bifunctional glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase [Pseudomonas aeruginosa PAO1]
Protein Classification
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase( domain architecture ID 11440231)
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase functions as both an uridyltransferase and acetyltransferase, in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc).
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1-454 | 0e+00 | |||||||
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: 813.11 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1-454 | 0e+00 | |||||||
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: 813.11 E-value: 0e+00
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| glmU | TIGR01173 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
3-452 | 0e+00 | |||||||
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars] Pssm-ID: 273482 [Multi-domain] Cd Length: 451 Bit Score: 767.98 E-value: 0e+00
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| glmU | PRK09451 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-453 | 0e+00 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 668.66 E-value: 0e+00
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| GT2_GlmU_N_bac | cd02540 | N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
5-228 | 7.46e-124 | |||||||
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively. Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 359.14 E-value: 7.46e-124
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| NTP_transf_3 | pfam12804 | MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-121 | 2.91e-18 | |||||||
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain. Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 81.47 E-value: 2.91e-18
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| Name | Accession | Description | Interval | E-value | |||||||
| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1-454 | 0e+00 | |||||||
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: 813.11 E-value: 0e+00
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| glmU | TIGR01173 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
3-452 | 0e+00 | |||||||
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars] Pssm-ID: 273482 [Multi-domain] Cd Length: 451 Bit Score: 767.98 E-value: 0e+00
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| glmU | PRK09451 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-453 | 0e+00 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 668.66 E-value: 0e+00
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-451 | 0e+00 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 588.72 E-value: 0e+00
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| glmU | PRK14353 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-446 | 0e+00 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 546.38 E-value: 0e+00
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| glmU | PRK14352 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-449 | 3.14e-173 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 494.46 E-value: 3.14e-173
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-447 | 1.18e-168 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 481.94 E-value: 1.18e-168
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| glmU | PRK14360 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-451 | 7.06e-168 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 479.81 E-value: 7.06e-168
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| glmU | PRK14356 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-443 | 2.83e-161 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 463.04 E-value: 2.83e-161
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| glmU | PRK14357 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-451 | 1.86e-157 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 453.07 E-value: 1.86e-157
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| glmU | PRK14358 | bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
3-448 | 8.70e-155 | |||||||
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 447.50 E-value: 8.70e-155
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| glmU | PRK14359 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-445 | 3.35e-146 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 424.02 E-value: 3.35e-146
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| GT2_GlmU_N_bac | cd02540 | N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
5-228 | 7.46e-124 | |||||||
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively. Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 359.14 E-value: 7.46e-124
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
248-440 | 5.30e-121 | |||||||
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: 350.57 E-value: 5.30e-121
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| Arch_glmU | TIGR03992 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
6-424 | 1.89e-78 | |||||||
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them. Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 249.05 E-value: 1.89e-78
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| NTP_transferase | cd04181 | NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-210 | 1.48e-40 | |||||||
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 144.26 E-value: 1.48e-40
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| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
277-425 | 3.03e-34 | |||||||
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: 125.78 E-value: 3.03e-34
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| GCD1 | COG1208 | NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-210 | 3.12e-33 | |||||||
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 125.27 E-value: 3.12e-33
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| NTP_transferase_WcbM_like | cd06915 | WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-210 | 8.16e-26 | |||||||
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars. Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 104.56 E-value: 8.16e-26
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| GT_2_like_f | cd04182 | GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
5-115 | 3.78e-22 | |||||||
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 93.39 E-value: 3.78e-22
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| MocA | COG2068 | CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-116 | 6.33e-22 | |||||||
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 92.92 E-value: 6.33e-22
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| COG1213 | COG1213 | Choline kinase [Lipid transport and metabolism]; |
6-220 | 5.14e-21 | |||||||
Choline kinase [Lipid transport and metabolism]; Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 91.46 E-value: 5.14e-21
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| RmlA1 | COG1209 | dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-210 | 6.45e-21 | |||||||
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 92.46 E-value: 6.45e-21
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| G1P_TT_long | cd04189 | G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-212 | 2.71e-20 | |||||||
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 89.55 E-value: 2.71e-20
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| NTP_transf_3 | pfam12804 | MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-121 | 2.91e-18 | |||||||
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain. Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 81.47 E-value: 2.91e-18
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| NTP_transferase_like_1 | cd06422 | NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-155 | 7.21e-18 | |||||||
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 82.23 E-value: 7.21e-18
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| PC_cytidylyltransferase | cd02523 | Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
5-164 | 7.01e-17 | |||||||
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide. Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 79.58 E-value: 7.01e-17
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
265-436 | 6.18e-16 | |||||||
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: 76.29 E-value: 6.18e-16
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-217 | 3.33e-15 | |||||||
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars. Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 74.98 E-value: 3.33e-15
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| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
264-431 | 6.51e-13 | |||||||
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: 69.28 E-value: 6.51e-13
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
308-436 | 6.65e-13 | |||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 65.66 E-value: 6.65e-13
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| matur_MocA_YgfJ | TIGR03310 | molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
6-120 | 4.03e-12 | |||||||
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide. Pssm-ID: 274516 Cd Length: 188 Bit Score: 64.67 E-value: 4.03e-12
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| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
265-432 | 1.71e-11 | |||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 65.16 E-value: 1.71e-11
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| MobA | COG0746 | Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-120 | 2.62e-11 | |||||||
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 62.52 E-value: 2.62e-11
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| LbH_AT_putative | cd03360 | Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
324-436 | 4.99e-11 | |||||||
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: 61.73 E-value: 4.99e-11
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| UGPase_prokaryotic | cd02541 | Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
6-210 | 8.01e-11 | |||||||
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 62.55 E-value: 8.01e-11
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| IspD | COG1211 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
6-117 | 3.77e-10 | |||||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440824 Cd Length: 224 Bit Score: 59.76 E-value: 3.77e-10
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
350-425 | 3.98e-10 | |||||||
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms. Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 56.10 E-value: 3.98e-10
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| MobA | cd02503 | MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
6-120 | 1.14e-09 | |||||||
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target. Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 57.59 E-value: 1.14e-09
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| CDP-ME_synthetase | cd02516 | CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-117 | 3.23e-09 | |||||||
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 56.76 E-value: 3.23e-09
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| NeuD_NnaD | TIGR03570 | sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
315-436 | 4.61e-09 | |||||||
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: 55.96 E-value: 4.61e-09
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| LbH_unknown | cd05635 | Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
278-383 | 7.77e-09 | |||||||
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: 53.05 E-value: 7.77e-09
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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 ... |
335-441 | 8.51e-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: 53.27 E-value: 8.51e-09
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| GlgC | COG0448 | Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
6-336 | 9.21e-09 | |||||||
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 57.01 E-value: 9.21e-09
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| COG2266 | COG2266 | GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
8-127 | 1.39e-08 | |||||||
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 54.51 E-value: 1.39e-08
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| PRK02726 | PRK02726 | molybdenum cofactor guanylyltransferase; |
1-125 | 2.11e-08 | |||||||
molybdenum cofactor guanylyltransferase; Pssm-ID: 235063 Cd Length: 200 Bit Score: 54.27 E-value: 2.11e-08
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
350-436 | 3.48e-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: 50.90 E-value: 3.48e-08
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| ispD | PRK00155 | D-ribitol-5-phosphate cytidylyltransferase; |
1-52 | 3.53e-08 | |||||||
D-ribitol-5-phosphate cytidylyltransferase; Pssm-ID: 234670 Cd Length: 227 Bit Score: 53.98 E-value: 3.53e-08
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| ispD | TIGR00453 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
6-52 | 3.25e-07 | |||||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other] Pssm-ID: 213532 Cd Length: 217 Bit Score: 50.75 E-value: 3.25e-07
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
349-436 | 7.90e-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: 47.45 E-value: 7.90e-07
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| NTP_transferase_like_2 | cd06426 | NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-169 | 8.21e-07 | |||||||
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 49.82 E-value: 8.21e-07
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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 ... |
265-336 | 8.50e-07 | |||||||
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: 46.47 E-value: 8.50e-07
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| molyb_mobA | TIGR02665 | molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
5-115 | 8.67e-07 | |||||||
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 274249 Cd Length: 186 Bit Score: 49.20 E-value: 8.67e-07
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| LbH_MAT_like | cd04647 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
256-310 | 1.61e-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: 46.68 E-value: 1.61e-06
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| LbH_XAT | cd03349 | Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
391-430 | 2.63e-06 | |||||||
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: 46.77 E-value: 2.63e-06
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| mobA | PRK00317 | molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-127 | 2.75e-06 | |||||||
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 47.87 E-value: 2.75e-06
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| GDP-M1P_Guanylyltransferase | cd02509 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
5-160 | 3.87e-06 | |||||||
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes. Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 48.34 E-value: 3.87e-06
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| GalU | COG1210 | UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
6-102 | 5.11e-06 | |||||||
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 48.10 E-value: 5.11e-06
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| CysE | COG1045 | Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
367-436 | 7.76e-06 | |||||||
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: 46.23 E-value: 7.76e-06
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| GT2_BcE_like | cd04183 | GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
5-101 | 7.96e-06 | |||||||
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 46.86 E-value: 7.96e-06
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
256-338 | 1.15e-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: 45.10 E-value: 1.15e-05
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| LbH_gamma_CA | cd00710 | Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
271-389 | 1.16e-05 | |||||||
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain. Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 45.31 E-value: 1.16e-05
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| ispDF | PRK09382 | bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
1-115 | 1.30e-05 | |||||||
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional Pssm-ID: 236492 [Multi-domain] Cd Length: 378 Bit Score: 47.15 E-value: 1.30e-05
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| LbH_SAT | cd03354 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
245-299 | 1.36e-05 | |||||||
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: 43.58 E-value: 1.36e-05
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
261-342 | 2.42e-05 | |||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 44.09 E-value: 2.42e-05
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| WbbJ | COG0110 | Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
257-310 | 2.54e-05 | |||||||
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 44.09 E-value: 2.54e-05
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| PRK12461 | PRK12461 | UDP-N-acetylglucosamine acyltransferase; Provisional |
270-429 | 3.21e-05 | |||||||
UDP-N-acetylglucosamine acyltransferase; Provisional Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 45.40 E-value: 3.21e-05
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| M1P_guanylylT_A_like_N | cd06428 | N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
6-43 | 3.46e-05 | |||||||
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation. Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 45.32 E-value: 3.46e-05
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| PLN02357 | PLN02357 | serine acetyltransferase |
393-436 | 3.51e-05 | |||||||
serine acetyltransferase Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 45.64 E-value: 3.51e-05
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
265-342 | 3.97e-05 | |||||||
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: 41.79 E-value: 3.97e-05
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| PRK05450 | PRK05450 | 3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
5-120 | 4.10e-05 | |||||||
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional Pssm-ID: 235473 Cd Length: 245 Bit Score: 44.72 E-value: 4.10e-05
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
264-437 | 4.37e-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: 43.55 E-value: 4.37e-05
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| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
254-336 | 7.56e-05 | |||||||
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: 41.68 E-value: 7.56e-05
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| PaaY | COG0663 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
265-431 | 1.05e-04 | |||||||
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 42.71 E-value: 1.05e-04
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| G1P_cytidylyltransferase | cd02524 | G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
5-36 | 1.41e-04 | |||||||
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity. Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 43.33 E-value: 1.41e-04
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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 ... |
282-359 | 1.62e-04 | |||||||
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 39.92 E-value: 1.62e-04
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| eIF-2B_gamma_N | cd04198 | The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
3-38 | 1.84e-04 | |||||||
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex. Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 42.65 E-value: 1.84e-04
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| M1P_guanylylT_B_like_N | cd06425 | N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-169 | 1.88e-04 | |||||||
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation. Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 42.97 E-value: 1.88e-04
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| PRK13368 | PRK13368 | 3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-115 | 1.93e-04 | |||||||
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional Pssm-ID: 184007 Cd Length: 238 Bit Score: 42.64 E-value: 1.93e-04
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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 ... |
258-321 | 1.94e-04 | |||||||
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: 40.95 E-value: 1.94e-04
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| eIF-2B_gamma_N_like | cd02507 | The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
3-38 | 2.03e-04 | |||||||
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex. Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 42.63 E-value: 2.03e-04
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| LbH_MAT_GAT | cd03357 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
395-436 | 3.03e-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: 3.03e-04
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| IspD | pfam01128 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
5-115 | 3.51e-04 | |||||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP). Pssm-ID: 460075 Cd Length: 219 Bit Score: 41.67 E-value: 3.51e-04
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| LbH_THP_succinylT | cd03350 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
287-437 | 3.66e-04 | |||||||
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs. Pssm-ID: 100041 [Multi-domain] Cd Length: 139 Bit Score: 40.44 E-value: 3.66e-04
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| PLN02694 | PLN02694 | serine O-acetyltransferase |
332-436 | 4.44e-04 | |||||||
serine O-acetyltransferase Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 41.94 E-value: 4.44e-04
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| LbetaH | cd00208 | Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
265-342 | 4.77e-04 | |||||||
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms. Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 38.77 E-value: 4.77e-04
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| GT2_SpsF | cd02518 | SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
5-105 | 7.82e-04 | |||||||
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration. Pssm-ID: 133011 Cd Length: 233 Bit Score: 41.02 E-value: 7.82e-04
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| LbH_UDP-GlcNAc_AT | cd03351 | UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
276-429 | 8.10e-04 | |||||||
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: 40.88 E-value: 8.10e-04
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| LpxA | COG1043 | Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
276-439 | 1.15e-03 | |||||||
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: 40.39 E-value: 1.15e-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 ... |
282-366 | 1.31e-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: 1.31e-03
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| SpsF | COG1861 | Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
5-38 | 1.41e-03 | |||||||
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441466 Cd Length: 245 Bit Score: 40.19 E-value: 1.41e-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 ... |
317-401 | 1.56e-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: 37.22 E-value: 1.56e-03
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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 ... |
265-320 | 1.56e-03 | |||||||
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 37.17 E-value: 1.56e-03
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| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
265-341 | 1.91e-03 | |||||||
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization. Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 37.83 E-value: 1.91e-03
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| NRPS_term_dom | TIGR02353 | non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
265-342 | 1.96e-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: 1.96e-03
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| CTP_transf_3 | pfam02348 | Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
5-116 | 2.19e-03 | |||||||
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand. Pssm-ID: 396773 Cd Length: 217 Bit Score: 39.24 E-value: 2.19e-03
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| LbH_XAT | cd03349 | Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
278-310 | 2.42e-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: 2.42e-03
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| CMP-KDO-Synthetase | cd02517 | CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
5-115 | 2.44e-03 | |||||||
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design. Pssm-ID: 133010 Cd Length: 239 Bit Score: 39.38 E-value: 2.44e-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 ... |
352-428 | 2.53e-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: 2.53e-03
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| LbH_paaY_like | cd04745 | paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
271-377 | 2.66e-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: 38.50 E-value: 2.66e-03
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| Hexapep | pfam00132 | Bacterial transferase hexapeptide (six repeats); |
263-291 | 3.00e-03 | |||||||
Bacterial transferase hexapeptide (six repeats); Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 35.01 E-value: 3.00e-03
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| PRK05289 | PRK05289 | acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
276-453 | 3.48e-03 | |||||||
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 38.93 E-value: 3.48e-03
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
267-342 | 5.98e-03 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 38.70 E-value: 5.98e-03
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| CMP-NeuAc_Synthase | cd02513 | CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
22-143 | 7.70e-03 | |||||||
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm. Pssm-ID: 133006 Cd Length: 223 Bit Score: 37.90 E-value: 7.70e-03
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| PRK14489 | PRK14489 | putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
6-53 | 7.93e-03 | |||||||
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 38.19 E-value: 7.93e-03
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| LbH_THP_succinylT | cd03350 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
265-338 | 8.14e-03 | |||||||
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: 36.59 E-value: 8.14e-03
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| PRK13385 | PRK13385 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
1-154 | 8.91e-03 | |||||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional Pssm-ID: 184017 Cd Length: 230 Bit Score: 37.54 E-value: 8.91e-03
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| CpsB | COG0836 | Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
6-72 | 9.00e-03 | |||||||
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 38.12 E-value: 9.00e-03
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