MULTISPECIES: glucose-1-phosphate adenylyltransferase [Vibrio]
Protein Classification
glucose-1-phosphate adenylyltransferase( domain architecture ID 11479259)
glucose-1-phosphate adenylyltransferase catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| glgC | PRK00844 | glucose-1-phosphate adenylyltransferase; Provisional |
1-403 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional : Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 758.21 E-value: 0e+00
|
|||||||||||
| Name | Accession | Description | Interval | E-value | |||||||
| glgC | PRK00844 | glucose-1-phosphate adenylyltransferase; Provisional |
1-403 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 758.21 E-value: 0e+00
|
|||||||||||
| GlgC | COG0448 | Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
4-401 | 0e+00 | |||||||
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 569.32 E-value: 0e+00
|
|||||||||||
| glgC | TIGR02091 | glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
6-378 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 273965 [Multi-domain] Cd Length: 361 Bit Score: 558.03 E-value: 0e+00
|
|||||||||||
| ADP_Glucose_PP | cd02508 | ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
6-258 | 7.48e-87 | |||||||
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: 262.09 E-value: 7.48e-87
|
|||||||||||
| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-272 | 3.11e-65 | |||||||
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: 208.26 E-value: 3.11e-65
|
|||||||||||
| Name | Accession | Description | Interval | E-value | |||||||
| glgC | PRK00844 | glucose-1-phosphate adenylyltransferase; Provisional |
1-403 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 758.21 E-value: 0e+00
|
|||||||||||
| GlgC | COG0448 | Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
4-401 | 0e+00 | |||||||
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 569.32 E-value: 0e+00
|
|||||||||||
| glgC | TIGR02091 | glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
6-378 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 273965 [Multi-domain] Cd Length: 361 Bit Score: 558.03 E-value: 0e+00
|
|||||||||||
| glgC | PRK00725 | glucose-1-phosphate adenylyltransferase; Provisional |
5-397 | 0e+00 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 551.75 E-value: 0e+00
|
|||||||||||
| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
4-404 | 2.31e-136 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 395.01 E-value: 2.31e-136
|
|||||||||||
| glgC | PRK02862 | glucose-1-phosphate adenylyltransferase; Provisional |
1-401 | 3.05e-117 | |||||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 348.03 E-value: 3.05e-117
|
|||||||||||
| PLN02241 | PLN02241 | glucose-1-phosphate adenylyltransferase |
4-401 | 2.71e-102 | |||||||
glucose-1-phosphate adenylyltransferase Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 310.25 E-value: 2.71e-102
|
|||||||||||
| ADP_Glucose_PP | cd02508 | ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
6-258 | 7.48e-87 | |||||||
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: 262.09 E-value: 7.48e-87
|
|||||||||||
| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-272 | 3.11e-65 | |||||||
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: 208.26 E-value: 3.11e-65
|
|||||||||||
| glgD | TIGR02092 | glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
1-403 | 7.30e-45 | |||||||
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 273966 [Multi-domain] Cd Length: 369 Bit Score: 159.08 E-value: 7.30e-45
|
|||||||||||
| NTP_transferase | cd04181 | NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-259 | 9.61e-43 | |||||||
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: 148.88 E-value: 9.61e-43
|
|||||||||||
| GCD1 | COG1208 | NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
7-274 | 1.80e-40 | |||||||
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: 143.75 E-value: 1.80e-40
|
|||||||||||
| LbH_G1P_AT_C | cd04651 | Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
303-403 | 7.04e-37 | |||||||
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: 129.89 E-value: 7.04e-37
|
|||||||||||
| NTP_transferase_WcbM_like | cd06915 | WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
7-268 | 1.99e-20 | |||||||
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: 89.15 E-value: 1.99e-20
|
|||||||||||
| rmlA_long | TIGR01208 | glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
6-384 | 1.72e-18 | |||||||
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: 85.92 E-value: 1.72e-18
|
|||||||||||
| NTP_transferase_like_2 | cd06426 | NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-268 | 9.08e-18 | |||||||
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: 81.40 E-value: 9.08e-18
|
|||||||||||
| M1P_guanylylT_B_like_N | cd06425 | N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
7-267 | 1.05e-17 | |||||||
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: 81.49 E-value: 1.05e-17
|
|||||||||||
| RmlA1 | COG1209 | dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-263 | 1.15e-16 | |||||||
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 79.75 E-value: 1.15e-16
|
|||||||||||
| G1P_TT_long | cd04189 | G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
4-274 | 1.35e-16 | |||||||
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: 78.38 E-value: 1.35e-16
|
|||||||||||
| G1P_TT_short | cd02538 | G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
6-183 | 5.99e-13 | |||||||
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: 67.99 E-value: 5.99e-13
|
|||||||||||
| NTP_transferase_like_1 | cd06422 | NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-264 | 1.52e-10 | |||||||
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: 60.66 E-value: 1.52e-10
|
|||||||||||
| PC_cytidylyltransferase | cd02523 | Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-262 | 1.79e-09 | |||||||
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: 57.63 E-value: 1.79e-09
|
|||||||||||
| COG1213 | COG1213 | Choline kinase [Lipid transport and metabolism]; |
6-61 | 2.91e-08 | |||||||
Choline kinase [Lipid transport and metabolism]; Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 54.09 E-value: 2.91e-08
|
|||||||||||
| LbH_G1P_AT_C_like | cd03356 | Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
322-379 | 3.16e-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: 3.16e-08
|
|||||||||||
| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
313-378 | 4.34e-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: 49.88 E-value: 4.34e-08
|
|||||||||||
| PRK15480 | PRK15480 | glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
6-213 | 6.10e-08 | |||||||
glucose-1-phosphate thymidylyltransferase RfbA; Provisional Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 53.91 E-value: 6.10e-08
|
|||||||||||
| G1P_cytidylyltransferase | cd02524 | G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
7-212 | 7.88e-08 | |||||||
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: 52.96 E-value: 7.88e-08
|
|||||||||||
| LbH_eIF2B_epsilon | cd05787 | eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
329-404 | 3.96e-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: 47.19 E-value: 3.96e-07
|
|||||||||||
| M1P_guanylylT_A_like_N | cd06428 | N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
98-239 | 1.53e-06 | |||||||
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: 49.17 E-value: 1.53e-06
|
|||||||||||
| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
329-379 | 6.24e-06 | |||||||
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: 46.63 E-value: 6.24e-06
|
|||||||||||
| PRK05289 | PRK05289 | acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
334-403 | 4.40e-05 | |||||||
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 44.70 E-value: 4.40e-05
|
|||||||||||
| LpxD | COG1044 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
287-397 | 5.33e-05 | |||||||
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: 45.01 E-value: 5.33e-05
|
|||||||||||
| glmU | PRK09451 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
342-383 | 8.55e-05 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 44.63 E-value: 8.55e-05
|
|||||||||||
| LpxA | COG1043 | Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
334-404 | 2.26e-04 | |||||||
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: 42.31 E-value: 2.26e-04
|
|||||||||||
| LbH_UDP-GlcNAc_AT | cd03351 | UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
335-403 | 3.73e-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: 41.65 E-value: 3.73e-04
|
|||||||||||
| LbH_G1P_TT_C_like | cd05636 | Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
311-379 | 4.56e-04 | |||||||
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: 40.65 E-value: 4.56e-04
|
|||||||||||
| lpxD | PRK00892 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
287-379 | 5.23e-04 | |||||||
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 41.66 E-value: 5.23e-04
|
|||||||||||
| LbH_GlmU_C | cd03353 | N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
304-377 | 5.79e-04 | |||||||
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer. Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 40.48 E-value: 5.79e-04
|
|||||||||||
| eIF-2B_gamma_N | cd04198 | The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
8-147 | 9.13e-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: 40.33 E-value: 9.13e-04
|
|||||||||||
| LbH_G1P_AT_C_like | cd03356 | Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
335-376 | 1.05e-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: 37.61 E-value: 1.05e-03
|
|||||||||||
| LbH_G1P_AT_C_like | cd03356 | Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
305-372 | 1.65e-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: 1.65e-03
|
|||||||||||
| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
308-375 | 1.67e-03 | |||||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 40.59 E-value: 1.67e-03
|
|||||||||||
| eIF-2B_gamma_N_like | cd02507 | The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
8-182 | 4.33e-03 | |||||||
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: 38.39 E-value: 4.33e-03
|
|||||||||||
| LbH_Dynactin_6 | cd04646 | Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ... |
335-378 | 6.57e-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: 37.30 E-value: 6.57e-03
|
|||||||||||
| MocA | COG2068 | CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-55 | 7.33e-03 | |||||||
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 37.45 E-value: 7.33e-03
|
|||||||||||
| LbH_LpxD | cd03352 | UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
345-379 | 8.39e-03 | |||||||
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 37.39 E-value: 8.39e-03
|
|||||||||||
| LbH_eIF2B_gamma_C | cd04652 | eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
323-373 | 8.65e-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: 35.25 E-value: 8.65e-03
|
|||||||||||
| Blast search parameters | ||||
|
