Species | Paenibacillus lautus_A | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lautus_A | |||||||||||
CAZyme ID | MGYG000001371_01120 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Dimodular nonribosomal peptide synthase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 24945; End: 32174 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
NF038078 | NRPS_MxcG | 0.0 | 7 | 1047 | 3 | 1049 | myxochelin non-ribosomal peptide synthetase MxcG. |
PRK05691 | PRK05691 | 0.0 | 12 | 2113 | 679 | 2771 | peptide synthase; Validated |
PRK12467 | PRK12467 | 0.0 | 1040 | 2241 | 2627 | 3795 | peptide synthase; Provisional |
cd05930 | A_NRPS | 0.0 | 1537 | 2033 | 1 | 444 | The adenylation domain of nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. |
cd19540 | LCL_NRPS-like | 0.0 | 1059 | 1491 | 1 | 433 | LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QND46664.1 | 0.0 | 50 | 2387 | 602 | 2929 |
ACX49739.1 | 1.43e-301 | 11 | 1774 | 12 | 1816 |
BAZ00088.1 | 1.18e-236 | 972 | 2248 | 2140 | 3423 |
BAZ75991.1 | 1.18e-236 | 972 | 2248 | 2140 | 3423 |
BAY90071.1 | 2.03e-222 | 1238 | 2117 | 303 | 1177 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5U89_A | 0.0 | 438 | 1509 | 3 | 1070 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
6MFZ_A | 3.49e-275 | 463 | 2110 | 209 | 1790 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
6MFY_A | 3.33e-261 | 463 | 2042 | 209 | 1721 | Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis] |
6P1J_A | 2.81e-211 | 1058 | 2033 | 4 | 964 | Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae] |
6N8E_A | 2.36e-184 | 1037 | 2293 | 14 | 1245 | Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P39846 | 0.0 | 4 | 2113 | 6 | 2072 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
Q70LM6 | 0.0 | 101 | 2134 | 2679 | 4695 | Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1 |
Q70LM5 | 0.0 | 103 | 2115 | 2705 | 4689 | Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1 |
P27206 | 0.0 | 9 | 2128 | 6 | 2092 | Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4 |
P45745 | 0.0 | 1 | 2390 | 1 | 2376 | Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000053 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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