Species | Paenibacillus_B thiaminolyticus | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus | |||||||||||
CAZyme ID | MGYG000002490_03177 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | D-alanine--poly(phosphoribitol) ligase subunit 1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 117873; End: 127097 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd12117 | A_NRPS_Srf_like | 0.0 | 478 | 958 | 1 | 483 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain. |
cd05930 | A_NRPS | 0.0 | 488 | 958 | 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. |
PRK12316 | PRK12316 | 0.0 | 7 | 1115 | 1548 | 2668 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 32 | 1053 | 66 | 1106 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 32 | 1051 | 1133 | 2169 | peptide synthase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAY90071.1 | 0.0 | 163 | 3061 | 269 | 2678 |
BAY30132.1 | 0.0 | 245 | 3061 | 361 | 2689 |
BAZ00088.1 | 0.0 | 245 | 3053 | 361 | 2682 |
BAZ75991.1 | 0.0 | 245 | 3053 | 361 | 2682 |
AFY93865.1 | 0.0 | 449 | 1958 | 305 | 1861 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VSQ_A | 1.26e-179 | 6 | 1050 | 3 | 1046 | Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis] |
4MZ0_A | 9.81e-167 | 1086 | 1958 | 41 | 935 | ChainA, CurL [Moorena producens 3L],4MZ0_B Chain B, CurL [Moorena producens 3L] |
7S6C_A | 1.64e-158 | 1083 | 2440 | 31 | 1372 | ChainA, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_D Chain D, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_A Chain A, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct] |
7M7J_A | 7.95e-155 | 1086 | 2599 | 35 | 1485 | ChainA, EryAI [Saccharopolyspora erythraea],7M7J_B Chain B, EryAI [Saccharopolyspora erythraea] |
7M7I_A | 7.95e-155 | 1086 | 2599 | 35 | 1485 | ChainA, EryAI [Saccharopolyspora erythraea],7M7I_B Chain B, EryAI [Saccharopolyspora erythraea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O30409 | 2.39e-278 | 44 | 3067 | 3159 | 5644 | Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1 |
P0C064 | 3.43e-271 | 13 | 3051 | 1059 | 3562 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
P0C063 | 1.68e-268 | 13 | 3051 | 1059 | 3563 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
Q04747 | 1.00e-266 | 7 | 3051 | 1 | 2515 | Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3 |
O30408 | 1.22e-260 | 9 | 3053 | 6 | 2520 | Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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