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CAZyme Information: MGYG000001095_02660

You are here: Home > Sequence: MGYG000001095_02660

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 Chryseobacterium gambrini
Lineage Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Chryseobacterium; Chryseobacterium gambrini
CAZyme ID MGYG000001095_02660
CAZy Family GT2
CAZyme Description Dimodular nonribosomal peptide synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1468 MGYG000001095_441|CGC1 170273.68 5.2903
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001095 4128611 MAG Sweden Europe
Gene Location Start: 7413;  End: 11819  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001095_02660.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12467 PRK12467 1.14e-175 3 1366 52 1441
peptide synthase; Provisional
cd05930 A_NRPS 7.42e-157 470 933 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.
cd12116 A_NRPS_Ta1_like 2.34e-153 470 933 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.
PRK10252 entF 1.77e-150 3 1022 10 1045
enterobactin non-ribosomal peptide synthetase EntF.
PRK12316 PRK12316 1.27e-147 7 1442 1563 3021
peptide synthase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFZ04852.1 3.11e-119 234 1018 368 1179
BAY90071.1 3.96e-103 3 1073 2238 3324
QND46664.1 1.61e-102 257 1422 812 2017
ACX49739.1 1.32e-94 1 1330 10 1376
BAZ00088.1 4.32e-93 237 1042 366 1196

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5U89_A 1.10e-133 431 1339 3 932
Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
4ZXH_A 5.09e-109 7 1004 23 1026
ChainA, ABBFA_003403 [Acinetobacter baumannii AB307-0294],4ZXI_A Chain A, Tyrocidine synthetase 3 [Acinetobacter baumannii AB307-0294]
2VSQ_A 4.13e-107 7 1022 19 1039
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFW_A 2.05e-101 455 1427 204 1173
Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A 2.78e-101 455 1427 204 1173
Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45745 5.57e-168 2 1407 10 1438
Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P27206 1.84e-165 3 1424 8 1451
Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
Q9R9J1 1.07e-158 7 1447 2502 3942
Mycosubtilin synthase subunit A OS=Bacillus subtilis OX=1423 GN=mycA PE=1 SV=1
P39845 1.04e-155 2 1443 7 1462
Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P0C064 2.08e-154 2 1442 14 1470
Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB 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
1.000054 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001095_02660.