARV 142
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
24-156 1.03e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 74.52  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  24 FISLFITIGK--YIYCIIFFNDGRMAL--YCDLTVGlkelktkrTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSKLEDG 99
Cdd:COG0110     4 LLLFGARIGDgvVIGPGVRIYGGNITIgdNVYIGPG--------VTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102 100 VSYPK---LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKIIPKI 156
Cdd:COG0110    76 PLRTGpvtIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 71-153 4.80e-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: 71.72  E-value: 4.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIY---QCVTIGSKLEDGVSYPK---LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCI 144
Cdd:cd04647    21 GITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSApivIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSI 100


                  ....*....
gi 1186663102 145 AIGNPAKII 153
Cdd:cd04647   101 VAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 72-153 6.01e-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: 73.23  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  72 VVIGKGVQLGYDCKIYqcvTIG---------SKLEDGvsYP-KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPD 141
Cdd:cd03357    83 VTIGDNVLIGPNVQIY---TAGhpldpeernRGLEYA--KPiTIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPA 157

                          90
                  ....*....|..
gi 1186663102 142 NCIAIGNPAKII 153
Cdd:cd03357   158 NVVAAGNPARVI 169
PLN02357 PLN02357
serine acetyltransferase
 65-153 7.06e-16

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 72.99  E-value: 7.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  65 ILPHPIGVVIGKGVQLGYDCKIYQCVTIG-SKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNC 143
Cdd:PLN02357  240 LLDHATGVVIGETAVVGNNVSILHNVTLGgTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRT 319

                          90
                  ....*....|
gi 1186663102 144 IAIGNPAKII 153
Cdd:PLN02357  320 TAVGNPARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 62-153 2.24e-15

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 71.21  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIG-SKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:PLN02694  171 KGILFDHATGVVIGETAVIGNNVSILHHVTLGgTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVP 250

                          90
                  ....*....|...
gi 1186663102 141 DNCIAIGNPAKII 153
Cdd:PLN02694  251 PRTTAVGNPARLV 263
PLN02739 PLN02739
serine acetyltransferase
 62-153 6.79e-15

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 70.45  E-value: 6.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  62 KRTILPHPIGVVIGKGVQLGYDCKIYQCVTIG-SKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:PLN02739  216 KGILLDHGTGVVIGETAVIGDRVSILHGVTLGgTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVP 295

                          90
                  ....*....|...
gi 1186663102 141 DNCIAIGNPAKII 153
Cdd:PLN02739  296 SHSMVAGNPAKLI 308
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 71-149 2.83e-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: 66.74  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTI--GSKLEDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGN 148
Cdd:cd03360   120 NVIINTGAVIGHDCVIGDFVHIapGVVLSGGV---TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGN 196


                  .
gi 1186663102 149 P 149
Cdd:cd03360   197 P 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 71-150 2.14e-13

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: 64.44  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTI--GSKLEDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGN 148
Cdd:TIGR03570 123 NVIINTGAIVEHDCVIGDFVHIapGVTLSGGV---VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGV 199


                  ..
gi 1186663102 149 PA 150
Cdd:TIGR03570 200 PA 201
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 71-154 6.86e-13

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: 61.36  E-value: 6.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTI------GSKLEDGVSY--PKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDN 142
Cdd:cd03358    28 NVSIYEGVTIEDDVFIGPNVVFtndlypRSKIYRKWELkgTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPY 107

                          90
                  ....*....|..
gi 1186663102 143 CIAIGNPAKIIP 154
Cdd:cd03358   108 ALVVGNPARIIG 119
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 71-135 1.11e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGSKLedgvsypKLGDNVTIYANSVI-------------------VGGVSVGNNVTIGA 131
Cdd:PRK00892  142 GAVIGDGVKIGADCRLHANVTIYHAV-------RIGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGDDVEIGA 214


                  ....
gi 1186663102 132 STLI 135
Cdd:PRK00892  215 NTTI 218
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 105-156 1.28e-11

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 59.44  E-value: 1.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1186663102 105 LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKIIPKI 156
Cdd:PRK10092  132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
cysE PRK11132
serine acetyltransferase; Provisional
 65-155 2.26e-11

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 60.10  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  65 ILPHPIGVVIGKGVQLGYDCKIYQCVTIG-SKLEDGVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNC 143
Cdd:PRK11132  155 MLDHATGIVIGETAVIENDVSILQSVTLGgTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHT 234

                          90
                  ....*....|..
gi 1186663102 144 IAIGNPAKIIPK 155
Cdd:PRK11132  235 TAAGVPARIVGK 246
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-153 1.17e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 58.40  E-value: 1.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1186663102  98 DGVS-YP-KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKII 153
Cdd:PRK14360  384 DGVKkHRtVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVI 441
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 71-135 1.97e-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: 57.33  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVI--------------------VGGVSVGNNVTIG 130
Cdd:COG1044   138 GVVIGDGVVIGDDCVLHPNVTIY----ERC---VIGDRVIIHSGAVIgadgfgfapdedggwvkipqLGRVVIGDDVEIG 210


                  ....*
gi 1186663102 131 ASTLI 135
Cdd:COG1044   211 ANTTI 215
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 71-135 3.49e-10

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 56.95  E-value: 3.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLI 135
Cdd:COG1044   120 FAVIGAGVVIGDGVVIGPGVVIG----DGV---VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 101-156 4.98e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 55.39  E-value: 4.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1186663102 101 SYP-KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKIIPKI 156
Cdd:PRK09527  129 SFPiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREI 185
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 71-135 6.44e-10

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 55.11  E-value: 6.44e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLI 135
Cdd:cd03352    13 NAVIGEGVVIGDGVVIGPGVVIG----DGV---VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 104-155 6.74e-10

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 54.88  E-value: 6.74e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1186663102 104 KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKIIPK 155
Cdd:PRK09677  132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 71-135 7.95e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.92  E-value: 7.95e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLI 135
Cdd:PRK00892  124 NAVIGAGVVIGDGVVIGAGAVIG----DGV---KIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 72-151 1.16e-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: 54.34  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  72 VVIGKGVQLGYDCKIYQCVTI-GSKledgvsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPA 150
Cdd:cd03352   127 VQIAHNVRIGENCLIAAQVGIaGST--------TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPA 198


                  .
gi 1186663102 151 K 151
Cdd:cd03352   199 Q 199
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 71-135 2.24e-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: 53.57  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVI-------------------VGGVSVGNNVTIGA 131
Cdd:cd03352    31 GVVIGDGVVIGDDCVIHPNVTIY----EGC---IIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVIIGDDVEIGA 103


                  ....
gi 1186663102 132 STLI 135
Cdd:cd03352   104 NTTI 107
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 72-151 1.31e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 52.33  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  72 VVIGKGVQLGYDCKIYQCVTI-GSKledgvsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPA 150
Cdd:COG1044   235 VQIAHNVRIGEHTAIAAQVGIaGST--------KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPA 306


                  .
gi 1186663102 151 K 151
Cdd:COG1044   307 Q 307
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 72-142 2.76e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.29  E-value: 2.76e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186663102  72 VVIGKGVQLGYDCKIYQCVTI-GSKledgvsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDN 142
Cdd:PRK00892  238 VQIAHNVVIGRHTAIAAQVGIaGST--------KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEP 301
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 68-144 3.78e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.91  E-value: 3.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186663102  68 HPiGVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKD--IPDNCI 144
Cdd:PRK00892  104 HP-SAVIDPSAKIGEGVSIGPNAVIG----AGV---VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAvrIGNRVI 174
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 68-144 4.75e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 50.79  E-value: 4.75e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186663102  68 HPiGVVIGKGVQLGYDCKIYQCVTIGskleDGVsypKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKD--IPDNCI 144
Cdd:COG1044   100 HP-SAVIDPSAKIGEGVSIGPFAVIG----AGV---VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERcvIGDRVI 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 68-156 5.85e-08

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: 48.95  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  68 HPIGVVIGKGVQLGYDCKIYQCvTIGskledgvsypklgDNVTIYANSVIVGGVSVGNNVTIGASTLIL--KDIPDNCIA 145
Cdd:cd04645    57 PGYPTIIGDNVTVGHGAVLHGC-TIG-------------DNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLV 122

                          90
                  ....*....|.
gi 1186663102 146 IGNPAKIIPKI 156
Cdd:cd04645   123 AGSPAKVVREL 133
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 68-156 7.83e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 48.87  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  68 HPIGVVIGKgVQLGYDCKI-YQCV--------TIG--SKLEDGV------SYP-KLGDNVTIYANSVIVG---------- 119
Cdd:COG0663    20 APTAVVIGD-VTIGEDVSVwPGAVlrgdvgpiRIGegSNIQDGVvlhvdpGYPlTIGDDVTIGHGAILHGctigdnvlig 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1186663102 120 -------GVSVGNNVTIGASTLIL--KDIPDNCIAIGNPAKIIPKI 156
Cdd:COG0663    99 mgaivldGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 106-153 1.92e-07

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: 47.54  E-value: 1.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1186663102 106 GDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKII 153
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 81-156 1.93e-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: 1.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186663102  81 GYDCKIYQCVTIGSKLEdgVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLIL--KDIPDNCIAIGNPAKIIPKI 156
Cdd:cd04650    59 GYPTEIGDYVTIGHNAV--VHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 104-147 2.02e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.19  E-value: 2.02e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1186663102 104 KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIG 147
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 105-153 3.39e-07

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 46.06  E-value: 3.39e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1186663102 105 LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKII 153
Cdd:cd05825    59 IGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 71-136 8.09e-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: 44.16  E-value: 8.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGSKLEDGVSYP-KLGDNVTIYANSVIVGGVSVGNNVTIGASTLIL 136
Cdd:cd00208    12 KAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPtIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 106-147 1.64e-06

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: 46.17  E-value: 1.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1186663102 106 GDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIG 147
Cdd:COG1207   398 GDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIA 439
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 71-135 3.22e-06

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 45.11  E-value: 3.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186663102  71 GVVIGKGVQLGydckiyQCVTIGSKLEDGVSYP-KLGDNVTIYANSVIVGGVSVGNN------VTIGASTLI 135
Cdd:COG2171   144 CAQIGKNVHLS------GGAGIGGVLEPLQAAPvIIEDNCFIGARSGVVEGVIVGEGavlgagVYLTASTKI 209
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-147 3.33e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.49  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  73 VIGKGVQ---LGY--DCKIYQCVTIGSKL----EDGVSYPK--LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPD 141
Cdd:PRK14356  358 VLGKGAKanhLTYlgDAEIGAGANIGAGTitcnYDGVNKHRtvIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPD 437


                  ....*.
gi 1186663102 142 NCIAIG 147
Cdd:PRK14356  438 GSLAIA 443
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 70-150 4.52e-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: 45.13  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  70 IGVVIGKGVQL-GYDCKIYQCVTIGSK-------------LEDGV---SYPKLGDNVTIYANSVIVGGVSVGNNVTIGAS 132
Cdd:TIGR02353 596 LGVKIGRGVYIdGTDLTERDLVTIGDDstlnegsviqthlFEDRVmksDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPD 675

                          90       100
                  ....*....|....*....|
gi 1186663102 133 TLILK--DIPDNCIAIGNPA 150
Cdd:TIGR02353 676 SLVMKgeEVPAHTRWRGNPA 695
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-142 6.60e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.63  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  74 IGKGVQLGY-----DCKIYQCVTIGSKL----EDGVSYPK--LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDN 142
Cdd:PRK09451  355 LGKGSKAGHltylgDAEIGDNVNIGAGTitcnYDGANKFKtiIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAEN 434
PRK10502 PRK10502
putative acyl transferase; Provisional
 105-153 1.76e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 42.63  E-value: 1.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1186663102 105 LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKII 153
Cdd:PRK10502  127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 72-152 4.09e-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: 41.93  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  72 VVIGKgvqlgyDCKIYQCVTI--GSKLEDGV----------SYP------KLGDNVTIyANSVIVGG-VSVGNNVTIGAS 132
Cdd:COG1043    80 LEIGD------NNTIREFVTIhrGTVQGGGVtrigddnllmAYVhvahdcVVGNNVIL-ANNATLAGhVEVGDHAIIGGL 152

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1186663102 133 TLI------------------LKDIPDNCIAIGNPAKI 152
Cdd:COG1043   153 SAVhqfvrigahamvgggsgvVKDVPPYVLAAGNPARL 190
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
72-152 4.38e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  72 VVIGKgvqlgyDCKIYQCVTI--GSKLEDGVSypKLGDNV-----------------TIYANSVIVGG-VSVGNNVTIGA 131
Cdd:PRK05289   81 LVIGD------NNTIREFVTInrGTVQGGGVT--RIGDNNllmayvhvahdcvvgnhVILANNATLAGhVEVGDYAIIGG 152

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1186663102 132 STLI------------------LKDIPDNCIAIGNPAKI 152
Cdd:PRK05289  153 LTAVhqfvrigahamvggmsgvSQDVPPYVLAEGNPARL 191
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
103-131 4.84e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.47  E-value: 4.84e-05
                          10        20
                  ....*....|....*....|....*....
gi 1186663102 103 PKLGDNVTIYANSVIVGGVSVGNNVTIGA 131
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 69-130 7.63e-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: 40.87  E-value: 7.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186663102  69 PIGVVIGKGVQLGYDCKIYQCVTIgsklEDGVsypkLGDNVTIYANSVIVGGVsVGNNVTIG 130
Cdd:cd03353    25 DPGVILEGKTVIGEDCVIGPNCVI----KDST----IGDGVVIKASSVIEGAV-IGNGATVG 77
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 104-152 1.15e-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: 40.88  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186663102 104 KLGDNVTIyANSVIVGG-VSVGNNVTIGASTLI------------------LKDIPDNCIAIGNPAKI 152
Cdd:cd03351   122 VIGNNVIL-ANNATLAGhVEIGDYAIIGGLSAVhqfcrigrhamvgggsgvVQDVPPYVIAAGNRARL 188
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 104-152 1.56e-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: 40.40  E-value: 1.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1186663102 104 KLGDNVTIYANSVIVGGVSVGNNVTIGASTLIlkdipDNCIaIGNPAKI 152
Cdd:COG1207   268 EIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-----KDST-IGDGVVI 310
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 77-153 1.57e-04

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 40.32  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  77 GVQLGYDCKIYQCVTI--GSKLEDGVS----------YP------KLGDNVTIYANSVIVGGVSVGNNVTIG-------- 130
Cdd:TIGR01852  76 RLIIGDNNTIREFVTInrGTASGGGVTrignnnllmaYShiahdcVVGNHVILANNATLAGHVEVGDYAIIGglvavhqf 155

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1186663102 131 ----------ASTLILKDIPDNCIAIGNPAKII 153
Cdd:TIGR01852 156 vrigryamigGLSAVSKDVPPYCLAEGNRARLR 188
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-147 1.97e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 1.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1186663102  74 IGKGVQLGydckiyqCVTIGSKLeDGVSYPK--LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIG 147
Cdd:PRK14354  371 VGENVNIG-------CGTITVNY-DGKNKFKtiIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 105-153 2.21e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1186663102 105 LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGNPAKII 153
Cdd:PRK14357  386 IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-146 2.29e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 2.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186663102  74 IGKGVQLGydckiyqCVTIGSKLeDGVSYPK--LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAI 146
Cdd:PRK14355  375 IGRNVNIG-------CGTITCNY-DGVKKHRtvIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 69-154 3.81e-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: 38.94  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  69 PIGVVIGKGVQLGYDCKIYQCVTIGSKLedgvsypKLGDNVTIYANSVIVGGVsVGNNVTIGASTLIlkdipDNCIaIGN 148
Cdd:cd03353     7 PETTYIDGDVEIGVDVVIDPGVILEGKT-------VIGEDCVIGPNCVIKDST-IGDGVVIKASSVI-----EGAV-IGN 72


                  ....*.
gi 1186663102 149 PAKIIP 154
Cdd:cd03353    73 GATVGP 78
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 106-144 6.10e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.85  E-value: 6.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1186663102 106 GDNVTIYANSVIVGGVSVGNNVTIGASTlILKD--IPDNCI 144
Cdd:PRK09451  269 GRDVEIDTNVIIEGNVTLGNRVKIGAGC-VLKNcvIGDDCE 308
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 104-144 6.37e-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: 6.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1186663102 104 KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKD--IPDNCI 144
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGvvIGDDCV 45
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 64-148 7.94e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.46  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  64 TILPHpigVVIGKGVQLGYDCKIYQCVTIGSKLED-----GVSYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKD 138
Cdd:PRK12461   37 WIGPH---AVILGPTRIGKNNKIHQGAVVGDEPQDftykgEESRLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLMAY 113

                          90
                  ....*....|..
gi 1186663102 139 --IPDNCIaIGN 148
Cdd:PRK12461  114 shVAHDCQ-IGN 124
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-147 8.22e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.30  E-value: 8.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1186663102  98 DGVSYPK--LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIG 147
Cdd:PRK14353  374 DGFNKHRteIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-155 2.21e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.12  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  74 IGKGVQLGYDCKIYQCVTIGSKledgvsyPKLGDNVTIYANSVIVGGVsVGNNVTIGASTLILKDIPDNCIaIGNPAKII 153
Cdd:PRK14354  262 IDADVEIGSDTVIEPGVVIKGN-------TVIGEDCVIGPGSRIVDST-IGDGVTITNSVIEESKVGDNVT-VGPFAHLR 332


                  ..
gi 1186663102 154 PK 155
Cdd:PRK14354  333 PG 334
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 80-135 2.25e-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: 35.25  E-value: 2.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1186663102  80 LGYDCKIYQCVTI-GSKLEDGVsypKLGDNVTIyANSVIVGGVSVGNNVTIGASTLI 135
Cdd:cd05787    19 IGRNCKIGKNVVIdNSYIWDDV---TIEDGCTI-HHSIVADGAVIGKGCTIPPGSLI 71
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 71-140 2.28e-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: 36.20  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1186663102  71 GVVIGKGVQLGYDCKIYQCVTIGSKLEDGVSYPK-LGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIP 140
Cdd:cd03350    43 WATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPViIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 68-153 2.66e-03

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: 36.19  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  68 HPIGVVIGKgVQLGYDCKIYQCVTI-----GSKLEDGV---------SYP---------------------KLGDNVTIY 112
Cdd:cd04745    10 HPTAVLIGD-VIIGKNCYIGPHASLrgdfgRIVIRDGAnvqdncvihGFPgqdtvleenghighgailhgcTIGRNALVG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1186663102 113 ANSVIVGGVSVGNNVTIGASTLILK--DIPDNCIAIGNPAKII 153
Cdd:cd04745    89 MNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVI 131
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 57-154 2.83e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.03  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186663102  57 KELKTKRTILPHPIGVVIGKGVQLGYDCKIYQCVTIGSKLEdgvsypkLGDNVTIYANSVIvGGVSVGNNVTIGASTLIL 136
Cdd:PRK14355  248 RELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTR-------IGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLE 319

                          90
                  ....*....|....*...
gi 1186663102 137 KDIPDNCIAIGNPAKIIP 154
Cdd:PRK14355  320 DSVVGDDVAIGPMAHLRP 337
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 64-130 5.21e-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: 36.16  E-value: 5.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186663102  64 TILPhpiGVVIGKGVQLGYDCKIYQcvtiGSKLEDGVsypkLGDNVTIYaNSVIVGGVsVGNNVTIG 130
Cdd:COG1207   274 VIDP---NVILEGKTVIGEGVVIGP----NCTLKDST----IGDGVVIK-YSVIEDAV-VGAGATVG 327
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-153 5.58e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 36.07  E-value: 5.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1186663102  98 DGV--SYPKLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAI-GNPAKII 153
Cdd:PRK14352  393 DGVnkHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI 451
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-154 9.68e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 35.35  E-value: 9.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1186663102 104 KLGDNVTIYANSVIVGGVSVGNNVTIGASTLILKDIPDNCIAIGN-PAKIIP 154
Cdd:PRK14359  369 IIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRaPQKNIK 420
 
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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