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Conserved domains on  [gi|15598352|ref|NP_251846|]
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UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase [Pseudomonas aeruginosa PAO1]

Protein Classification

acyltransferase( domain architecture ID 10129729)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to Helicobacter pullorum N-acetyltransferase

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0120225
PubMed:  15500694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.39e-62

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: 187.71  E-value: 6.39e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  35 IGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANC 114
Cdd:cd03358   1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598352 115 TIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:cd03358  81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.39e-62

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: 187.71  E-value: 6.39e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  35 IGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANC 114
Cdd:cd03358   1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598352 115 TIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:cd03358  81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
32-157 1.47e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.51  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  32 GARIGAGVSLGQNVFV-GNKVVIGDRCKIQNNVSVYD--NVTLEEGVFCGPSMVFTNVYNPRSLIERKDQY-RNTLVKKG 107
Cdd:COG0110   8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15598352 108 ATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSE 157
Cdd:COG0110  88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 4-149 8.94e-21

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: 85.24  E-value: 8.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352     4 YQHPSAIVDDGAQIGsdsrvwHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLeegvfCGpsmvf 83
Cdd:TIGR03570  89 LIHPSAIVSPSASIG------EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTL-----SG----- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598352    84 tnvynprslierkdqyrNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPA 149
Cdd:TIGR03570 153 -----------------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 6-75 5.76e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 77.10  E-value: 5.76e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGV 75
Cdd:PRK00892 104 HPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRV 173
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.39e-62

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: 187.71  E-value: 6.39e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  35 IGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANC 114
Cdd:cd03358   1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598352 115 TIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:cd03358  81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
32-157 1.47e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.51  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  32 GARIGAGVSLGQNVFV-GNKVVIGDRCKIQNNVSVYD--NVTLEEGVFCGPSMVFTNVYNPRSLIERKDQY-RNTLVKKG 107
Cdd:COG0110   8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15598352 108 ATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSE 157
Cdd:COG0110  88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 34-152 1.92e-23

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: 89.44  E-value: 1.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  34 RIGAGVSLGQNVFV--GNKVVIGDRCKIQNNVSVYDNvtleegvfcgpsmvFTNVYNPRSLIERKDQYRNTLVKKGATLG 111
Cdd:cd04647   3 SIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDH--------------NHDIDDPERPIEQGVTSAPIVIGDDVWIG 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598352 112 ANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:cd04647  69 ANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 4-149 8.94e-21

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: 85.24  E-value: 8.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352     4 YQHPSAIVDDGAQIGsdsrvwHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLeegvfCGpsmvf 83
Cdd:TIGR03570  89 LIHPSAIVSPSASIG------EGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTL-----SG----- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598352    84 tnvynprslierkdqyrNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPA 149
Cdd:TIGR03570 153 -----------------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 6-148 1.14e-19

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: 82.15  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDsrvwhfVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLeegvfCGpsmvftn 85
Cdd:cd03360  88 HPSAVVSPSAVIGEG------CVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVL-----SG------- 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598352  86 vynprslierkdqyrNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVP 148
Cdd:cd03360 150 ---------------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 6-150 2.04e-19

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: 83.91  E-value: 2.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMV--- 82
Cdd:COG1044 100 HPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAViga 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  83 --FTNVYNPRSLIERKDQ----------------------YRNTLVKKG------------------------------A 108
Cdd:COG1044 180 dgFGFAPDEDGGWVKIPQlgrvvigddveiganttidrgaLGDTVIGDGtkidnlvqiahnvrigehtaiaaqvgiagsT 259

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15598352 109 TLGANCTI-----VCG-VTIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:COG1044 260 KIGDNVVIggqvgIAGhLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 23-153 2.92e-17

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: 75.12  E-value: 2.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  23 VWHFVHICAGARIGAGVSLGQNVFV--GNKVVIGDRCKIQNNVSVYDNVTLeeGVfcgpsmvftnvynpRSLIERKdqyR 100
Cdd:COG1045  56 LSERARFLTGIDIHPGATIGRGFFIdhGTGVVIGETAVIGDNVTIYQGVTL--GG--------------TGKEKGK---R 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598352 101 NTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:COG1045 117 HPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 6-75 5.76e-17

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 77.10  E-value: 5.76e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGV 75
Cdd:PRK00892 104 HPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRV 173
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 6-150 1.54e-15

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: 72.08  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSV--------Y----------D 67
Cdd:cd03351   3 HPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkYkgeptrleigD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  68 NVTLEEGVFCGPS----------------MVFTNVY------NprslierkdqyrNTLVKKGATLGANCTI----VCG-- 119
Cdd:cd03351  83 NNTIREFVTIHRGtaqgggvtrignnnllMAYVHVAhdcvigN------------NVILANNATLAGHVEIgdyaIIGgl 150

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15598352 120 ------VTIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:cd03351 151 savhqfCRIGRHAMVGGGSGVVQDVPPYVIAAGNRAR 187
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 27-148 4.03e-15

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: 67.47  E-value: 4.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  27 VHICAGARIGAGVSLGQnvfvGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGpsmvftnvyNPRSLIerkdqyrntlVKK 106
Cdd:cd03354   3 IDIHPGAKIGPGLFIDH----GTGIVIGETAVIGDNCTIYQGVTLGGKGKGG---------GKRHPT----------IGD 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15598352 107 GATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVP 148
Cdd:cd03354  60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 6-150 1.62e-14

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: 69.28  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSV--------Y----------D 67
Cdd:COG1043   5 HPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIgeepqdlkYkgeptrleigD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  68 NVTLEEGV--------------------F---------C--GPSMVFTNvynprslierkdqyrntlvkkGATLGANCTI 116
Cdd:COG1043  85 NNTIREFVtihrgtvqgggvtrigddnlLmayvhvahdCvvGNNVILAN---------------------NATLAGHVEV 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15598352 117 --------VCGV----TIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:COG1043 144 gdhaiiggLSAVhqfvRIGAHAMVGGGSGVVKDVPPYVLAAGNPAR 189
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 27-152 1.73e-14

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 67.83  E-value: 1.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  27 VHICAGARI--GAGVSLGQNVFV--------GNKVVIGDRCKIQNNVSVYdnvtleegvfcgpsmvfTnVYNPRSLIERK 96
Cdd:cd03357  49 VYIEPPFHCdyGYNIHIGDNFYAnfnctildVAPVTIGDNVLIGPNVQIY-----------------T-AGHPLDPEERN 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598352  97 DQYRNTL---VKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:cd03357 111 RGLEYAKpitIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 8-151 4.70e-14

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: 67.06  E-value: 4.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   8 SAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNkVVIGDRCKIQNNvSVYDNVTLEEGVFCGPsmvFTNVy 87
Cdd:cd03353   9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKAS-SVIEGAVIGNGATVGP---FAHL- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  88 NPRSLIER-------------------------------------------------KDQYRnTLVKKGATLGANCTIVC 118
Cdd:cd03353  83 RPGTVLGEgvhignfveikkstigegskanhlsylgdaeigegvnigagtitcnydgVNKHR-TVIGDNVFIGSNSQLVA 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 15598352 119 GVTIGEYAFVGAGAVINKNVPSYALMVGVpARQ 151
Cdd:cd03353 162 PVTIGDGATIAAGSTITKDVPPGALAIAR-ARQ 193
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 15-126 8.91e-14

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: 66.66  E-value: 8.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  15 AQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMV-----FTNVYNP 89
Cdd:cd03352   2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVigsdgFGFAPDG 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598352  90 RSLIeRKDQYRNTLVKKGATLGANCTIVCGV----TIGEYA 126
Cdd:cd03352  82 GGWV-KIPQLGGVIIGDDVEIGANTTIDRGAlgdtVIGDGT 121
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
6-150 2.29e-13

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 66.28  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSV--------Y----------D 67
Cdd:PRK05289   6 HPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkYkgeptrlvigD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   68 NVTLEEGV--------------------F---------C--GPSMVFTNvynprslierkdqyrntlvkkGATLGANCTI 116
Cdd:PRK05289  86 NNTIREFVtinrgtvqgggvtrigdnnlLmayvhvahdCvvGNHVILAN---------------------NATLAGHVEV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15598352  117 --------VCGV----TIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:PRK05289 145 gdyaiiggLTAVhqfvRIGAHAMVGGMSGVSQDVPPYVLAEGNPAR 190
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 6-152 3.50e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 64.28  E-value: 3.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQ-IGSdsrvwhfVHICAGARIGAGVSL-GQNvfvgNKVVIGDRCKIQNNVSV-----YDnVTLEEGVFCG 78
Cdd:COG0663  14 HPSAFVAPTAVvIGD-------VTIGEDVSVWPGAVLrGDV----GPIRIGEGSNIQDGVVLhvdpgYP-LTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  79 PsmvftnvynpRSLIErkdqyrntlvkkGATLGANC-----TIVC-GVTIGEYAFVGAGAVI--NKNVPSYALMVGVPAR 150
Cdd:COG0663  82 H----------GAILH------------GCTIGDNVligmgAIVLdGAVIGDGSIVGAGALVteGKVVPPGSLVVGSPAK 139


                ..
gi 15598352 151 QI 152
Cdd:COG0663 140 VV 141
PLN02739 PLN02739
serine acetyltransferase
 27-157 8.75e-13

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 65.44  E-value: 8.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   27 VHICAGARIGAGVSL--GQNVFVGNKVVIGDRckiqnnVSVYDNVTLeegvfcGPSMVFTNVYNPRslierkdqyrntlV 104
Cdd:PLN02739 206 IDIHPAARIGKGILLdhGTGVVIGETAVIGDR------VSILHGVTL------GGTGKETGDRHPK-------------I 260

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15598352  105 KKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSE 157
Cdd:PLN02739 261 GDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 110-154 1.46e-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: 62.18  E-value: 1.46e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15598352 110 LGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGW 154
Cdd:cd03349  82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-154 2.36e-12

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.47  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    8 SAIVDdgAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVgNKVVIGDRCKIqNNVSVYDNVTLEEGVFCGPSMVFTNvY 87
Cdd:PRK14354 312 SVIEE--SKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEI-KKSTIGEGTKV-SHLTYIGDAEVGENVNIGCGTITVN-Y 386

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   88 NPrslierKDQYRnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGvPARQI---GW 154
Cdd:PRK14354 387 DG------KNKFK-TIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA-RARQVnkeGY 448
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 11-154 2.77e-12

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: 64.28  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  11 VDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNkVVIGDRCKIQNnvSVYDNVTLEEGVFCGPsmvFTNVyNPR 90
Cdd:COG1207 263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD-STIGDGVVIKY--SVIEDAVVGAGATVGP---FARL-RPG 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  91 SLIER----------KdqyrNTLVKKG-----------ATLGANCTIVCG------------------------------ 119
Cdd:COG1207 336 TVLGEgvkignfvevK----NSTIGEGskvnhlsyigdAEIGEGVNIGAGtitcnydgvnkhrtvigdgafigsntnlva 411

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15598352 120 -VTIGEYAFVGAGAVINKNVPSYALMVGVpARQI---GW 154
Cdd:COG1207 412 pVTIGDGATIGAGSTITKDVPAGALAIAR-ARQRnieGW 449
PLN02357 PLN02357
serine acetyltransferase
 27-153 5.83e-12

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 62.98  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   27 VHICAGARIGAGVSLGQnvfvGNKVVIGDRCKIQNNVSVYDNVTLE-EGVFCGPsmvftnvynprslierkdqyRNTLVK 105
Cdd:PLN02357 227 VDIHPGAKIGQGILLDH----ATGVVIGETAVVGNNVSILHNVTLGgTGKQSGD--------------------RHPKIG 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598352  106 KGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:PLN02357 283 DGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
PLN02694 PLN02694
serine O-acetyltransferase
 27-153 1.87e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 61.20  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   27 VHICAGARIGAGVSLGQnvfvGNKVVIGDRCKIQNNVSVYDNVTLE-EGVFCGPsmvftnvynprslierkdqyRNTLVK 105
Cdd:PLN02694 161 VDIHPAAKIGKGILFDH----ATGVVIGETAVIGNNVSILHHVTLGgTGKACGD--------------------RHPKIG 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598352  106 KGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:PLN02694 217 DGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG 264
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-163 2.67e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 61.42  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    7 PSAIVDDGAQIGSDSrvwHFV--HICAGARIGA------GVSLGQNVFVGN-----KVVIGDRCKIqNNVSVYDNVTLEE 73
Cdd:PRK14353 285 PGVTVASGAVIHAFS---HLEgaHVGEGAEVGPyarlrpGAELGEGAKVGNfvevkNAKLGEGAKV-NHLTYIGDATIGA 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   74 GVFCGPSMVFTNV--YNprslierkdQYRnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGvPARQ 151
Cdd:PRK14353 361 GANIGAGTITCNYdgFN---------KHR-TEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG-RARQ 429

                        170
                 ....*....|....*
gi 15598352  152 I---GWMSEFGEQLQ 163
Cdd:PRK14353 430 EtkpGWAKKLRERLR 444
cysE PRK11132
serine acetyltransferase; Provisional
 27-153 3.46e-11

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 60.48  E-value: 3.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   27 VHICAGARIGAGVSLGQnvfvGNKVVIGDRCKIQNNVSVYDNVTLE-EGVFCGPsmvftnvynprslierkdqyRNTLVK 105
Cdd:PRK11132 142 VDIHPAAKIGRGIMLDH----ATGIVIGETAVIENDVSILQSVTLGgTGKTSGD--------------------RHPKIR 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598352  106 KGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIG 153
Cdd:PRK11132 198 EGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-163 7.48e-11

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 60.16  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    8 SAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLG-----QNVFVGNKV-VIGDRCK---IQNNVSVYDNVTLEEG-VFC 77
Cdd:PRK14357 249 TTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGpmtriVDCEIGNNVkIIRSECEksvIEDDVSVGPFSRLREGtVLK 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   78 GPSMVFTNVYNPRSLIERK-----------------------------DQYRN--TLVKKGATLGANCTIVCGVTIGEYA 126
Cdd:PRK14357 329 KSVKIGNFVEIKKSTIGENtkaqhltylgdatvgknvnigagtitcnyDGKKKnpTFIEDGAFIGSNSSLVAPVRIGKGA 408

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15598352  127 FVGAGAVINKNVPSYALMVGvPARQI---GWMSEFGEQLQ 163
Cdd:PRK14357 409 LIGAGSVITEDVPPYSLALG-RARQIvkeGWVLKKRKEEE 447
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 6-149 1.50e-10

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 58.50  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352    6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYD------------------ 67
Cdd:PRK12461   3 HPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDepqdftykgeesrleigd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   68 ------NVTLEEGVFCGPS---------MVFTNVYNPRSLIERKDQYRNTL------VKKGATLGANCTIVCGVTIGEYA 126
Cdd:PRK12461  83 rnvireGVTIHRGTKGGGVtrigndnllMAYSHVAHDCQIGNNVILVNGALlaghvtVGDRAIISGNCLVHQFCRIGALA 162

                        170       180
                 ....*....|....*....|...
gi 15598352  127 FVGAGAVINKNVPSYALMVGVPA 149
Cdd:PRK12461 163 MMAGGSRISKDVPPYCMMAGHPT 185
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 6-184 4.09e-10

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 55.50  E-value: 4.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQ-IGSdsrvwhfVHICAGARIGAGVSL-GQNvfvgNKVVIGDRCKIQNNVSV----YDNVTLEEGVFCGP 79
Cdd:cd04645   3 DPSAFIAPNATvIGD-------VTLGEGSSVWFGAVLrGDV----NPIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGH 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  80 -SMVFTNVYNPRSLIerkdqyrntlvkkgatlGANCTIVCGVTIGEYAFVGAGAVI--NKNVPSYALMVGVPARQIGwms 156
Cdd:cd04645  72 gAVLHGCTIGDNCLI-----------------GMGAIILDGAVIGKGSIVAAGSLVppGKVIPPGSLVAGSPAKVVR--- 131

                       170       180
                ....*....|....*....|....*...
gi 15598352 157 efgeqlQLNEQGEAVCSHSGARYVLNGK 184
Cdd:cd04645 132 ------ELTDEEIAELRESAEHYVELAK 153
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 15-146 4.65e-10

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 57.81  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   15 AQIGSDSRVWHFVHIcAGARIGAGVSLG------------QNVFVGN-----KVVIGDRCKIqNNVSVYDNVTLEEGVFC 77
Cdd:PRK14356 305 AVVSSGATIHSFSHL-EGAEVGDGCSVGpyarlrpgavleEGARVGNfvemkKAVLGKGAKA-NHLTYLGDAEIGAGANI 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598352   78 GPSMVFTNvYnprsliERKDQYRnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVG 146
Cdd:PRK14356 383 GAGTITCN-Y------DGVNKHR-TVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 22-152 7.88e-10

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 55.65  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   22 RVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSV--YDNVTLEEGVFCGpSMVFTNVYNPRSLIERKDQY 99
Cdd:PRK09677  37 YIRNDGSINFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIacIESITIGRDTLIA-SKVFITDHNHGSFKHSDDFS 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598352  100 RNTL--VKKGAT-----------LGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:PRK09677 116 SPNLppDMRTLEssavvigqrvwIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 4-65 1.45e-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: 55.11  E-value: 1.45e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598352   4 YQHPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSV 65
Cdd:cd03352   9 SIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 15-154 2.30e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 55.70  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   15 AQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVgNKVVIGDRCKIqNNVSVYDNVTLEEGVFCGPSMVFTNvYNPrsliE 94
Cdd:PRK14360 314 SQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEI-KKSQLGEGSKV-NHLSYIGDATLGEQVNIGAGTITAN-YDG----V 386

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598352   95 RKDQyrnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGvPARQI---GW 154
Cdd:PRK14360 387 KKHR---TVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA-RSRQVikeNW 445
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-154 1.31e-08

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 53.40  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   13 DGAQIGSDSRVWHFVHICAGARIGAGVSLGqnVFVGNK-VVIGDRCKIQNNVSVYDnVTLEEGVFCGPSMVFTNvYNPrs 91
Cdd:PRK14352 321 SESEIGAGATVGPFTYLRPGTVLGEEGKLG--AFVETKnATIGRGTKVPHLTYVGD-ADIGEHSNIGASSVFVN-YDG-- 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598352   92 liERKdqyRNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMV-GVPARQI-GW 154
Cdd:PRK14352 395 --VNK---HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNIeGW 454
PRK10502 PRK10502
putative acyl transferase; Provisional
 16-150 1.91e-08

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 51.49  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   16 QIGSDSRVWhfVHICAGARIGAGVSL--GQNVFVGNKVVIGDRCKIQNNVSVY--DNVTLEEG-VFCGPSMVFTNVYNPR 90
Cdd:PRK10502  37 QPLYRWRAF--LLRLFGAKIGKGVVIrpSVRITYPWKLTIGDYAWIGDDVWLYnlGEITIGAHcVISQKSYLCTGSHDYS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598352   91 S----LIERKdqyrnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:PRK10502 115 DphfdLNTAP-----IVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 2-157 2.28e-08

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 51.03  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   2 SYYQHPSAIVDDGAQIGSDSRVWHFVhicagarigagVSLGQNvfvgNKVVIGDRCKIQNNVSVYDN----VTLEEGVFC 77
Cdd:cd04650   6 KAYVHPTSYVIGDVVIGELTSVWHYA-----------VIRGDN----DSIYIGKYSNVQENVSIHTDhgypTEIGDYVTI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  78 GPSMVftnVYNPRslierkdqyrntlVKKGATLGANCTIVCGVTIGEYAFVGAGAVI--NKNVPSYALMVGVPARQIGWM 155
Cdd:cd04650  71 GHNAV---VHGAK-------------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVtpGKEIPDYSLVLGVPAKVVRKL 134


                ..
gi 15598352 156 SE 157
Cdd:cd04650 135 TE 136
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-135 2.63e-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: 49.17  E-value: 2.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  51 VVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRslierkdQYRNTLVKKGATLGANCTIVCGVTIGEYAFVGA 130
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN-------EKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73


                ....*
gi 15598352 131 GAVIN 135
Cdd:cd00208  74 GAVVT 78
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 44-152 2.98e-08

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: 49.53  E-value: 2.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  44 NVFVGNKVVIGDRCKIQNNVSVY--DNVTLEEGVF-CGPSMVFTNVYNPrsLIERkdqyrNTLVKKGATLGANCTIVCGV 120
Cdd:cd05825   3 NLTIGDNSWIGEGVWIYNLAPVTigSDACISQGAYlCTGSHDYRSPAFP--LITA-----PIVIGDGAWVAAEAFVGPGV 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598352 121 TIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:cd05825  76 TIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 7-152 6.43e-08

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: 49.30  E-value: 6.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   7 PSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVydnvtleEGVFCGPSMVftnv 86
Cdd:cd03350   6 PGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI-------GGVLEPLQAT---- 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598352  87 ynprslierkdqyrNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVG------VPARQI 152
Cdd:cd03350  75 --------------PVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGeiyygrVPPGSV 132
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 40-152 6.49e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 50.39  E-value: 6.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   40 SLGQNVFV--------GNKVVIGDRCKIQNNVSVYDN--VTLEEGVFCGPSMVFTNVYNP--RSLIERKDQYRNTL-VKK 106
Cdd:PRK09527  57 TVGENAWVeppvyfsyGSNIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVTLSVTGHPvhHELRKNGEMYSFPItIGN 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15598352  107 GATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:PRK09527 137 NVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 6-150 8.76e-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: 50.10  E-value: 8.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDSRVWHFVHICAGARIG------AGVSLGQ-------------------NVFVGNKV--------- 51
Cdd:cd03352  29 GPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGdrviihSGAVIGSdgfgfapdgggwvkipqlgGVIIGDDVeiganttid 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  52 -------VIGDRCKIQNNVSVYDNVTLEEG-VFCGPSMVFTnvynprslierkdqyrNTLVKKGATLGANCTIVCGVTIG 123
Cdd:cd03352 109 rgalgdtVIGDGTKIDNLVQIAHNVRIGENcLIAAQVGIAG----------------STTIGDNVIIGGQVGIAGHLTIG 172

                       170       180
                ....*....|....*....|....*..
gi 15598352 124 EYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:cd03352 173 DGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 29-134 2.28e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   29 ICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGpsmvftnvynprslierkdqyRNTlvkkga 108
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIG---------------------ADC------ 155

                         90       100
                 ....*....|....*....|....*.
gi 15598352  109 TLGANCTIVCGVTIGEYAFVGAGAVI 134
Cdd:PRK00892 156 RLHANVTIYHAVRIGNRVIIHSGAVI 181
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 36-152 1.02e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 46.73  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   36 GAGVSLGQNVFVGNKVVIGDRCKIQnnvsVYDNVTLEEGVFcgpsmVFTNVYnPRSLIERKDQYRntlVKKGATLGAN-- 113
Cdd:PRK10092  71 GYNIFLGNNFYANFDCVMLDVCPIR----IGDNCMLAPGVH-----IYTATH-PLDPVARNSGAE---LGKPVTIGNNvw 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15598352  114 ----CTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQI 152
Cdd:PRK10092 138 iggrAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 26-127 2.93e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.86  E-value: 2.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  26 FVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFcgpsmvftnvynprslierkdqyrntlVK 105
Cdd:cd03352   1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVT---------------------------IY 53

                        90       100
                ....*....|....*....|..
gi 15598352 106 KGATLGANCTIVCGVTIGEYAF 127
Cdd:cd03352  54 EGCIIGDRVIIHSGAVIGSDGF 75
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 35-124 4.12e-06

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: 42.95  E-value: 4.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  35 IGAGVSLGQNVFVGNKVvIGDRCKIQNNVS-----VYDNVTLEEGVFCGPSMVFTNVynprslierkdqyrntLVKKGAT 109
Cdd:cd05787   2 IGRGTSIGEGTTIKNSV-IGRNCKIGKNVVidnsyIWDDVTIEDGCTIHHSIVADGA----------------VIGKGCT 64

                        90
                ....*....|....*
gi 15598352 110 LGANCTIVCGVTIGE 124
Cdd:cd05787  65 IPPGSLISFGVVIGD 79
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 2-157 7.44e-06

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: 43.90  E-value: 7.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   2 SYYQHPSAIVddgaqIGSdsrvwhfVHICAGARIGAGVSLGQNvfvGNKVVIGDRCKIQNNVSVY----DNVTLEEGVFC 77
Cdd:cd04745   6 SSFVHPTAVL-----IGD-------VIIGKNCYIGPHASLRGD---FGRIVIRDGANVQDNCVIHgfpgQDTVLEENGHI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  78 GPSMVftnVYNPRslIERkdqyrNTLVkkgatlGANCTIVCGVTIGEYAFVGAGAVI--NKNVPSYALMVGVPARQIGWM 155
Cdd:cd04745  71 GHGAI---LHGCT--IGR-----NALV------GMNAVVMDGAVIGEESIVGAMAFVkaGTVIPPRSLIAGSPAKVIREL 134


                ..
gi 15598352 156 SE 157
Cdd:cd04745 135 SD 136
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 11-145 1.36e-05

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 44.58  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   11 VDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQnvFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPR 90
Cdd:PRK14358 319 VLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGN--FVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVN 396

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15598352   91 slierKDQYRntlVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMV 145
Cdd:PRK14358 397 -----KHQSK---VGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAV 443
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 9-76 3.11e-05

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: 40.70  E-value: 3.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598352   9 AIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLG--------QNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVF 76
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 34-130 3.57e-05

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: 40.69  E-value: 3.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  34 RIGAGVSLGQNVFVGNkVVIGDRCKIQNNVSVYDnvtleegvfcgpSMVFTNVYnprslIERKDQYRNTLVKKGATLGAN 113
Cdd:cd03356   1 LIGESTVIGENAIIKN-SVIGDNVRIGDGVTITN------------SILMDNVT-----IGANSVIVDSIIGDNAVIGEN 62

                        90
                ....*....|....*..
gi 15598352 114 CTIVCGVTIGEYAFVGA 130
Cdd:cd03356  63 VRVVNLCIIGDDVVVED 79
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-155 4.80e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.81  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   11 VDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNkVVIGDRCKIQNNvSVYDNVTLEEGVFCGP------SMVFT 84
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAG-SVLEDSVVGDDVAIGPmahlrpGTELS 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   85 NVYNPRSLIERKDQYRNTLVKKG-------ATLGANCTIVCG-------------------------------VTIGEYA 126
Cdd:PRK14355 343 AHVKIGNFVETKKIVMGEGSKAShltylgdATIGRNVNIGCGtitcnydgvkkhrtvieddvfvgsdvqfvapVTVGRNS 422

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15598352  127 FVGAGAVINKNVPSYALMVGvPARQI---GWM 155
Cdd:PRK14355 423 LIAAGTTVTKDVPPDSLAIA-RSPQVnkeGWK 453
PRK10191 PRK10191
putative acyl transferase; Provisional
 103-150 1.63e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 1.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15598352  103 LVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPAR 150
Cdd:PRK10191  94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKAR 141
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 9-88 1.72e-04

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: 40.87  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   9 AIVDDGAQIGSDsrvwhfVHICAGARIGaGV-SLGQNvfvgNKVVIGDRCKIQNN------VSVYDNVTLEEGVFCGPSm 81
Cdd:COG2171 139 ATVGSCAQIGKN------VHLSGGAGIG-GVlEPLQA----APVIIEDNCFIGARsgvvegVIVGEGAVLGAGVYLTAS- 206


                ....*..
gi 15598352  82 vfTNVYN 88
Cdd:COG2171 207 --TKIYD 211
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 39-134 3.68e-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: 39.70  E-value: 3.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  39 VSLGQNVFVGNKVVIGDrckiqnNVSVYDNVTLEEGVFCGPsmvftnvynprslierkdqyrNTLVKKGATLGANCTIVC 118
Cdd:cd03352   2 AKIGENVSIGPNAVIGE------GVVIGDGVVIGPGVVIGD---------------------GVVIGDDCVIHPNVTIYE 54

                        90
                ....*....|....*.
gi 15598352 119 GVTIGEYAFVGAGAVI 134
Cdd:cd03352  55 GCIIGDRVIIHSGAVI 70
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 10-79 4.77e-04

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: 37.61  E-value: 4.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  10 IVDDGAQIGSDSRVWHFVhICAGARIGAGVS-----LGQNVFVGNKV-----VIGDRCKIQNNVSVYDNVTLEEGVFCGP 79
Cdd:cd03356   1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTitnsiLMDNVTIGANSvivdsIIGDNAVIGENVRVVNLCIIGDDVVVED 79
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 37-166 6.43e-04

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: 38.73  E-value: 6.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352  37 AGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPsmvftnvynpRSLIERKDQYRNTLVkkgatlGANCTI 116
Cdd:cd03359  41 ATVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGE----------NCVVNAAQIGSYVHI------GKNCVI 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15598352 117 VCGVTIGEYAFVGAGAVINKN--VPSYALMVGVPARQIGWMSEFGEQLQLNE 166
Cdd:cd03359 105 GRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQELMEEE 156
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 6-134 7.07e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 38.34  E-value: 7.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   6 HPSAIVDDGAQIGSDsrvwhfVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVsVYDNVTLEEGVFCGPSMVFTN 85
Cdd:cd05636  21 GEGAIVRSGAYIEGP------VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI-IMDGTKVPHLNYVGDSVLGEN 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598352  86 VY--------NPRSL-----IERKDQYRNTLVKK-------GATLGANCTIVCGVTIGEYAFVGAGAVI 134
Cdd:cd05636  94 VNlgagtitaNLRFDdkpvkVRLKGERVDTGRRKlgaiigdGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 6-71 1.09e-03

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: 36.46  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598352   6 HPSAIVDDGAQIGSDSRVWHFVHICA--GARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTL 71
Cdd:cd00208  10 HPKAVIRGPVVIGDNVNIGPGAVIGAatGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-154 2.17e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598352   14 GAQIGSDSRVWHFVHIcAGARIGAGVSLGQNVFVGNkVVIGDRCKIQNNVSV--YDNVtleegvfcgpsmvftNVYNprs 91
Cdd:PRK09451 335 GAELAEGAHVGNFVEM-KKARLGKGSKAGHLTYLGD-AEIGDNVNIGAGTITcnYDGA---------------NKFK--- 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598352   92 lierkdqyrnTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVG-VPARQI-GW 154
Cdd:PRK09451 395 ----------TIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISrVPQRHIqGW 449
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 106-138 4.51e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 4.51e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 15598352  106 KGATLGANCTIVCGVTIGEYAFVGAGAVINKNV 138
Cdd:PRK00892 117 EGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
 
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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