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Conserved domains on  [gi|517795074|ref|WP_018965282|]
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acyltransferase [Porphyromonas gulae]

Protein Classification

acyltransferase( domain architecture ID 10444459)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to O-antigen biosynthesis protein WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid

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 ...
 32-150 2.59e-64

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: 193.87  E-value: 2.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  32 VGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCVFTNVINPRAFIERKSEYRSTHLREGVSIGANA 111
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517795074 112 TILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
11-39 3.10e-03

Bacterial transferase hexapeptide (six repeats);


:

Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 517795074   11 GCVLGQGTRVWHFSHLMGGAEVGENCNIG 39
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
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 ...
 32-150 2.59e-64

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: 193.87  E-value: 2.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  32 VGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCVFTNVINPRAFIERKSEYRSTHLREGVSIGANA 111
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517795074 112 TILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
29-154 1.33e-35

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 121.52  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  29 GAEVGENCNIGQNVVI-MSGVRLGRGCKVQNNVSLYS--GVVCEDYVFLGPSCVFTNVINPRAFIERKSEY-RSTHLREG 104
Cdd:COG0110    8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517795074 105 VSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIGWVSR 154
Cdd:COG0110   88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 2-146 6.99e-27

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: 101.03  E-value: 6.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074    2 IHPTAIVEDGCVLGQGTRVwhfshlMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGpscvft 81
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVI------MAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIG------ 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074   82 nvinprafierkseyrsthlrEGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPA 146
Cdd:TIGR03570 158 ---------------------EGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-150 2.16e-21

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 87.85  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLysGVVCEDYVFLG-PSCV 79
Cdd:PRK05289   4 KIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI--GEDPQDLKYKGePTRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  80 ftnVINPRAFIeRksEY----RST-------------------------HLREGVSIGANATI--------------LCG 116
Cdd:PRK05289  82 ---VIGDNNTI-R--EFvtinRGTvqgggvtrigdnnllmayvhvahdcVVGNHVILANNATLaghvevgdyaiiggLTA 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 517795074 117 I----TIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:PRK05289 156 VhqfvRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
11-39 3.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 517795074   11 GCVLGQGTRVWHFSHLMGGAEVGENCNIG 39
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
32-64 3.15e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 517795074   32 VGENCNIGQNVVImsGVRLGRGCKVQNNVSLYS 64
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
 
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 ...
 32-150 2.59e-64

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: 193.87  E-value: 2.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  32 VGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCVFTNVINPRAFIERKSEYRSTHLREGVSIGANA 111
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517795074 112 TILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
29-154 1.33e-35

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 121.52  E-value: 1.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  29 GAEVGENCNIGQNVVI-MSGVRLGRGCKVQNNVSLYS--GVVCEDYVFLGPSCVFTNVINPRAFIERKSEY-RSTHLREG 104
Cdd:COG0110    8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517795074 105 VSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIGWVSR 154
Cdd:COG0110   88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 2-146 6.99e-27

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: 101.03  E-value: 6.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074    2 IHPTAIVEDGCVLGQGTRVwhfshlMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGpscvft 81
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVI------MAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIG------ 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074   82 nvinprafierkseyrsthlrEGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPA 146
Cdd:TIGR03570 158 ---------------------EGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 31-149 1.22e-24

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: 92.52  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  31 EVGENCNIGQNVVI--MSGVRLGRGCKVQNNVSLYSGvvcedyvflgpscvFTNVINPRAFIERKSEYRSTHLREGVSIG 108
Cdd:cd04647    3 SIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDH--------------NHDIDDPERPIEQGVTSAPIVIGDDVWIG 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 517795074 109 ANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:cd04647   69 ANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-145 1.58e-24

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: 94.86  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVwhfshlMGGAEVGENCNIGQNVVIMSGVRLGRGCKVqnnvslysgvvcEDYVFLGPSCVFT 81
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVI------MAGAVINPDARIGDNVIINTGAVIGHDCVI------------GDFVHIAPGVVLS 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074  82 -NVinprafierkseyrstHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNP 145
Cdd:cd03360  149 gGV----------------TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 20-150 1.66e-22

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: 88.99  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  20 VWHFSHLMGGAEVGENCNIGQNVVIM--SGVRLGRGCKVQNNVSLYSGVVcedyvfLGPScvftnvinprafiERKSEYR 97
Cdd:COG1045   56 LSERARFLTGIDIHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVT------LGGT-------------GKEKGKR 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517795074  98 STHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:COG1045  117 HPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 1-150 3.97e-22

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: 89.80  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLysGVVCED--------YV 72
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI--GEAPQDlkykgeptRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  73 FLGPSCVF-TNV-INpRAFIERKSEYR---------STHL----REG--------------VSIGANATI--LCGI---- 117
Cdd:cd03351   79 EIGDNNTIrEFVtIH-RGTAQGGGVTRignnnllmaYVHVahdcVIGnnvilannatlaghVEIGDYAIIggLSAVhqfc 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517795074 118 TIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:cd03351  158 RIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 1-147 7.50e-22

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: 88.92  E-value: 7.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLysGVVCED--------YV 72
Cdd:COG1043    3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI--GEEPQDlkykgeptRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  73 FLGPSCVF-TNV-INpRAFIERKSEYR---------STHL----REG--------------VSIGANATI--LCGI---- 117
Cdd:COG1043   81 EIGDNNTIrEFVtIH-RGTVQGGGVTRigddnllmaYVHVahdcVVGnnvilannatlaghVEVGDHAIIggLSAVhqfv 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 517795074 118 TIGAYAMVGAGAVVIRDVPPYALVVGNPAR 147
Cdd:COG1043  160 RIGAHAMVGGGSGVVKDVPPYVLAAGNPAR 189
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-150 2.16e-21

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 87.85  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLysGVVCEDYVFLG-PSCV 79
Cdd:PRK05289   4 KIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI--GEDPQDLKYKGePTRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  80 ftnVINPRAFIeRksEY----RST-------------------------HLREGVSIGANATI--------------LCG 116
Cdd:PRK05289  82 ---VIGDNNTI-R--EFvtinRGTvqgggvtrigdnnllmayvhvahdcVVGNHVILANNATLaghvevgdyaiiggLTA 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 517795074 117 I----TIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:PRK05289 156 VhqfvRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 31-149 1.96e-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: 80.54  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  31 EVGENCNIGQNVVIM--SGVRLGrgckvqnnvslysgvvceDYVFLGPSCVFTNVINPRAFIERKS--EY-RSTHLREGV 105
Cdd:cd03357   64 HIGDNFYANFNCTILdvAPVTIG------------------DNVLIGPNVQIYTAGHPLDPEERNRglEYaKPITIGDNV 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517795074 106 SIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:cd03357  126 WIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 22-151 8.36e-19

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: 78.35  E-value: 8.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  22 HFSHLMGGAEVGENCNIGQNVVIMSGV--RLgrgckvqnnvslysgvvceDYVFLGPSCVFTNVINPRAFIERKSEYRST 99
Cdd:cd03349   14 DCDVGGDKLSIGKFCSIAPGVKIGLGGnhPT-------------------DWVSTYPFYIFGGEWEDDAKFDDWPSKGDV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517795074 100 HLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIGW 151
Cdd:cd03349   75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 29-145 9.93e-18

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: 74.40  E-value: 9.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  29 GAEVGENCNIGQNVVIM--SGVRLGRGCKVQNNVSLYSGVVcedyvflgpscvftnvINPRAFIERKseyRSTHLREGVS 106
Cdd:cd03354    2 GIDIHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVT----------------LGGKGKGGGK---RHPTIGDNVV 62

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517795074 107 IGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNP 145
Cdd:cd03354   63 IGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 2-158 1.04e-17

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: 78.07  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074    2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSL--------YSGVvcEDYVF 73
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIggvpqdlkYKGE--KTRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   74 LGPSCVftnvINPRAFIER--KSEYRST------------HLREGVSIG-----ANATILCG------------------ 116
Cdd:TIGR01852  79 IGDNNT----IREFVTINRgtASGGGVTrignnnllmaysHIAHDCVVGnhvilANNATLAGhvevgdyaiigglvavhq 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 517795074  117 -ITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIGwVSRVGHR 158
Cdd:TIGR01852 155 fVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRG-LNIVGLR 196
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-147 1.45e-16

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: 75.82  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCV-- 79
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVig 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  80 -----FTNVINPRAF---------------------IERKSeYRSTHLREG------------VSIGANaTILCG----- 116
Cdd:COG1044  179 adgfgFAPDEDGGWVkipqlgrvvigddveiganttIDRGA-LGDTVIGDGtkidnlvqiahnVRIGEH-TAIAAqvgia 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517795074 117 --------------------ITIGAYAMVGAGAVVIRDVPPYALVVGNPAR 147
Cdd:COG1044  257 gstkigdnvviggqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 1-146 1.29e-15

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 72.36  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSL--------YSGVvcEDYV 72
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftYKGE--ESRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  73 FLGPSCVF---------------TNVINPRAFIERkseyrsTHLREGVSIG-----ANATILCG---------------- 116
Cdd:PRK12461  79 EIGDRNVIregvtihrgtkgggvTRIGNDNLLMAY------SHVAHDCQIGnnvilVNGALLAGhvtvgdraiisgnclv 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517795074 117 ---ITIGAYAMVGAGAVVIRDVPPYALVVGNPA 146
Cdd:PRK12461 153 hqfCRIGALAMMAGGSRISKDVPPYCMMAGHPT 185
PLN02694 PLN02694
serine O-acetyltransferase
 2-150 2.46e-15

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 72.37  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTrvwhfshlmgGAEVGENCNIGQNVVIMSGVRLGRgckvqnnvslySGVVCEDyvflgpscvft 81
Cdd:PLN02694 163 IHPAAKIGKGILFDHAT----------GVVIGETAVIGNNVSILHHVTLGG-----------TGKACGD----------- 210

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517795074  82 nvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:PLN02694 211 ---------------RHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG 264
PLN02739 PLN02739
serine acetyltransferase
 2-184 3.09e-15

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 72.38  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTrvwhfshlmgGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNvslysgvvcedyvflgpscvft 81
Cdd:PLN02739 208 IHPAARIGKGILLDHGT----------GVVIGETAVIGDRVSILHGVTLGGTGKETGD---------------------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  82 nvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIGWVSRVGHRLSF 161
Cdd:PLN02739 256 ---------------RHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTM 320

                        170       180
                 ....*....|....*....|....
gi 517795074 162 D-DKGMAVCPETGERYREVEETGT 184
Cdd:PLN02739 321 EyDATREFFQNVAVAYRETIPNGS 344
cysE PRK11132
serine acetyltransferase; Provisional
 2-150 4.36e-15

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 71.27  E-value: 4.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTrvwhfshlmgGAEVGENCNIGQNVVIMSGVRLGRgckvqnnvslySGVVCEDyvflgpscvft 81
Cdd:PRK11132 144 IHPAAKIGRGIMLDHAT----------GIVIGETAVIENDVSILQSVTLGG-----------TGKTSGD----------- 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517795074  82 nvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:PRK11132 192 ---------------RHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
PLN02357 PLN02357
serine acetyltransferase
 2-150 1.75e-14

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 70.30  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTrvwhfshlmgGAEVGENCNIGQNVVIMSGVRLGRgckvqnnvslySGVVCEDyvflgpscvft 81
Cdd:PLN02357 229 IHPGAKIGQGILLDHAT----------GVVIGETAVVGNNVSILHNVTLGG-----------TGKQSGD----------- 276

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517795074  82 nvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRIG 150
Cdd:PLN02357 277 ---------------RHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 2-149 4.84e-14

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: 66.28  E-value: 4.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLgqgtrvwhfshlMGGAEVGENCNIGQNVVI---MSGVRLGRGCKVQNNVSL----YSGVVCEDYVFL 74
Cdd:cd04645    2 IDPSAFIAPNATV------------IGDVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVLhvdpGYPTIIGDNVTV 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517795074  75 GPSCVFtnvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVI--RDVPPYALVVGNPARRI 149
Cdd:cd04645   70 GHGAVL----------------HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVV 130
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 2-149 6.15e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 66.20  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLgqgtrvwhfshlMGGAEVGENCNIGQNVVI---MSGVRLGRGCKVQNNVSLY----SGVVCEDYVFL 74
Cdd:COG0663   13 IHPSAFVAPTAVV------------IGDVTIGEDVSVWPGAVLrgdVGPIRIGEGSNIQDGVVLHvdpgYPLTIGDDVTI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517795074  75 GPSCVFtnvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVI--RDVPPYALVVGNPARRI 149
Cdd:COG0663   81 GHGAIL----------------HGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVV 141
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 2-147 8.02e-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: 8.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYS----------------- 64
Cdd:cd03352   10 IGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgfapdgggwvkipq 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  65 --GVVCEDYVFLGPSCVftnvinprafIERKSeYRSTHLREG------------VSIGANaTILCG-------------- 116
Cdd:cd03352   90 lgGVIIGDDVEIGANTT----------IDRGA-LGDTVIGDGtkidnlvqiahnVRIGEN-CLIAAqvgiagsttigdnv 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 517795074 117 -----------ITIGAYAMVGAGAVVIRDVPPYALVVGNPAR 147
Cdd:cd03352  158 iiggqvgiaghLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-113 2.47e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.00  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVcedyvfLGPSCvft 81
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVR------IGNRV--- 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 517795074  82 nVINPRA--------FIERKSEYR------STHLREGVSIGANATI 113
Cdd:PRK00892 174 -IIHSGAvigsdgfgFANDRGGWVkipqlgRVIIGDDVEIGANTTI 218
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 31-149 5.31e-12

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: 59.54  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  31 EVGENCNIGQNVVIMSgvrLGRgckvqnnVSLYSGVVCEDYVFLgpsCVFTNVINPRAFIERKseyRSTHLREGVSIGAN 110
Cdd:cd05825    5 TIGDNSWIGEGVWIYN---LAP-------VTIGSDACISQGAYL---CTGSHDYRSPAFPLIT---APIVIGDGAWVAAE 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517795074 111 ATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:cd05825   69 AFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-155 1.22e-11

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: 62.35  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   8 VEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVImSGVRLGRGCKVQNnvSLYSGVVCEDYVFLGPscvFT-----N 82
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKY--SVIEDAVVGAGATVGP---FArlrpgT 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  83 VINPRA----FIERKseyRST--------HLR--------EGVSIGAnATILC------------------G-------- 116
Cdd:COG1207  337 VLGEGVkignFVEVK---NSTigegskvnHLSyigdaeigEGVNIGA-GTITCnydgvnkhrtvigdgafiGsntnlvap 412

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 517795074 117 ITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI--GWVSRV 155
Cdd:COG1207  413 VTIGDGATIGAGSTITKDVPAGALAIARARQRNieGWVRPK 453
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-164 1.78e-11

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 61.68  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHP-TAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVImsgvrlgRGCKVQNNVSLYSGVVCEDYVF------ 73
Cdd:PRK14355 257 LIDPeTTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-------KGCRIGDDVTVKAGSVLEDSVVgddvai 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  74 -----LGPSCVFTNVINPRAFIERKseyrSTHLREG-----------VSIGANATILCG--------------------- 116
Cdd:PRK14355 330 gpmahLRPGTELSAHVKIGNFVETK----KIVMGEGskashltylgdATIGRNVNIGCGtitcnydgvkkhrtvieddvf 405

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517795074 117 ----------ITIGAYAMVGAGAVVIRDVPPYALVVGnparRIGWVSRVGHRLSFDDK 164
Cdd:PRK14355 406 vgsdvqfvapVTVGRNSLIAAGTTVTKDVPPDSLAIA----RSPQVNKEGWKLRKKDK 459
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-143 9.16e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 59.88  E-value: 9.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  11 GCVLGQGTRVWHFSHLMGGAEVGENCNIGqNVVIMSGVRLGRGCKVqNNVSlYSGvvceDyVFLGPScvfTNV------I 84
Cdd:PRK14353 303 GAHVGEGAEVGPYARLRPGAELGEGAKVG-NFVEVKNAKLGEGAKV-NHLT-YIG----D-ATIGAG---ANIgagtitC 371

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517795074  85 NPRAFierkSEYRsTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVG 143
Cdd:PRK14353 372 NYDGF----NKHR-TEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
PRK10502 PRK10502
putative acyl transferase; Provisional
 38-149 1.07e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 57.65  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  38 IGQNVVIMSGVR--------LGRGCKVQNNVSLYSgvvcEDYVFLGPSCVftnvINPRAFIERKS-EYRSTH-------- 100
Cdd:PRK10502  54 IGKGVVIRPSVRitypwkltIGDYAWIGDDVWLYN----LGEITIGAHCV----ISQKSYLCTGShDYSDPHfdlntapi 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517795074 101 -LREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:PRK10502 126 vIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 2-143 1.58e-10

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: 57.43  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEdGCVLGQGTRVWHFSHLMGGAEVGENCNIGqNVVIMSGVRLGRGCKVqNNVSlYSG--VVCEDyVFLGPSCV 79
Cdd:cd03353   59 IKASSVIE-GAVIGNGATVGPFAHLRPGTVLGEGVHIG-NFVEIKKSTIGEGSKA-NHLS-YLGdaEIGEG-VNIGAGTI 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517795074  80 FTNVinprafiERKSEYRsTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVG 143
Cdd:cd03353  134 TCNY-------DGVNKHR-TVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-151 2.75e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 58.40  E-value: 2.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  12 CVLGQGTRVWHFSHLMGGAEVGENCNIGqNVVIMSGVRLGRGCKVqNNVSlysgvvcedyvFLGPSCVFTNV------IN 85
Cdd:PRK14360 314 SQIGDGVKIGPYAHLRPEAQIGSNCRIG-NFVEIKKSQLGEGSKV-NHLS-----------YIGDATLGEQVnigagtIT 380

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517795074  86 prAFIERKSEYRsTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI--GW 151
Cdd:PRK14360 381 --ANYDGVKKHR-TVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIkeNW 445
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 2-149 2.92e-10

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: 56.04  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEvgencnigqnvvimsGVRLGRGCKVQNNVSLYS--GVVCE--DYVFLGPS 77
Cdd:cd04650    9 VHPTSYVIGDVVIGELTSVWHYAVIRGDND---------------SIYIGKYSNVQENVSIHTdhGYPTEigDYVTIGHN 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517795074  78 CVFtnvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVI--RDVPPYALVVGNPARRI 149
Cdd:cd04650   74 AVV----------------HGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVV 131
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-143 3.46e-10

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 58.20  E-value: 3.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  13 VLGQGTRVWHFSHLmGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCED-----YVFLGPScvftnVINPR 87
Cdd:PRK14356 306 VVSSGATIHSFSHL-EGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGakanhLTYLGDA-----EIGAG 379

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074  88 AFI---------ERKSEYRsTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVG 143
Cdd:PRK14356 380 ANIgagtitcnyDGVNKHR-TVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 48-131 8.41e-10

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: 53.02  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  48 VRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCVFTNVINPRafierksEYRSTHLREGVSIGANATILCGITIGAYAMVGA 127
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN-------EKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73


                 ....
gi 517795074 128 GAVV 131
Cdd:cd00208   74 GAVV 77
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 2-154 2.89e-09

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: 53.53  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLgqgtrvwhfshlMGGAEVGENCNIGQNVVI---MSGVRLGRGCKVQNNVSLYSG----VVCEDYVFL 74
Cdd:cd04745    3 VDPSSFVHPTAVL------------IGDVIIGKNCYIGPHASLrgdFGRIVIRDGANVQDNCVIHGFpgqdTVLEENGHI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  75 GPSCVFtnvinprafierkseyRSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIR--DVPPYALVVGNPARRIGWV 152
Cdd:cd04745   71 GHGAIL----------------HGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIREL 134


                 ..
gi 517795074 153 SR 154
Cdd:cd04745  135 SD 136
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 67-149 5.93e-09

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 52.89  E-value: 5.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  67 VCE----DYVFLGPSCVFTNVINPRAFIERKS--EY-RSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYA 139
Cdd:PRK10092  91 VCPirigDNCMLAPGVHIYTATHPLDPVARNSgaELgKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNV 170

                         90
                 ....*....|
gi 517795074 140 LVVGNPARRI 149
Cdd:PRK10092 171 VVGGNPARII 180
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-154 6.31e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.38  E-value: 6.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  23 FSHLMGGAEVGENCNIGqNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDyVFLGP---SCVFTNVINPRAFIErkseyrst 99
Cdd:PRK14357 318 FSRLREGTVLKKSVKIG-NFVEIKKSTIGENTKAQHLTYLGDATVGKN-VNIGAgtiTCNYDGKKKNPTFIE-------- 387

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517795074 100 hlrEGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNpARRI---GWVSR 154
Cdd:PRK14357 388 ---DGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGR-ARQIvkeGWVLK 441
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-157 9.38e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 53.68  E-value: 9.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  13 VLGQGTRVWHFSHlMGGAEVGENCNIGQNVVimsgvrlgrgckvqnnVSLYSGV-----VCEDYVFlgpscvftnvinpr 87
Cdd:PRK14354 353 TIGEGTKVSHLTY-IGDAEVGENVNIGCGTI----------------TVNYDGKnkfktIIGDNAF-------------- 401

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517795074  88 afierkseyrsthlregvsIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNpARRI---GWVSRVGH 157
Cdd:PRK14354 402 -------------------IGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIAR-ARQVnkeGYVKKLPH 454
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-154 1.56e-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: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  10 DGCVLGQGTRVWHFSHLMGGAEVGENCNIGQnVVIMSGVRLGRGCKVQNnvsL-YSG-VVCEDYVFLGPSCVFTNVINpr 87
Cdd:PRK14352 321 SESEIGAGATVGPFTYLRPGTVLGEEGKLGA-FVETKNATIGRGTKVPH---LtYVGdADIGEHSNIGASSVFVNYDG-- 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517795074  88 afiERKSEyrsTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVV-GNPARRI-GWVSR 154
Cdd:PRK14352 395 ---VNKHR---TTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNIeGWVQR 457
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-151 2.93e-08

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 52.34  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGcVLGQGTRVWHFSHLMGGAEVGENCNIGqNVVIMSGVRLGRGCKVqNNVSLYSGVVCEDYVFLGPSCVFT 81
Cdd:PRK09451 309 ISPYSVVEDA-NLGAACTIGPFARLRPGAELAEGAHVG-NFVEMKKARLGKGSKA-GHLTYLGDAEIGDNVNIGAGTITC 385

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517795074  82 NVINPRAFierkseyrSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGN-PARRI-GW 151
Cdd:PRK09451 386 NYDGANKF--------KTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRvPQRHIqGW 449
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-154 1.25e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 50.75  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   6 AIVEDGcVLGQGTRVWHFShLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQN-----NVSLYSGVVCEDYVFLGPSCVF 80
Cdd:PRK14358 301 SVVTDS-VLHEGAVIKPHS-VLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGNfvetkNARLDAGVKAGHLAYLGDVTIG 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  81 --TNVINPR--AFIERKSEYRSThLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI--GWVSR 154
Cdd:PRK14358 379 aeTNVGAGTivANFDGVNKHQSK-VGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNleGWSRR 457
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 30-149 2.32e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 48.85  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  30 AEVGENCNIGQNVVIMSG--VRLGRGCKVQNNVSLYSG--VVCEDYVFLGPSCVFTNVINPRAFIERKS-EYRSTHLREG 104
Cdd:PRK09527  56 ATVGENAWVEPPVYFSYGsnIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVTLSVTGHPVHHELRKNgEMYSFPITIG 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 517795074 105 --VSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:PRK09527 136 nnVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 2-131 4.33e-07

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: 47.58  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCED-------YV-- 72
Cdd:cd05636    8 VEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGtkvphlnYVgd 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074  73 -FLGPSCVF---TNVINPR-----AFIERKSEYRSTHLR-------EGVSIGANATILCGITIGAYAMVGAGAVV 131
Cdd:cd05636   88 sVLGENVNLgagTITANLRfddkpVKVRLKGERVDTGRRklgaiigDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
PRK10191 PRK10191
putative acyl transferase; Provisional
 100-147 5.80e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 46.81  E-value: 5.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 517795074 100 HLREGVSIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPAR 147
Cdd:PRK10191  94 HIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKAR 141
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 31-149 6.33e-07

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 47.56  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  31 EVGENCNIGQNVVIMS--GVRLGRgckvqnNVSLYSGVVCEDY---VFLGPSCVFTNVINPrafIERKSEYRSTHLREGV 105
Cdd:PRK09677  67 FFGDNVQVNDYVHIACieSITIGR------DTLIASKVFITDHnhgSFKHSDDFSSPNLPP---DMRTLESSAVVIGQRV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517795074 106 SIGANATILCGITIGAYAMVGAGAVVIRDVPPYALVVGNPARRI 149
Cdd:PRK09677 138 WIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-147 4.65e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.90  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQGTRVWhfshlmGGAEVGENCNIGQNVVIMSGVRLG---------RGC--KV-QNnvslySGVVCE 69
Cdd:PRK00892 139 IGAGAVIGDGVKIGADCRLH------ANVTIYHAVRIGNRVIIHSGAVIGsdgfgfandRGGwvKIpQL-----GRVIIG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  70 DYVFLGPSCVftnvinprafIERKSeYRSTHLREG------------VSIGANaTILCG--------------------- 116
Cdd:PRK00892 208 DDVEIGANTT----------IDRGA-LDDTVIGEGvkidnlvqiahnVVIGRH-TAIAAqvgiagstkigrycmiggqvg 275

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517795074 117 ----ITIGAYAMVGAGAVVIRDVPPYALVVGN-PAR 147
Cdd:PRK00892 276 iaghLEIGDGVTITAMSGVTKSIPEPGEYSSGiPAQ 311
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 1-146 7.17e-06

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: 43.91  E-value: 7.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMGGAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSLySGVVceDYVFLGPscvf 80
Cdd:cd03350    3 RVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI-GGVL--EPLQATP---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  81 tnvinprAFIErkseyrsthlrEGVSIGANATILCGITIGAYAMVGAGAVVIR---------------DVPPYALVV-GN 144
Cdd:cd03350   76 -------VIIE-----------DDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGSVVVaGS 137


                 ..
gi 517795074 145 PA 146
Cdd:cd03350  138 LP 139
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-146 1.06e-04

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 42.05  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   45 MSGVRLGRGCKVQN-NVSLYSGVVCEDYVFLGPSCVF-TNVINPRAFierKSEYrsTHLREGVSIGANATILCGITIGAY 122
Cdd:TIGR02353 595 LLGVKIGRGVYIDGtDLTERDLVTIGDDSTLNEGSVIqTHLFEDRVM---KSDT--VTIGDGATLGPGAIVLYGVVMGEG 669

                          90       100
                  ....*....|....*....|....*.
gi 517795074  123 AMVGAGAVVIR--DVPPYALVVGNPA 146
Cdd:TIGR02353 670 SVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 6-70 1.78e-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: 38.76  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517795074   6 AIVEDGCVLGQGTRVWHfSHLMGGAEVGENCNIgQNVVIMSGVRLGRGCKVQNNVSLYSGVVCED 70
Cdd:cd03356   17 SVIGDNVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 35-159 5.61e-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: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  35 NCNIGQNVVIMSGVRLGRGCKVQNNVSLYSGVVCEDYVFLGPSCVftnvinprafIERKSEYRSTHlregvsIGANATIL 114
Cdd:cd03359   42 TVSIGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCV----------VNAAQIGSYVH------IGKNCVIG 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 517795074 115 CGITIGAYAMVGAGAVVIRD--VPPYALVVGNPARRIGWVSRVGHRL 159
Cdd:cd03359  106 RRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQEL 152
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 7-59 6.35e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 37.44  E-value: 6.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517795074   7 IVEDG----CVLGQGTRVWHFSH-----LMGGAEVGENCNIgQNVVIMSGVRLGRGCKVQNN 59
Cdd:cd04651   20 IISGGtvenSVLFRGVRVGSGSVvedsvIMPNVGIGRNAVI-RRAIIDKNVVIPDGVVIGGD 80
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1-62 7.30e-04

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: 36.84  E-value: 7.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   1 MIHPTAIVEDGCVLGQGTRVWHFSHLMG--------GAEVGENCNIGQNVVIMSGVRLGRGCKVQNNVSL 62
Cdd:cd00208    8 KIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
PLN02296 PLN02296
carbonate dehydratase
 26-147 8.74e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 38.95  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074  26 LMGGAEVGENCNIGQNVVI---MSGVRLGRGCKVQNNV------SLYSGVVCE----DYVFLGPSCVFTN-VINPRAFIe 91
Cdd:PLN02296  67 VIGDVQVGRGSSIWYGCVLrgdVNSISVGSGTNIQDNSlvhvakTNLSGKVLPtiigDNVTIGHSAVLHGcTVEDEAFV- 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517795074  92 rkseyrsthlregvsiGANATILCGITIGAYAMVGAGAVVIRD--VPPYALVVGNPAR 147
Cdd:PLN02296 146 ----------------GMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 84-135 1.64e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 1.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517795074  84 INPRAFIERkseyrSTHLREGVSIGANATILCGITIGAYAMVGAGAVVIRDV 135
Cdd:PRK00892 103 IHPSAVIDP-----SAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 7-58 1.78e-03

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.02  E-value: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517795074   7 IVEDGCVLGQGTRVWHfSHLMGGAEVGENCNIgQNVVIMSGVRLGRGCKVQN 58
Cdd:cd04652   18 VIGANCKIGKRVKITN-CVIMDNVTIEDGCTL-ENCIIGNGAVIGEKCKLKD 67
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
11-39 3.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 517795074   11 GCVLGQGTRVWHFSHLMGGAEVGENCNIG 39
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
32-64 3.15e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 517795074   32 VGENCNIGQNVVImsGVRLGRGCKVQNNVSLYS 64
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
29-58 3.71e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 517795074   29 GAEVGENCNIGQNVVIMSGVRLGRGCKVQN 58
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 2-81 6.02e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 35.64  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517795074   2 IHPTAIVEDGCVLGQ-----------GTRVWHFSHLmGGAEVGENCNIGQNVV-------------------IMSGVR-- 49
Cdd:cd05636   50 IRGYTVLGDGCVVGNsvevknsiimdGTKVPHLNYV-GDSVLGENVNLGAGTItanlrfddkpvkvrlkgerVDTGRRkl 128

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517795074  50 ---LGRGCKVQNNVSLYSGVVCEDYVFLGPSCVFT 81
Cdd:cd05636  129 gaiIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
 
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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