glucose-1-phosphate thymidylyltransferase [Caldisphaera lagunensis]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| rmlA_long super family | cl36843 | glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-353 | 1.22e-155 | ||||||
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase The actual alignment was detected with superfamily member TIGR01208: Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 440.69 E-value: 1.22e-155
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| Name | Accession | Description | Interval | E-value | ||||||
| rmlA_long | TIGR01208 | glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-353 | 1.22e-155 | ||||||
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 440.69 E-value: 1.22e-155
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| G1P_TT_long | cd04189 | G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-237 | 1.23e-129 | ||||||
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: 370.36 E-value: 1.23e-129
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| RmlA1 | COG1209 | dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-304 | 3.98e-118 | ||||||
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 343.23 E-value: 3.98e-118
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-235 | 2.13e-63 | ||||||
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: 201.71 E-value: 2.13e-63
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| PRK15480 | PRK15480 | glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-244 | 2.36e-38 | ||||||
glucose-1-phosphate thymidylyltransferase RfbA; Provisional Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 138.65 E-value: 2.36e-38
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| Name | Accession | Description | Interval | E-value | |||||||
| rmlA_long | TIGR01208 | glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-353 | 1.22e-155 | |||||||
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 440.69 E-value: 1.22e-155
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| G1P_TT_long | cd04189 | G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-237 | 1.23e-129 | |||||||
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: 370.36 E-value: 1.23e-129
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| RmlA1 | COG1209 | dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-304 | 3.98e-118 | |||||||
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 343.23 E-value: 3.98e-118
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| Arch_glmU | TIGR03992 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-330 | 6.25e-94 | |||||||
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: 285.26 E-value: 6.25e-94
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| G1P_TT_short | cd02538 | G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-234 | 1.19e-76 | |||||||
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short 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 homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. 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. Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 235.55 E-value: 1.19e-76
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| NTP_transferase | cd04181 | NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-222 | 1.94e-75 | |||||||
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: 231.70 E-value: 1.94e-75
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| GCD1 | COG1208 | NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-243 | 5.62e-69 | |||||||
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: 216.17 E-value: 5.62e-69
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-235 | 2.13e-63 | |||||||
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: 201.71 E-value: 2.13e-63
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| rmlA | TIGR01207 | glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ... |
2-242 | 1.25e-47 | |||||||
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 130274 [Multi-domain] Cd Length: 286 Bit Score: 162.56 E-value: 1.25e-47
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| UGPase_prokaryotic | cd02541 | Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-231 | 7.19e-46 | |||||||
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: 157.31 E-value: 7.19e-46
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| GalU | COG1210 | UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-231 | 4.64e-40 | |||||||
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 142.86 E-value: 4.64e-40
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| PRK15480 | PRK15480 | glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-244 | 2.36e-38 | |||||||
glucose-1-phosphate thymidylyltransferase RfbA; Provisional Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 138.65 E-value: 2.36e-38
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| M1P_guanylylT_B_like_N | cd06425 | N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-235 | 2.45e-38 | |||||||
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: 136.57 E-value: 2.45e-38
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| NTP_transferase_WcbM_like | cd06915 | WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-230 | 2.72e-36 | |||||||
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: 130.75 E-value: 2.72e-36
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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 ... |
4-226 | 1.74e-35 | |||||||
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: 128.78 E-value: 1.74e-35
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-333 | 1.69e-26 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 109.15 E-value: 1.69e-26
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-333 | 5.59e-26 | |||||||
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: 107.80 E-value: 5.59e-26
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| glmU | PRK14357 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-332 | 1.62e-23 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 100.61 E-value: 1.62e-23
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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 ... |
2-230 | 4.59e-23 | |||||||
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: 95.72 E-value: 4.59e-23
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| PRK10122 | PRK10122 | UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-224 | 1.82e-21 | |||||||
UTP--glucose-1-phosphate uridylyltransferase GalF; Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 93.03 E-value: 1.82e-21
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| GT2_GlmU_N_bac | cd02540 | N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-210 | 2.73e-21 | |||||||
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: 91.04 E-value: 2.73e-21
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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 ... |
3-197 | 2.49e-20 | |||||||
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: 88.85 E-value: 2.49e-20
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| PRK13389 | PRK13389 | UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-205 | 1.97e-19 | |||||||
UTP--glucose-1-phosphate uridylyltransferase GalU; Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 87.27 E-value: 1.97e-19
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| COG1213 | COG1213 | Choline kinase [Lipid transport and metabolism]; |
2-234 | 3.07e-18 | |||||||
Choline kinase [Lipid transport and metabolism]; Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 82.60 E-value: 3.07e-18
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| PC_cytidylyltransferase | cd02523 | Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-206 | 3.21e-18 | |||||||
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: 82.28 E-value: 3.21e-18
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
1-337 | 3.65e-17 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 81.84 E-value: 3.65e-17
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| GlgC | COG0448 | Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-322 | 2.63e-16 | |||||||
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 78.96 E-value: 2.63e-16
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| GT2_BcE_like | cd04183 | GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-175 | 7.41e-15 | |||||||
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: 73.06 E-value: 7.41e-15
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| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
251-331 | 1.40e-14 | |||||||
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: 70.69 E-value: 1.40e-14
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| glgC | PRK02862 | glucose-1-phosphate adenylyltransferase; Provisional |
3-316 | 1.56e-12 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 67.99 E-value: 1.56e-12
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| glmU | PRK14353 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-157 | 1.57e-12 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 67.96 E-value: 1.57e-12
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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; ... |
1-78 | 3.14e-11 | |||||||
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: 62.29 E-value: 3.14e-11
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| PLN02241 | PLN02241 | glucose-1-phosphate adenylyltransferase |
3-316 | 4.37e-10 | |||||||
glucose-1-phosphate adenylyltransferase Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 60.64 E-value: 4.37e-10
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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 ... |
276-338 | 4.41e-10 | |||||||
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: 55.33 E-value: 4.41e-10
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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 ... |
242-318 | 1.05e-09 | |||||||
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: 54.56 E-value: 1.05e-09
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| glmU | PRK14356 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-328 | 1.09e-09 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 59.35 E-value: 1.09e-09
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| glmU | PRK09451 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-338 | 1.46e-09 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 58.88 E-value: 1.46e-09
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-316 | 2.67e-09 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 58.22 E-value: 2.67e-09
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| G1P_cytidylyltransferase | cd02524 | G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
4-184 | 3.22e-09 | |||||||
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: 56.81 E-value: 3.22e-09
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| eIF-2B_gamma_N_like | cd02507 | The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-76 | 5.22e-09 | |||||||
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: 55.72 E-value: 5.22e-09
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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 ... |
276-338 | 5.68e-09 | |||||||
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: 52.19 E-value: 5.68e-09
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| glmU | PRK14360 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-333 | 1.38e-08 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 56.09 E-value: 1.38e-08
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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 ... |
253-335 | 2.66e-08 | |||||||
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: 50.32 E-value: 2.66e-08
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| glmU | PRK14359 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-320 | 3.70e-08 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 54.61 E-value: 3.70e-08
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
254-335 | 9.44e-08 | |||||||
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: 48.73 E-value: 9.44e-08
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| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
277-338 | 5.84e-07 | |||||||
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: 46.80 E-value: 5.84e-07
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| CDP-ME_synthetase | cd02516 | CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-74 | 1.29e-06 | |||||||
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: 48.67 E-value: 1.29e-06
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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; ... |
3-54 | 2.69e-06 | |||||||
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: 47.17 E-value: 2.69e-06
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| glmU | PRK14352 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-310 | 4.60e-06 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 48.01 E-value: 4.60e-06
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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 ... |
254-337 | 6.30e-06 | |||||||
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: 43.72 E-value: 6.30e-06
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| MocA | COG2068 | CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-54 | 6.52e-06 | |||||||
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 46.31 E-value: 6.52e-06
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| NTP_transf_3 | pfam12804 | MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-108 | 8.64e-06 | |||||||
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: 45.26 E-value: 8.64e-06
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| LbH_Dynactin_5 | cd03359 | Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
242-316 | 1.77e-05 | |||||||
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 44.51 E-value: 1.77e-05
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
254-351 | 4.21e-05 | |||||||
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: 43.95 E-value: 4.21e-05
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| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
243-306 | 4.81e-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: 42.07 E-value: 4.81e-05
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| ispD | PRK00155 | D-ribitol-5-phosphate cytidylyltransferase; |
4-53 | 7.74e-05 | |||||||
D-ribitol-5-phosphate cytidylyltransferase; Pssm-ID: 234670 Cd Length: 227 Bit Score: 43.58 E-value: 7.74e-05
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| ADP_Glucose_PP | cd02508 | ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-52 | 8.58e-05 | |||||||
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2. Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 42.91 E-value: 8.58e-05
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| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
242-333 | 9.93e-05 | |||||||
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: 42.79 E-value: 9.93e-05
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| LbH_gamma_CA_like | cd04645 | Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
242-338 | 1.17e-04 | |||||||
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: 42.01 E-value: 1.17e-04
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| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
260-338 | 1.47e-04 | |||||||
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization. Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 40.52 E-value: 1.47e-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 ... |
242-300 | 2.41e-04 | |||||||
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 39.10 E-value: 2.41e-04
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| MobA | cd02503 | MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
1-59 | 3.11e-04 | |||||||
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: 41.02 E-value: 3.11e-04
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| PaaY | COG0663 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
251-341 | 4.03e-04 | |||||||
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only]; Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 40.40 E-value: 4.03e-04
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| IspD | COG1211 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-53 | 4.81e-04 | |||||||
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: 40.88 E-value: 4.81e-04
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| mobA | PRK00317 | molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-52 | 6.99e-04 | |||||||
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 40.17 E-value: 6.99e-04
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| COG2266 | COG2266 | GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
8-52 | 7.21e-04 | |||||||
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: 39.87 E-value: 7.21e-04
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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 ... |
242-294 | 1.11e-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: 37.56 E-value: 1.11e-03
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| ispDF | PRK09382 | bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
4-52 | 1.13e-03 | |||||||
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: 40.60 E-value: 1.13e-03
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| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
242-337 | 2.50e-03 | |||||||
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 38.54 E-value: 2.50e-03
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| LbH_Dynactin_6 | cd04646 | Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ... |
242-336 | 2.67e-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: 38.08 E-value: 2.67e-03
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| GDP-M1P_Guanylyltransferase | cd02509 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-104 | 3.34e-03 | |||||||
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: 38.71 E-value: 3.34e-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 ... |
234-308 | 3.64e-03 | |||||||
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange. Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.02 E-value: 3.64e-03
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| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
260-333 | 9.95e-03 | |||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 37.43 E-value: 9.95e-03
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