MULTISPECIES: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [Enterobacter]
Protein Classification
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase( domain architecture ID 11479317)
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
2-340 | 0e+00 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional : Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 559.76 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
2-340 | 0e+00 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 559.76 E-value: 0e+00
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| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
3-336 | 0e+00 | ||||||
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: 513.03 E-value: 0e+00
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| lipid_A_lpxD | TIGR01853 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ... |
8-330 | 2.11e-158 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, 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. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 273834 [Multi-domain] Cd Length: 324 Bit Score: 446.35 E-value: 2.11e-158
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
109-314 | 5.96e-112 | ||||||
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: 323.59 E-value: 5.96e-112
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| LpxD | pfam04613 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ... |
23-89 | 7.45e-22 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins. Pssm-ID: 461366 [Multi-domain] Cd Length: 69 Bit Score: 87.55 E-value: 7.45e-22
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| Name | Accession | Description | Interval | E-value | ||||||
| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
2-340 | 0e+00 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 559.76 E-value: 0e+00
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| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
3-336 | 0e+00 | ||||||
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: 513.03 E-value: 0e+00
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| lipid_A_lpxD | TIGR01853 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ... |
8-330 | 2.11e-158 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, 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. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 273834 [Multi-domain] Cd Length: 324 Bit Score: 446.35 E-value: 2.11e-158
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
109-314 | 5.96e-112 | ||||||
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: 323.59 E-value: 5.96e-112
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| LpxA | COG1043 | Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
122-274 | 1.97e-32 | ||||||
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: 121.28 E-value: 1.97e-32
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| PRK05289 | PRK05289 | acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
122-274 | 4.37e-31 | ||||||
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 117.89 E-value: 4.37e-31
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| LbH_UDP-GlcNAc_AT | cd03351 | UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
122-274 | 1.32e-30 | ||||||
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: 116.38 E-value: 1.32e-30
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| lipid_A_lpxA | TIGR01852 | acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ... |
122-273 | 2.09e-28 | ||||||
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: 110.43 E-value: 2.09e-28
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| PRK12461 | PRK12461 | UDP-N-acetylglucosamine acyltransferase; Provisional |
122-273 | 8.21e-23 | ||||||
UDP-N-acetylglucosamine acyltransferase; Provisional Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 8.21e-23
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| LpxD | pfam04613 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ... |
23-89 | 7.45e-22 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins. Pssm-ID: 461366 [Multi-domain] Cd Length: 69 Bit Score: 87.55 E-value: 7.45e-22
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| LbH_AT_putative | cd03360 | Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
200-306 | 1.38e-14 | ||||||
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation. Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 71.36 E-value: 1.38e-14
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
101-263 | 3.78e-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: 70.14 E-value: 3.78e-14
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
200-306 | 6.79e-14 | ||||||
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff. Pssm-ID: 274656 [Multi-domain] Cd Length: 201 Bit Score: 69.44 E-value: 6.79e-14
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
121-258 | 1.07e-13 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 67.20 E-value: 1.07e-13
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| LbH_AT_putative | cd03360 | Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
78-258 | 7.21e-13 | ||||||
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation. Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 66.35 E-value: 7.21e-13
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
116-251 | 1.79e-12 | ||||||
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff. Pssm-ID: 274656 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 1.79e-12
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
106-263 | 3.08e-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: 66.97 E-value: 3.08e-12
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| LbH_WxcM_N_like | cd03358 | WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
130-257 | 6.96e-11 | ||||||
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity. Pssm-ID: 100048 [Multi-domain] Cd Length: 119 Bit Score: 58.67 E-value: 6.96e-11
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| PaaY | COG0663 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
88-297 | 1.82e-10 | ||||||
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 58.89 E-value: 1.82e-10
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| glmU | PRK09451 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
113-252 | 2.36e-10 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 61.20 E-value: 2.36e-10
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
135-297 | 3.70e-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: 57.81 E-value: 3.70e-10
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| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
105-273 | 1.38e-09 | ||||||
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: 56.44 E-value: 1.38e-09
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
106-263 | 1.04e-08 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 56.38 E-value: 1.04e-08
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| LbH_paaY_like | cd04745 | paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
198-306 | 1.25e-08 | ||||||
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: 1.25e-08
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| glmU | PRK14360 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
102-274 | 3.03e-08 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 54.93 E-value: 3.03e-08
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| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
100-231 | 4.78e-08 | ||||||
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: 51.82 E-value: 4.78e-08
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
145-275 | 9.94e-08 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 50.25 E-value: 9.94e-08
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
142-251 | 1.56e-07 | ||||||
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: 48.99 E-value: 1.56e-07
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| LbH_Dynactin_5 | cd03359 | Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
114-258 | 5.69e-07 | ||||||
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: 48.75 E-value: 5.69e-07
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
111-263 | 5.79e-07 | ||||||
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain. Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 48.56 E-value: 5.79e-07
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
124-263 | 1.35e-06 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 49.74 E-value: 1.35e-06
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
162-306 | 3.28e-06 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 46.02 E-value: 3.28e-06
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
200-273 | 5.09e-06 | ||||||
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: 44.75 E-value: 5.09e-06
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| PRK10092 | PRK10092 | maltose O-acetyltransferase; Provisional |
111-145 | 5.37e-06 | ||||||
maltose O-acetyltransferase; Provisional Pssm-ID: 182235 [Multi-domain] Cd Length: 183 Bit Score: 46.34 E-value: 5.37e-06
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| LbH_unknown | cd05635 | Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
116-214 | 6.04e-06 | ||||||
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain] Cd Length: 101 Bit Score: 44.19 E-value: 6.04e-06
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
110-156 | 1.04e-05 | ||||||
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: 44.71 E-value: 1.04e-05
|
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
111-145 | 1.83e-05 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 43.71 E-value: 1.83e-05
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| LbH_Dynactin_5 | cd03359 | Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
105-153 | 2.15e-05 | ||||||
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 44.13 E-value: 2.15e-05
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
110-169 | 2.58e-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: 41.85 E-value: 2.58e-05
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| LbH_G1P_AT_C_like | cd03356 | Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
111-211 | 3.10e-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: 41.84 E-value: 3.10e-05
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
111-145 | 3.59e-05 | ||||||
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: 42.44 E-value: 3.59e-05
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| LbH_WxcM_N_like | cd03358 | WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
99-181 | 3.85e-05 | ||||||
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: 42.49 E-value: 3.85e-05
|
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| DapD | COG2171 | Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
113-148 | 4.15e-05 | ||||||
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: 44.34 E-value: 4.15e-05
|
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
164-274 | 5.64e-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: 41.08 E-value: 5.64e-05
|
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
147-231 | 5.93e-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: 5.93e-05
|
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| LbH_THP_succinylT | cd03350 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
122-261 | 6.41e-05 | ||||||
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: 42.37 E-value: 6.41e-05
|
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| lacA | PRK09527 | galactoside O-acetyltransferase; Reviewed |
112-145 | 6.57e-05 | ||||||
galactoside O-acetyltransferase; Reviewed Pssm-ID: 181930 [Multi-domain] Cd Length: 203 Bit Score: 43.45 E-value: 6.57e-05
|
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| glmU | PRK14356 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
100-263 | 7.30e-05 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 44.33 E-value: 7.30e-05
|
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| glmU | PRK14358 | bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
124-252 | 9.17e-05 | ||||||
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 44.20 E-value: 9.17e-05
|
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
111-212 | 1.11e-04 | ||||||
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: 40.90 E-value: 1.11e-04
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| LbH_gamma_CA | cd00710 | Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
199-273 | 1.21e-04 | ||||||
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain. Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 41.84 E-value: 1.21e-04
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| LbH_paaY_like | cd04745 | paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
126-297 | 1.29e-04 | ||||||
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity. Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 41.58 E-value: 1.29e-04
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
110-138 | 1.40e-04 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 38.47 E-value: 1.40e-04
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
163-275 | 1.63e-04 | ||||||
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: 40.52 E-value: 1.63e-04
|
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| LbH_MAT_GAT | cd03357 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
113-152 | 1.97e-04 | ||||||
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: 41.25 E-value: 1.97e-04
|
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| PLN02694 | PLN02694 | serine O-acetyltransferase |
20-164 | 2.17e-04 | ||||||
serine O-acetyltransferase Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 42.32 E-value: 2.17e-04
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
112-210 | 2.44e-04 | ||||||
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: 39.10 E-value: 2.44e-04
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
200-268 | 2.49e-04 | ||||||
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 42.71 E-value: 2.49e-04
|
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| CysE | COG1045 | Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
106-172 | 2.71e-04 | ||||||
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: 41.22 E-value: 2.71e-04
|
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
106-273 | 2.74e-04 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 42.42 E-value: 2.74e-04
|
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
111-145 | 2.77e-04 | ||||||
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: 39.73 E-value: 2.77e-04
|
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
207-295 | 2.77e-04 | ||||||
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: 39.73 E-value: 2.77e-04
|
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
203-292 | 2.86e-04 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 42.42 E-value: 2.86e-04
|
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| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
112-154 | 3.05e-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: 39.37 E-value: 3.05e-04
|
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
222-250 | 3.17e-04 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 37.32 E-value: 3.17e-04
|
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| LbH_unknown | cd05635 | Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
224-275 | 3.58e-04 | ||||||
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain] Cd Length: 101 Bit Score: 39.18 E-value: 3.58e-04
|
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
106-164 | 4.69e-04 | ||||||
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: 38.96 E-value: 4.69e-04
|
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
145-174 | 6.07e-04 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 36.55 E-value: 6.07e-04
|
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| LbH_FBP | cd04650 | Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ... |
105-148 | 6.80e-04 | ||||||
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: 39.48 E-value: 6.80e-04
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| glmU | PRK14353 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
120-273 | 8.00e-04 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 41.00 E-value: 8.00e-04
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
124-225 | 1.02e-03 | ||||||
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: 37.80 E-value: 1.02e-03
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
203-286 | 1.03e-03 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 40.59 E-value: 1.03e-03
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| BCL_like | cd05919 | Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
5-136 | 1.12e-03 | ||||||
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP. Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 40.52 E-value: 1.12e-03
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
113-143 | 1.28e-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: 37.23 E-value: 1.28e-03
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| LbH_gamma_CA | cd00710 | Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
118-264 | 1.30e-03 | ||||||
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain. Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 39.15 E-value: 1.30e-03
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
100-152 | 1.62e-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: 36.84 E-value: 1.62e-03
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
142-245 | 1.77e-03 | ||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 36.79 E-value: 1.77e-03
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| LbH_XAT | cd03349 | Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
128-253 | 1.83e-03 | ||||||
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: 38.29 E-value: 1.83e-03
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
202-274 | 2.28e-03 | ||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 36.40 E-value: 2.28e-03
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
224-285 | 2.51e-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: 2.51e-03
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
121-150 | 2.65e-03 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 35.01 E-value: 2.65e-03
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
127-156 | 2.70e-03 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 35.01 E-value: 2.70e-03
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| dapD | PRK11830 | 2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional |
115-148 | 2.82e-03 | ||||||
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional Pssm-ID: 236996 [Multi-domain] Cd Length: 272 Bit Score: 39.02 E-value: 2.82e-03
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| PLN02241 | PLN02241 | glucose-1-phosphate adenylyltransferase |
135-233 | 2.88e-03 | ||||||
glucose-1-phosphate adenylyltransferase Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 39.07 E-value: 2.88e-03
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| PLN02357 | PLN02357 | serine acetyltransferase |
54-164 | 3.53e-03 | ||||||
serine acetyltransferase Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 38.71 E-value: 3.53e-03
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| LbH_G1P_AT_C_like | cd03356 | Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
224-285 | 4.18e-03 | ||||||
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 35.68 E-value: 4.18e-03
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
100-150 | 4.26e-03 | ||||||
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: 37.77 E-value: 4.26e-03
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| LbH_FBP | cd04650 | Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ... |
157-297 | 4.31e-03 | ||||||
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: 37.16 E-value: 4.31e-03
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
100-151 | 4.43e-03 | ||||||
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: 36.28 E-value: 4.43e-03
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| NRPS_term_dom | TIGR02353 | non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
146-251 | 4.87e-03 | ||||||
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: 38.58 E-value: 4.87e-03
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| LbH_paaY_like | cd04745 | paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
104-152 | 6.00e-03 | ||||||
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity. Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 36.96 E-value: 6.00e-03
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| LbH_MAT_GAT | cd03357 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
111-251 | 6.52e-03 | ||||||
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: 37.02 E-value: 6.52e-03
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| glgC | PRK02862 | glucose-1-phosphate adenylyltransferase; Provisional |
139-243 | 6.64e-03 | ||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 37.94 E-value: 6.64e-03
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| PRK10502 | PRK10502 | putative acyl transferase; Provisional |
200-278 | 6.82e-03 | ||||||
putative acyl transferase; Provisional Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 37.24 E-value: 6.82e-03
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| glgC | PRK00844 | glucose-1-phosphate adenylyltransferase; Provisional |
216-285 | 8.57e-03 | ||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 37.88 E-value: 8.57e-03
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
95-238 | 9.79e-03 | ||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 37.54 E-value: 9.79e-03
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