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CAZyme Information: MGYG000000012_00949
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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 | Bacillus subtilis | |||||||||||
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| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis | |||||||||||
| CAZyme ID | MGYG000000012_00949 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Polyketide synthase PksJ | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 899842; End: 914961 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd05930 | A_NRPS | 0.0 | 1168 | 1639 | 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. |
| cd20484 | C_PKS-NRPS_PksJ-like | 0.0 | 693 | 1122 | 1 | 430 | Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ. Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. 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 such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, 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. |
| cd12116 | A_NRPS_Ta1_like | 0.0 | 1168 | 1639 | 1 | 470 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase. 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 myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity. |
| cd00833 | PKS | 0.0 | 3339 | 3773 | 1 | 421 | polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits. |
| cd05906 | A_NRPS_TubE_like | 0.0 | 20 | 561 | 1 | 540 | The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents. 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. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. 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 |
|---|---|---|---|---|---|
| BAY90071.1 | 2.93e-259 | 882 | 2263 | 317 | 1723 |
| BAY30132.1 | 5.93e-259 | 882 | 2263 | 318 | 1726 |
| BAZ00088.1 | 1.81e-258 | 882 | 2263 | 318 | 1724 |
| BAZ75991.1 | 1.81e-258 | 882 | 2263 | 318 | 1724 |
| AFY93865.1 | 2.46e-230 | 1131 | 2249 | 307 | 1446 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4NA2_A | 0.0 | 3335 | 3949 | 20 | 637 | CrystalStructure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate [Bacillus subtilis subsp. subtilis str. 168],4NA2_B Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate [Bacillus subtilis subsp. subtilis str. 168],4NA3_A Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to a hexanoyl substrate mimic [Bacillus subtilis subsp. subtilis str. 168],4NA3_B Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to a hexanoyl substrate mimic [Bacillus subtilis subsp. subtilis str. 168] |
| 4NA1_A | 0.0 | 3335 | 3949 | 20 | 637 | CrystalStructure of the second ketosynthase from the bacillaene polyketide synthase [Bacillus subtilis subsp. subtilis str. 168],4NA1_B Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase [Bacillus subtilis subsp. subtilis str. 168] |
| 5KTK_A | 7.83e-302 | 3950 | 4468 | 1 | 519 | Ketoreductasefrom module 3 of the bacillaene synthase from Bacillus subtilis 168 [Bacillus subtilis subsp. subtilis str. 168] |
| 5ELP_A | 7.20e-298 | 1752 | 2356 | 19 | 621 | Ketosynthasefrom module 1 of the bacillaene synthase from Bacillus amyloliquefaciens FZB42 [Bacillus amyloliquefaciens],5ELP_B Ketosynthase from module 1 of the bacillaene synthase from Bacillus amyloliquefaciens FZB42 [Bacillus amyloliquefaciens],5ELP_C Ketosynthase from module 1 of the bacillaene synthase from Bacillus amyloliquefaciens FZB42 [Bacillus amyloliquefaciens],5ELP_D Ketosynthase from module 1 of the bacillaene synthase from Bacillus amyloliquefaciens FZB42 [Bacillus amyloliquefaciens] |
| 4J1Q_A | 1.91e-262 | 2668 | 3110 | 22 | 464 | Crystalstructure of a ketoreductase domain from the bacillaene assembly line [Bacillus subtilis subsp. subtilis str. 168],4J1S_A Crystal structure of a ketoreductase domain from the bacillaene assembly line [Bacillus subtilis subsp. subtilis str. 168] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P40872 | 0.0 | 1650 | 5004 | 268 | 3960 | Polyketide synthase PksM OS=Bacillus subtilis (strain 168) OX=224308 GN=pksM PE=1 SV=4 |
| Q2T4N2 | 0.0 | 663 | 3943 | 81 | 3458 | Polyketide synthase ThaH OS=Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) OX=271848 GN=thaH PE=3 SV=1 |
| O31782 | 0.0 | 695 | 4989 | 8 | 4512 | Polyketide synthase PksN OS=Bacillus subtilis (strain 168) OX=224308 GN=pksN PE=1 SV=3 |
| P40806 | 0.0 | 1 | 5039 | 1 | 5043 | Polyketide synthase PksJ OS=Bacillus subtilis (strain 168) OX=224308 GN=pksJ PE=1 SV=3 |
| Q05470 | 0.0 | 1588 | 5035 | 255 | 4537 | Polyketide synthase PksL OS=Bacillus subtilis (strain 168) OX=224308 GN=pksL PE=1 SV=3 |
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 |
|---|---|---|---|---|---|
| 1.000061 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |