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Conserved domains on  [gi|1466930614|gb|RGM59147|]
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serine acetyltransferase [Bacteroides uniformis]

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

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 ...
 11-127 8.78e-48

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: 151.39  E-value: 8.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  11 LIHKHNQYLTGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKG-GAPHIGNNVVIASGAKVIG 89
Cdd:COG1045    55 LLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILG 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1466930614  90 NITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKRG 127
Cdd:COG1045   135 PITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKG 172
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 11-127 8.78e-48

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: 151.39  E-value: 8.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  11 LIHKHNQYLTGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKG-GAPHIGNNVVIASGAKVIG 89
Cdd:COG1045    55 LLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILG 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1466930614  90 NITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKRG 127
Cdd:COG1045   135 PITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKG 172
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 20-119 4.28e-39

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: 127.17  E-value: 4.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  20 TGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKG-GAPHIGNNVVIASGAKVIGNITIGNNVM 98
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGkRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1466930614  99 IGSGAIVVTDIPDNSVVVGNP 119
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 22-123 4.18e-23

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 91.24  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  22 IQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVrGPKGG--APHIGNNVVIASGAKVIGNITIGNNVMI 99
Cdd:PLN02694  161 VDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGT-GKACGdrHPKIGDGVLIGAGATILGNVKIGEGAKI 239

                          90       100
                  ....*....|....*....|....
gi 1466930614 100 GSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:PLN02694  240 GAGSVVLIDVPPRTTAVGNPARLV 263
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 43-119 2.61e-16

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: 71.37  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  43 VINGSAI------IGDNCTIYHGVTVGsvrgpkgGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVV 116
Cdd:TIGR03570 125 IINTGAIvehdcvIGDFVHIAPGVTLS-------GGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVV 197


                  ...
gi 1466930614 117 GNP 119
Cdd:TIGR03570 198 GVP 200
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
73-101 2.17e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 1466930614  73 PHIGNNVVIASGAKVIGNITIGNNVMIGS 101
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 11-127 8.78e-48

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: 151.39  E-value: 8.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  11 LIHKHNQYLTGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKG-GAPHIGNNVVIASGAKVIG 89
Cdd:COG1045    55 LLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILG 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1466930614  90 NITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKRG 127
Cdd:COG1045   135 PITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKG 172
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 20-119 4.28e-39

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: 127.17  E-value: 4.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  20 TGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKG-GAPHIGNNVVIASGAKVIGNITIGNNVM 98
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGkRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1466930614  99 IGSGAIVVTDIPDNSVVVGNP 119
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 22-123 4.18e-23

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 91.24  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  22 IQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVrGPKGG--APHIGNNVVIASGAKVIGNITIGNNVMI 99
Cdd:PLN02694  161 VDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGT-GKACGdrHPKIGDGVLIGAGATILGNVKIGEGAKI 239

                          90       100
                  ....*....|....*....|....
gi 1466930614 100 GSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:PLN02694  240 GAGSVVLIDVPPRTTAVGNPARLV 263
PLN02739 PLN02739
serine acetyltransferase
 21-123 1.88e-22

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 90.48  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKGGA-PHIGNNVVIASGAKVIGNITIGNNVMI 99
Cdd:PLN02739  205 GIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRhPKIGDGALLGACVTILGNISIGAGAMV 284

                          90       100
                  ....*....|....*....|....
gi 1466930614 100 GSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:PLN02739  285 AAGSLVLKDVPSHSMVAGNPAKLI 308
PLN02357 PLN02357
serine acetyltransferase
 27-123 3.97e-22

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 89.56  E-value: 3.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  27 GTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKGGA-PHIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:PLN02357  232 GAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 311

                          90
                  ....*....|....*...
gi 1466930614 106 VTDIPDNSVVVGNPGKVI 123
Cdd:PLN02357  312 LKDVPPRTTAVGNPARLI 329
PRK10191 PRK10191
putative acyl transferase; Provisional
 19-122 7.61e-21

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 81.86  E-value: 7.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  19 LTGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVM 98
Cdd:PRK10191   39 FFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVT 118

                          90       100
                  ....*....|....*....|....
gi 1466930614  99 IGSGAIVVTDIPDNSVVVGNPGKV 122
Cdd:PRK10191  119 VGAGSVVLDSVPDNALVVGEKARV 142
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
18-126 6.81e-20

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 79.14  E-value: 6.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  18 YLTGIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIY---HGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIG 94
Cdd:COG0110    24 YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILtgnHPIDDPATFPLRTGPVTIGDDVWIGAGATILPGVTIG 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1466930614  95 NNVMIGSGAIVVTDIPDNSVVVGNPGKVISKR 126
Cdd:COG0110   104 DGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 25-123 1.38e-19

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: 79.39  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  25 GFGTKIGKALmFPHYSCIVINGSAI-IGDNC---------TIYHGVTVGS-VRGPKGGAP-HIGNNVVIASGAKVIGNIT 92
Cdd:cd03357    60 GYNIHIGDNF-YANFNCTILDVAPVtIGDNVligpnvqiyTAGHPLDPEErNRGLEYAKPiTIGDNVWIGGGVIILPGVT 138

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1466930614  93 IGNNVMIGSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:cd03357   139 IGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
cysE PRK11132
serine acetyltransferase; Provisional
 21-125 1.29e-18

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 78.97  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIGKALMFPHYSCIVINGSAIIGDNCTIYHGVTVGSVrGPKGG--APHIGNNVVIASGAKVIGNITIGNNVM 98
Cdd:PRK11132  141 QVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGT-GKTSGdrHPKIREGVMIGAGAKILGNIEVGRGAK 219

                          90       100
                  ....*....|....*....|....*..
gi 1466930614  99 IGSGAIVVTDIPDNSVVVGNPGKVISK 125
Cdd:PRK11132  220 IGAGSVVLQPVPPHTTAAGVPARIVGK 246
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 43-119 2.61e-16

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: 71.37  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  43 VINGSAI------IGDNCTIYHGVTVGsvrgpkgGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVV 116
Cdd:TIGR03570 125 IINTGAIvehdcvIGDFVHIAPGVTLS-------GGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVV 197


                  ...
gi 1466930614 117 GNP 119
Cdd:TIGR03570 198 GVP 200
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 21-123 5.40e-16

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: 68.25  E-value: 5.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIGkalmfpHYSCIVINGSAIIGDNCTIYHGVTV------------GSVRGPKGGAPHIGNNVVIASGAKVI 88
Cdd:cd04647     1 NISIGDNVYIG------PGCVISAGGGITIGDNVLIGPNVTIydhnhdiddperPIEQGVTSAPIVIGDDVWIGANVVIL 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1466930614  89 GNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:cd04647    75 PGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 25-125 1.03e-15

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 69.46  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  25 GFGTKIGKALmFPHYSCIVINGSAI-IGDNCTIYHGV----------TVGSVRGPKGGAP-HIGNNVVIASGAKVIGNIT 92
Cdd:PRK10092   71 GYNIFLGNNF-YANFDCVMLDVCPIrIGDNCMLAPGVhiytathpldPVARNSGAELGKPvTIGNNVWIGGRAVINPGVT 149

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1466930614  93 IGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISK 125
Cdd:PRK10092  150 IGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 1-119 1.93e-15

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: 69.05  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614   1 MAKFCLRCVQLIHKHNQYLTGIQIGFGTKIGKalmfphysCIVINGSAIIGDNCTIYHGVTVG--------SVRGPK--- 69
Cdd:cd03360    76 LLAAGYRFATLIHPSAVVSPSAVIGEGCVIMA--------GAVINPDARIGDNVIINTGAVIGhdcvigdfVHIAPGvvl 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1466930614  70 GGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNP 119
Cdd:cd03360   148 SGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 47-123 7.97e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 61.58  E-value: 7.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466930614  47 SAIIGDNCTIYHGVTVGsvrgpkgGApHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVV--TDIPDNSVVVGNPGKVI 123
Cdd:COG0663    71 PLTIGDDVTIGHGAILH-------GC-TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVV 141
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 24-123 1.04e-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: 60.21  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  24 IGFGTKIGKALMfphyscivINGSAIIGDNCTI------YHGVTVGS--------------------VRGPKGGAPHIGN 77
Cdd:cd03358     1 IGDNCIIGTNVF--------IENDVKIGDNVKIqsnvsiYEGVTIEDdvfigpnvvftndlyprskiYRKWELKGTTVKR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1466930614  78 NVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVI 123
Cdd:cd03358    73 GASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARII 118
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 49-123 2.25e-12

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 60.12  E-value: 2.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466930614  49 IIGDNCTIYHGVTVGSVRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIVV--TDIPDNSVVVGNPGKVI 123
Cdd:cd04645    62 IIGDNVTVGHGAVLHGCT--------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVV 130
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 22-126 5.22e-12

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: 59.09  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  22 IQIGFGTKIGkalmfpHYSCIVINGSAIIGDNCTIYHGVTVG--------------------SVRGPKGGAPH------- 74
Cdd:cd03349     2 ISVGDYSYGS------GPDCDVGGDKLSIGKFCSIAPGVKIGlggnhptdwvstypfyifggEWEDDAKFDDWpskgdvi 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1466930614  75 IGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKR 126
Cdd:cd03349    76 IGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 42-134 5.89e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 57.32  E-value: 5.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  42 IVINGSAIIGDNCTIYHGVTVGSVRGP------KGGAPH-----IGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIP 110
Cdd:PRK09527   90 IVDDYTVTIGDNVLIAPNVTLSVTGHPvhhelrKNGEMYsfpitIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIP 169

                          90       100
                  ....*....|....*....|....
gi 1466930614 111 DNSVVVGNPGKVISKRGLEHTKYY 134
Cdd:PRK09527  170 PNVVAAGVPCRVIREINDRDKQYY 193
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 64-129 4.54e-10

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 54.88  E-value: 4.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466930614  64 SVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKRGLE 129
Cdd:PRK09677  122 DMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHE 187
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 50-125 1.26e-09

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: 52.96  E-value: 1.26e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466930614  50 IGDNCTIYHGVTVGSVRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIVV--TDIPDNSVVVGNPGKVISK 125
Cdd:cd04650    64 IGDYVTIGHNAVVHGAK--------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRK 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 49-119 1.55e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 54.25  E-value: 1.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466930614  49 IIGDNCTIYHGVTV-GSVRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNP 119
Cdd:COG1044   242 RIGEHTAIAAQVGIaGSTK--------IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 43-105 1.51e-08

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: 48.40  E-value: 1.51e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGSVRGP-KGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:cd00208    14 VIRGPVVIGDNVNIGPGAVIGAATGPnEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 49-121 1.74e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 50.48  E-value: 1.74e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466930614  49 IIGDNCTIYHGVTV-GSVrgpkggapHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGK 121
Cdd:cd03352   134 RIGENCLIAAQVGIaGST--------TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 50-123 1.13e-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: 46.83  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  50 IGDNCTIYHGVTV--GS--VRGP----KGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGK 121
Cdd:cd05825    26 IGSDACISQGAYLctGShdYRSPafplITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAV 105


                  ..
gi 1466930614 122 VI 123
Cdd:cd05825   106 PV 107
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-116 1.42e-07

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 48.87  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIGkalmfpHYSCIvinGSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSG 102
Cdd:PRK09451  354 RLGKGSKAG------HLTYL---GDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAG 424

                          90
                  ....*....|....
gi 1466930614 103 AIVVTDIPDNSVVV 116
Cdd:PRK09451  425 TTVTRDVAENELVI 438
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 43-105 1.64e-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: 48.48  E-value: 1.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGSvrgpkgGApHIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:COG1044   122 VIGAGVVIGDGVVIGPGVVIGD------GV-VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 43-123 4.73e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGSvrgpkgGApHIGNNVVIASGAkVIG-NITIGNNVMIGSGAIVVTDipdnsVVVGN--- 118
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGA------GV-VIGDGVVIGAGA-VIGdGVKIGADCRLHANVTIYHA-----VRIGNrvi 174


                  ....*..
gi 1466930614 119 --PGKVI 123
Cdd:PRK00892  175 ihSGAVI 181
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 21-128 8.10e-07

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 46.27  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIGkalmfPHyscIVINGSAIIGDNCTIYHGVTVGSV----------------------------RGPKGGA 72
Cdd:cd03351    29 NVEIGDGTVIG-----SH---VVIDGPTTIGKNNRIFPFASIGEApqdlkykgeptrleigdnntirefvtihRGTAQGG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  73 P--------------------HIGNNVVIASGAKVIGNITIGNNV------------------MIGSGAIVVTDIPDNSV 114
Cdd:cd03351   101 GvtrignnnllmayvhvahdcVIGNNVILANNATLAGHVEIGDYAiigglsavhqfcrigrhaMVGGGSGVVQDVPPYVI 180

                         170
                  ....*....|....
gi 1466930614 115 VVGNPGKViskRGL 128
Cdd:cd03351   181 AAGNRARL---RGL 191
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 24-128 9.55e-07

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: 46.16  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  24 IGFGTKIGkalmfPHyscIVINGSAIIGDNCTIYHGVTVGSV----------------------------RG-PKGGAP- 73
Cdd:COG1043    34 IGDGTVIG-----SH---VVIEGPTTIGKNNRIFPFASIGEEpqdlkykgeptrleigdnntirefvtihRGtVQGGGVt 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  74 ------------------HIGNNVVIASGAKVIGNITIGNNV------------------MIGSGAIVVTDIPDNSVVVG 117
Cdd:COG1043   106 rigddnllmayvhvahdcVVGNNVILANNATLAGHVEVGDHAiigglsavhqfvrigahaMVGGGSGVVKDVPPYVLAAG 185

                         170
                  ....*....|.
gi 1466930614 118 NPGKViskRGL 128
Cdd:COG1043   186 NPARL---RGL 193
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 49-117 9.66e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 9.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  49 IIGDNCTIYHGVTV-GSVRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVG 117
Cdd:PRK00892  245 VIGRHTAIAAQVGIaGSTK--------IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSS 306
PRK10502 PRK10502
putative acyl transferase; Provisional
 26-126 1.51e-06

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 44.94  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  26 FGTKIGKALM--------FP------HYSCI----VIN--GSAIIGDNCTIYHGVTV--GSVR------GPKGGAPHIGN 77
Cdd:PRK10502   50 FGAKIGKGVVirpsvritYPwkltigDYAWIgddvWLYnlGEITIGAHCVISQKSYLctGSHDysdphfDLNTAPIVIGE 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1466930614  78 NVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVGNPGKVISKR 126
Cdd:PRK10502  130 GCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-123 3.44e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.92  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIGkalmfpHYSCIvinGSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSG 102
Cdd:PRK14360  350 QLGEGSKVN------HLSYI---GDATLGEQVNIGAGTITANYDGVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAG 420

                          90       100
                  ....*....|....*....|.
gi 1466930614 103 AIVVTDIPDNSVVVGNPGKVI 123
Cdd:PRK14360  421 STITKDVPDNSLAIARSRQVI 441
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 47-103 4.86e-06

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: 44.17  E-value: 4.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1466930614  47 SAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGA 103
Cdd:TIGR01852  76 RLIIGDNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNA 132
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
49-128 9.34e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 9.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  49 IIGDNCTIYHGVTV--GSVrgpKGGAP-------------------HIGNNVVIASGAKVIGNITIGNNV---------- 97
Cdd:PRK05289   82 VIGDNNTIREFVTInrGTV---QGGGVtrigdnnllmayvhvahdcVVGNHVILANNATLAGHVEVGDYAiiggltavhq 158

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1466930614  98 --------MIGSGAIVVTDIPDNSVVVGNPGKViskRGL 128
Cdd:PRK05289  159 fvrigahaMVGGMSGVSQDVPPYVLAEGNPARL---RGL 194
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 42-123 1.15e-05

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 42.36  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  42 IVINGSAIIGDNCTIYHGVTVGSVRGPKG----GA----PHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVV--TDIPD 111
Cdd:cd04745    40 IVIRDGANVQDNCVIHGFPGQDTVLEENGhighGAilhgCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKagTVIPP 119

                          90
                  ....*....|..
gi 1466930614 112 NSVVVGNPGKVI 123
Cdd:cd04745   120 RSLIAGSPAKVI 131
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-125 1.67e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.83  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  28 TKIGKALMFPHYSCIvinGSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVT 107
Cdd:PRK14357  342 STIGENTKAQHLTYL---GDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITE 418

                          90
                  ....*....|....*...
gi 1466930614 108 DIPDNSVVVGNPGKVISK 125
Cdd:PRK14357  419 DVPPYSLALGRARQIVKE 436
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 65-120 5.26e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.78  E-value: 5.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466930614  65 VRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGA--------IVV---TDIPDNSVVVGNPG 120
Cdd:COG0663     3 IYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAvlrgdvgpIRIgegSNIQDGVVLHVDPG 69
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 37-124 6.93e-05

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: 40.28  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  37 PHYSCIVINGSAIIGDNCTIYhgvtvgsvrgpkggAPHIGNNVVIASGAkVIGNIT-IGNNVMIGSGAIVVTD--IPDNS 113
Cdd:cd03359    68 VAFFPLHIGDYVFIGENCVVN--------------AAQIGSYVHIGKNC-VIGRRCiIKDCVKILDGTVVPPDtvIPPYS 132

                          90
                  ....*....|.
gi 1466930614 114 VVVGNPGKVIS 124
Cdd:cd03359   133 VVSGRPARFIG 143
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 49-115 7.79e-05

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 40.30  E-value: 7.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466930614  49 IIGDNCTIYHGVTVGSVrgpKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVV-TDIPDNSVV 115
Cdd:cd00710    44 IIGANVNIQDGVVIHAL---EGYSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFnAKVGDNCVI 108
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 43-105 8.51e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.47  E-value: 8.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGS-VRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:cd03352    15 VIGEGVVIGDGVVIGPGVVIGDgVV--------IGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-117 9.70e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 9.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1466930614  74 HIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVG 117
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 23-117 1.75e-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: 40.01  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIgkalmfPHYSCIvinGSAIIGDNCTI--------YHGV----TVgsvrgpkggaphIGNNVVIASGAKVIGN 90
Cdd:COG1207   354 TIGEGSKV------NHLSYI---GDAEIGEGVNIgagtitcnYDGVnkhrTV------------IGDGAFIGSNTNLVAP 412

                          90       100
                  ....*....|....*....|....*..
gi 1466930614  91 ITIGNNVMIGSGAIVVTDIPDNSVVVG 117
Cdd:COG1207   413 VTIGDGATIGAGSTITKDVPAGALAIA 439
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 46-117 2.47e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.32  E-value: 2.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466930614  46 GSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVVG 117
Cdd:PRK14356  372 GDAEIGAGANIGAGTITCNYDGVNKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 21-116 2.91e-04

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIGkalmfphySCIVINGSAIIGDNCTIYHGVTVGSVRGPKGGAPH-IGNNVVIASGAKVIGNITIGNNVMI 99
Cdd:cd03350    31 GAYVDEGTMVD--------SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPViIEDDVFIGANCEVVEGVIVGKGAVL 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1466930614 100 GSGAIVVT---------------DIPDNSVVV 116
Cdd:cd03350   103 AAGVVLTQstpiydretgeiyygRVPPGSVVV 134
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 47-105 4.71e-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: 38.16  E-value: 4.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1466930614  47 SAIIGDNCTIYHGVTVGSvrgpkgGApHIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:cd03352     1 SAKIGENVSIGPNAVIGE------GV-VIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
PLN02296 PLN02296
carbonate dehydratase
 72-115 5.00e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 38.57  E-value: 5.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1466930614  72 APHIGNNVVIASGAKVIGNITIG---------------NNVMIGSGaivvTDIPDNSVV 115
Cdd:PLN02296   52 APVVDKDAFVAPSASVIGDVQVGrgssiwygcvlrgdvNSISVGSG----TNIQDNSLV 106
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 24-105 5.05e-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: 38.16  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  24 IGFGTKIGK-ALMFPHyscIVINGSAIIGDNCTIYHGVTVGSvrgpkgGApHIGNNVVIASGAKV--------------- 87
Cdd:cd03352    16 IGEGVVIGDgVVIGPG---VVIGDGVVIGDDCVIHPNVTIYE------GC-IIGDRVIIHSGAVIgsdgfgfapdgggwv 85

                          90       100
                  ....*....|....*....|..
gi 1466930614  88 ----IGNITIGNNVMIGSGAIV 105
Cdd:cd03352    86 kipqLGGVIIGDDVEIGANTTI 107
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 43-129 5.49e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 38.59  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  43 VINGSAIIGDNCTIyhgvtvgSVRGPKGGAPHIGNNVVIASGA--KVIGNITIGNNVMIGS-GAIVVTDIPDNSVVVGnp 119
Cdd:PRK06416  109 IIRGEAKLVDPNTV-------RVMTEDGEQTYTAKNIILATGSrpRELPGIEIDGRVIWTSdEALNLDEVPKSLVVIG-- 179

                          90
                  ....*....|
gi 1466930614 120 GKVIskrGLE 129
Cdd:PRK06416  180 GGYI---GVE 186
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 75-116 6.40e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.43  E-value: 6.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1466930614  75 IGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVV 116
Cdd:PRK14359  370 IGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAI 411
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-117 7.62e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  29 KIGKALMFPHYSCI-----VINGSAIIGDNCTIYHGVTVGsvrgpkgGAPHIGNNVVIASGAkVIGNITIGNNVMIGSGA 103
Cdd:PRK14355  245 RINRELMLAGVTLIdpettYIDRGVVIGRDTTIYPGVCIS-------GDTRIGEGCTIEQGV-VIKGCRIGDDVTVKAGS 316

                          90
                  ....*....|....
gi 1466930614 104 IVVTDIPDNSVVVG 117
Cdd:PRK14355  317 VLEDSVVGDDVAIG 330
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 23-117 7.88e-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: 37.40  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIGkalmfpHYSCIvinGSAIIGDNCTI--------YHGV----TVgsvrgpkggaphIGNNVVIASGAKVIGN 90
Cdd:cd03353   104 TIGEGSKAN------HLSYL---GDAEIGEGVNIgagtitcnYDGVnkhrTV------------IGDNVFIGSNSQLVAP 162

                          90       100
                  ....*....|....*....|....*..
gi 1466930614  91 ITIGNNVMIGSGAIVVTDIPDNSVVVG 117
Cdd:cd03353   163 VTIGDGATIAAGSTITKDVPPGALAIA 189
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-117 8.92e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.89  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIgkalmfPHYSCIvinGSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSG 102
Cdd:PRK14354  353 TIGEGTKV------SHLTYI---GDAEVGENVNIGCGTITVNYDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAG 423

                          90
                  ....*....|....*
gi 1466930614 103 AIVVTDIPDNSVVVG 117
Cdd:PRK14354  424 STITKDVPEDALAIA 438
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 21-118 9.36e-04

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 37.30  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIgkalmfpHYSCIVI--NGSAIIGDNCTIYHGVTV--GSVRGPKGG------------------APHIGNN 78
Cdd:cd04646    17 DVTIGPGTVV-------HPRATIIaeAGPIIIGENNIIEEQVTIvnKKPKDPAEPkpmiigsnnvfevgckceALKIGNN 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1466930614  79 VVIASGAKVIGNITIGNNVMIGSGAIVVTD--IPDNSVVVGN 118
Cdd:cd04646    90 NVFESKSFVGKNVIITDGCIIGAGCKLPSSeiLPENTVIYGA 131
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
43-105 1.02e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.39  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGS-VRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:PRK05289   10 IVEPGAKIGENVEIGPFCVIGPnVV--------IGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 47-123 1.06e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.50  E-value: 1.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466930614  47 SAIIGDNCTIYHGVTVGSVrgpkggaphIGNNVVIASGAKVIGNItIGNNVMIGSGAIVVTDIPDNSVVVGnPGKVI 123
Cdd:PRK00844  315 DSLVSAGSIISGATVRNSV---------LSPNVVVESGAEVEDSV-LMDGVRIGRGAVVRRAILDKNVVVP-PGATI 380
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 46-116 1.07e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 1.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466930614  46 GSAIIGDNCTIYHGVTVGSVRGPKGGAPHIGNNVVIASGAKVIGNITIGNNVMIGSGAIVVTDIPDNSVVV 116
Cdd:PRK14355  371 GDATIGRNVNIGCGTITCNYDGVKKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 49-105 1.43e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.92  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466930614  49 IIGDNCTIYHGVTVGsvRGPKGGAP-------------------HIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:PRK12461   79 EIGDRNVIREGVTIH--RGTKGGGVtrigndnllmayshvahdcQIGNNVILVNGALLAGHVTVGDRAIISGNCLV 152
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 43-105 1.76e-03

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: 36.64  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466930614  43 VINGSAIIGDNCTIYHGVTVGS-VRgpkggaphIGNNVVIASGAKVIGNITIGNNVMIGSGAIV 105
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGPnVE--------IGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 21-103 2.14e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKIgkalmfphYSCIVINGSAIIGDNCTIYHGVTVGSVRgpkggaphIGNNVVIASGAkVIGNITIGNNVMIG 100
Cdd:PRK14355  268 GVVIGRDTTI--------YPGVCISGDTRIGEGCTIEQGVVIKGCR--------IGDDVTVKAGS-VLEDSVVGDDVAIG 330


                  ...
gi 1466930614 101 SGA 103
Cdd:PRK14355  331 PMA 333
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
73-101 2.17e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 1466930614  73 PHIGNNVVIASGAKVIGNITIGNNVMIGS 101
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PLN02296 PLN02296
carbonate dehydratase
 21-135 3.74e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 35.87  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  21 GIQIGFGTKI-GKALMfpHYSCIVINGS---AIIGDNCTI-----YHGVTVgsvrgpkggaphiGNNVVIASGAKVIGNI 91
Cdd:PLN02296   91 SISVGSGTNIqDNSLV--HVAKTNLSGKvlpTIIGDNVTIghsavLHGCTV-------------EDEAFVGMGATLLDGV 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1466930614  92 TIGNNVMIGSGAIVV--TDIPDNSVVVGNPGKVISKRGLEHTKYYS 135
Cdd:PLN02296  156 VVEKHAMVAAGALVRqnTRIPSGEVWAGNPAKFLRKLTEEEIAFIS 201
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-123 5.86e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 35.30  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  23 QIGFGTKIgkalmfPHYSCIvinGSAIIGDNCTI--------YHGV----TVgsvrgpkggaphIGNNVVIASGAKVIGN 90
Cdd:PRK14352  359 TIGRGTKV------PHLTYV---GDADIGEHSNIgassvfvnYDGVnkhrTT------------IGSHVRTGSDTMFVAP 417

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1466930614  91 ITIGNNVMIGSGAIVVTDIPDNSVVV-GNPGKVI 123
Cdd:PRK14352  418 VTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI 451
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 43-125 7.96e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 33.37  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466930614  43 VINGSAIIGDNCTIYHGVtvgsvrgpkggaphIGNNVVIASGAKVIGNItIGNNVMIGSGAIVVTDIPDNSVVVGNPGKV 122
Cdd:cd03356     1 LIGESTVIGENAIIKNSV--------------IGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIIGDNAVIGENVRV 65


                  ...
gi 1466930614 123 ISK 125
Cdd:cd03356    66 VNL 68
 
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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