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CAZyme Information: MGYG000004381_00539
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Lachnospira sp900772425 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp900772425 | |||||||||||
| CAZyme ID | MGYG000004381_00539 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Linear gramicidin synthase subunit D | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 246191; End: 250492 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd05930 | A_NRPS | 3.89e-167 | 467 | 940 | 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. |
| PRK12467 | PRK12467 | 7.74e-161 | 6 | 1019 | 52 | 1092 | peptide synthase; Provisional |
| PRK12316 | PRK12316 | 2.52e-159 | 6 | 1027 | 2605 | 3625 | peptide synthase; Provisional |
| PRK12467 | PRK12467 | 5.45e-157 | 6 | 1029 | 1119 | 2168 | peptide synthase; Provisional |
| cd17655 | A_NRPS_Bac | 2.59e-156 | 457 | 944 | 1 | 490 | bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QND46664.1 | 3.04e-122 | 97 | 1026 | 1715 | 2664 |
| BAY90071.1 | 1.35e-111 | 225 | 1084 | 352 | 1233 |
| BAY30132.1 | 2.43e-111 | 225 | 1026 | 353 | 1182 |
| AFZ04852.1 | 1.06e-110 | 214 | 1026 | 347 | 1185 |
| BAZ00088.1 | 5.89e-110 | 225 | 1111 | 353 | 1262 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MFZ_A | 3.04e-138 | 4 | 1024 | 786 | 1797 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
| 2VSQ_A | 5.49e-117 | 32 | 1033 | 39 | 1048 | Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis] |
| 1AMU_A | 6.54e-115 | 434 | 971 | 20 | 555 | PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis] |
| 4ZXH_A | 4.32e-113 | 6 | 1031 | 19 | 1051 | ChainA, ABBFA_003403 [Acinetobacter baumannii AB307-0294],4ZXI_A Chain A, Tyrocidine synthetase 3 [Acinetobacter baumannii AB307-0294] |
| 5U89_A | 6.04e-112 | 432 | 1031 | 4 | 609 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q70LM4 | 8.30e-158 | 6 | 1433 | 3641 | 5079 | Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1 |
| P0C064 | 3.40e-150 | 2 | 1024 | 3140 | 4160 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
| P0C063 | 7.16e-148 | 2 | 1024 | 3141 | 4161 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
| O30409 | 3.78e-142 | 2 | 1030 | 2091 | 3117 | Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1 |
| P39845 | 1.05e-139 | 4 | 1027 | 6 | 1035 | Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000067 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |