You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000147_02475
You are here: Home > Sequence: MGYG000000147_02475
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 | Bacillus paralicheniformis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis | |||||||||||
| CAZyme ID | MGYG000000147_02475 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | D-alanine--poly(phosphoribitol) ligase subunit 1 | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 674991; End: 690761 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd19543 | DCL_NRPS | 0.0 | 4210 | 4634 | 1 | 423 | DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (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). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as 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. |
| PRK05691 | PRK05691 | 0.0 | 34 | 1896 | 1128 | 3013 | peptide synthase; Validated |
| PRK05691 | PRK05691 | 0.0 | 38 | 2990 | 10 | 3085 | peptide synthase; Validated |
| cd05930 | A_NRPS | 0.0 | 4681 | 5152 | 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. |
| cd05930 | A_NRPS | 0.0 | 51 | 524 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QND46664.1 | 0.0 | 1217 | 3733 | 75 | 2665 |
| BAY90071.1 | 5.79e-296 | 15 | 2705 | 555 | 3305 |
| BAY30132.1 | 1.35e-280 | 936 | 3732 | 423 | 3296 |
| BAZ00088.1 | 1.71e-276 | 936 | 3732 | 423 | 3294 |
| BAZ75991.1 | 1.71e-276 | 936 | 3732 | 423 | 3294 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MFY_A | 0.0 | 2122 | 3654 | 202 | 1723 | 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] |
| 6MFZ_A | 0.0 | 2122 | 3733 | 202 | 1800 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
| 7LY7_A | 1.55e-294 | 631 | 1621 | 6 | 987 | ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris] |
| 7LY4_E | 1.60e-294 | 631 | 1621 | 6 | 987 | ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris] |
| 2VSQ_A | 3.06e-261 | 4201 | 5238 | 3 | 1039 | Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39846 | 0.0 | 1664 | 4198 | 3 | 2553 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
| Q04747 | 0.0 | 630 | 4200 | 4 | 3576 | Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3 |
| P94459 | 0.0 | 631 | 4203 | 6 | 3601 | Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2 |
| P39847 | 0.0 | 1672 | 4198 | 11 | 2548 | Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2 |
| Q70LM4 | 0.0 | 1671 | 5234 | 7 | 3611 | Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1 |
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 |
|---|---|---|---|---|---|
| 1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |