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CAZyme Information: MGYG000000012_00952

You are here: Home > Sequence: MGYG000000012_00952

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
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis
CAZyme ID MGYG000000012_00952
CAZy Family GT2
CAZyme Description Polyketide synthase PksN
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
5514 612469.92 5.5043
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000012 4053580 Isolate United Kingdom Europe
Gene Location Start: 941358;  End: 957902  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000012_00952.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1020 EntF 0.0 256 923 1 642
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].
cd17646 A_NRPS_AB3403-like 0.0 496 995 1 488
Peptide Synthetase. 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.
COG3321 PksD 0.0 4101 5193 3 1030
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism].
PRK10252 entF 0.0 34 1083 9 1047
enterobactin non-ribosomal peptide synthetase EntF.
COG3321 PksD 0.0 1116 2148 3 1028
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAY90071.1 1.07e-265 216 1618 312 1714
BAZ00088.1 3.60e-263 181 1618 277 1715
BAZ75991.1 3.60e-263 181 1618 277 1715
BAY30132.1 3.67e-263 181 1618 277 1717
AFY93865.1 1.22e-216 384 1609 214 1446

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MHL_A 2.37e-293 1114 1712 22 612
Crystalstructure of ketosynthase twelve from bacillaene polyketide synthase in Bacillus amyloliquefaciens [Bacillus amyloliquefaciens],6MHL_B Crystal structure of ketosynthase twelve from bacillaene polyketide synthase in Bacillus amyloliquefaciens [Bacillus amyloliquefaciens]
5ELP_A 8.77e-270 1110 1712 20 617
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]
4NA1_A 2.99e-252 2602 3207 24 632
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]
4NA2_A 6.54e-251 2602 3207 24 632
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]
4Z37_A 2.79e-188 2594 3207 13 632
Structureof the ketosynthase of module 2 of C0ZGQ5 (trans-AT PKS) from Brevibacillus brevis [Brevibacillus brevis NBRC 100599]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P40806 0.0 34 4541 695 4997
Polyketide synthase PksJ OS=Bacillus subtilis (strain 168) OX=224308 GN=pksJ PE=1 SV=3
Q2T4N2 0.0 1 3206 74 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 27 5514 1 5488
Polyketide synthase PksN OS=Bacillus subtilis (strain 168) OX=224308 GN=pksN PE=1 SV=3
Q2T4N1 0.0 1117 5470 14 4393
Polyketide synthase ThaG OS=Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) OX=271848 GN=thaG PE=2 SV=1
P40872 0.0 1037 4724 319 4129
Polyketide synthase PksM OS=Bacillus subtilis (strain 168) OX=224308 GN=pksM PE=1 SV=4

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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000012_00952.