UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [Vibrio tasmaniensis]
Protein Classification
LpxD family protein( domain architecture ID 11437199)
LpxD family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
1-309 | 2.83e-97 | ||||||
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: 291.54 E-value: 2.83e-97
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| Name | Accession | Description | Interval | E-value | ||||||
| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
1-309 | 2.83e-97 | ||||||
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: 291.54 E-value: 2.83e-97
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
106-299 | 2.11e-88 | ||||||
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: 264.27 E-value: 2.11e-88
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| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
1-309 | 1.00e-85 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 262.38 E-value: 1.00e-85
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| lipid_A_lpxD | TIGR01853 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ... |
6-309 | 5.01e-78 | ||||||
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: 241.81 E-value: 5.01e-78
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
113-142 | 9.44e-05 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 38.86 E-value: 9.44e-05
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| Name | Accession | Description | Interval | E-value | ||||||
| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
1-309 | 2.83e-97 | ||||||
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: 291.54 E-value: 2.83e-97
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
106-299 | 2.11e-88 | ||||||
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: 264.27 E-value: 2.11e-88
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| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
1-309 | 1.00e-85 | ||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 262.38 E-value: 1.00e-85
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| lipid_A_lpxD | TIGR01853 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ... |
6-309 | 5.01e-78 | ||||||
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: 241.81 E-value: 5.01e-78
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| LpxA | COG1043 | Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
106-280 | 2.81e-26 | ||||||
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: 105.10 E-value: 2.81e-26
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| LbH_UDP-GlcNAc_AT | cd03351 | UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
124-279 | 6.13e-25 | ||||||
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: 101.35 E-value: 6.13e-25
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| PRK05289 | PRK05289 | acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
106-280 | 2.70e-24 | ||||||
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 99.79 E-value: 2.70e-24
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| lipid_A_lpxA | TIGR01852 | acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ... |
106-283 | 9.20e-22 | ||||||
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: 92.71 E-value: 9.20e-22
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| PRK12461 | PRK12461 | UDP-N-acetylglucosamine acyltransferase; Provisional |
106-283 | 8.61e-19 | ||||||
UDP-N-acetylglucosamine acyltransferase; Provisional Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 8.61e-19
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| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
108-218 | 5.28e-13 | ||||||
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: 66.07 E-value: 5.28e-13
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| LbH_AT_putative | cd03360 | Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
187-292 | 3.23e-12 | ||||||
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: 64.43 E-value: 3.23e-12
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| LbH_AT_putative | cd03360 | Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
106-216 | 6.35e-12 | ||||||
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: 63.66 E-value: 6.35e-12
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
113-213 | 8.43e-12 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 62.20 E-value: 8.43e-12
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
187-293 | 8.75e-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: 63.28 E-value: 8.75e-12
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
106-215 | 3.24e-11 | ||||||
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: 61.74 E-value: 3.24e-11
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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 ... |
110-216 | 1.20e-09 | ||||||
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: 55.20 E-value: 1.20e-09
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
96-286 | 3.56e-09 | ||||||
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: 55.89 E-value: 3.56e-09
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
128-286 | 9.63e-09 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 56.29 E-value: 9.63e-09
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
103-286 | 1.14e-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: 1.14e-08
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
108-237 | 2.32e-08 | ||||||
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: 55.42 E-value: 2.32e-08
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
119-218 | 3.93e-08 | ||||||
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: 50.52 E-value: 3.93e-08
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
107-215 | 8.21e-08 | ||||||
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: 49.76 E-value: 8.21e-08
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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 ... |
106-169 | 1.11e-07 | ||||||
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: 49.81 E-value: 1.11e-07
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
194-292 | 2.39e-07 | ||||||
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: 48.21 E-value: 2.39e-07
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
131-294 | 2.83e-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: 48.22 E-value: 2.83e-07
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| CysE | COG1045 | Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
212-294 | 6.21e-07 | ||||||
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: 48.93 E-value: 6.21e-07
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
106-165 | 6.58e-07 | ||||||
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms. Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 46.47 E-value: 6.58e-07
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| LbH_wcaF_like | cd05825 | wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
206-294 | 9.26e-07 | ||||||
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms. Pssm-ID: 100063 [Multi-domain] Cd Length: 107 Bit Score: 46.83 E-value: 9.26e-07
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| CysE | COG1045 | Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
121-218 | 9.98e-07 | ||||||
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: 48.16 E-value: 9.98e-07
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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 ... |
190-294 | 1.01e-06 | ||||||
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: 47.11 E-value: 1.01e-06
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| LbH_Dynactin_5 | cd03359 | Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
108-218 | 1.67e-06 | ||||||
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: 47.21 E-value: 1.67e-06
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
129-280 | 2.09e-06 | ||||||
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 49.25 E-value: 2.09e-06
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| PRK10502 | PRK10502 | putative acyl transferase; Provisional |
206-294 | 4.02e-06 | ||||||
putative acyl transferase; Provisional Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 46.48 E-value: 4.02e-06
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| LbH_paaY_like | cd04745 | paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
185-297 | 4.97e-06 | ||||||
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity. Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 45.82 E-value: 4.97e-06
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
107-158 | 5.90e-06 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 45.25 E-value: 5.90e-06
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
132-225 | 1.50e-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: 42.62 E-value: 1.50e-05
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| LbH_MAT_GAT | cd03357 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
104-158 | 2.98e-05 | ||||||
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: 43.95 E-value: 2.98e-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 ... |
109-198 | 3.31e-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: 41.46 E-value: 3.31e-05
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| LbH_eIF2B_gamma_C | cd04652 | eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
110-166 | 4.54e-05 | ||||||
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: 41.41 E-value: 4.54e-05
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
113-142 | 9.44e-05 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 38.86 E-value: 9.44e-05
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
131-158 | 1.29e-04 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 38.47 E-value: 1.29e-04
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
106-225 | 1.57e-04 | ||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 43.32 E-value: 1.57e-04
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| glmU | PRK14357 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
75-286 | 1.64e-04 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 43.21 E-value: 1.64e-04
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| LbH_MAT_GAT | cd03357 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
115-294 | 2.83e-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: 40.87 E-value: 2.83e-04
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
131-280 | 3.36e-04 | ||||||
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer. Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 41.25 E-value: 3.36e-04
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
107-136 | 3.62e-04 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 37.32 E-value: 3.62e-04
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| PRK10092 | PRK10092 | maltose O-acetyltransferase; Provisional |
104-160 | 4.39e-04 | ||||||
maltose O-acetyltransferase; Provisional Pssm-ID: 182235 [Multi-domain] Cd Length: 183 Bit Score: 40.57 E-value: 4.39e-04
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| glmU | PRK14360 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
106-218 | 6.43e-04 | ||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 41.45 E-value: 6.43e-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 ... |
110-159 | 1.05e-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: 37.56 E-value: 1.05e-03
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
107-155 | 1.26e-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: 37.82 E-value: 1.26e-03
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| PaaY | COG0663 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
109-152 | 1.27e-03 | ||||||
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 39.24 E-value: 1.27e-03
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| NRPS_term_dom | TIGR02353 | non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
131-233 | 1.31e-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: 40.50 E-value: 1.31e-03
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
107-152 | 1.44e-03 | ||||||
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: 38.55 E-value: 1.44e-03
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| LbH_Dynactin_6 | cd04646 | Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ... |
127-257 | 1.75e-03 | ||||||
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Pssm-ID: 100052 [Multi-domain] Cd Length: 164 Bit Score: 38.46 E-value: 1.75e-03
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
209-234 | 3.27e-03 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 34.62 E-value: 3.27e-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 ... |
134-236 | 4.75e-03 | ||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 35.63 E-value: 4.75e-03
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| DapD | COG2171 | Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
115-155 | 5.28e-03 | ||||||
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: 38.17 E-value: 5.28e-03
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
108-169 | 5.64e-03 | ||||||
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: 37.01 E-value: 5.64e-03
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
111-154 | 5.77e-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: 35.88 E-value: 5.77e-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 ... |
209-280 | 5.89e-03 | ||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 35.25 E-value: 5.89e-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 ... |
112-159 | 5.89e-03 | ||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 35.25 E-value: 5.89e-03
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
125-154 | 6.71e-03 | ||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 33.85 E-value: 6.71e-03
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| PLN02357 | PLN02357 | serine acetyltransferase |
122-218 | 7.45e-03 | ||||||
serine acetyltransferase Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 37.94 E-value: 7.45e-03
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
107-155 | 8.42e-03 | ||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 36.39 E-value: 8.42e-03
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
106-154 | 9.55e-03 | ||||||
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: 36.70 E-value: 9.55e-03
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| Blast search parameters | ||||
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