dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003687_00487

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Basic Information help

Species

Paenibacillus polymyxa

Lineage

Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa

CAZyme ID

MGYG000003687_00487

CAZy Family

GT2

CAZyme Description

Surfactin synthase subunit 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1091	MGYG000003687_2\|CGC1	123906.48	5.4838

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003687	5656034	Isolate	China	Asia

Gene Location

Start: 5034; End: 8309 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003687_00487.

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
PRK05691	PRK05691	3	1049	3248	4308	peptide synthase; Validated
PRK12467	PRK12467	3	1046	2637	3669	peptide synthase; Provisional
cd05930	A_NRPS	483	964	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	29	1053	1133	2167	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	473	964	1	483	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAY30132.1	3.87e-135	10	1049	2244	3294
BAZ00088.1	2.36e-134	10	1024	2242	3266
BAZ75991.1	2.36e-134	10	1024	2242	3266
BAY90071.1	1.06e-133	10	1046	2233	3280
QND46664.1	2.56e-133	119	1055	1719	2668

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSQ_A	1.63e-246	1	1060	1	1050	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFZ_A	3.71e-147	1	1053	774	1801	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6P1J_A	3.83e-127	41	964	35	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
6MFY_A	4.03e-127	1	970	774	1718	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]
7LY7_A	5.32e-113	3	1051	10	1018	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O68008	1.36e-250	6	1049	2	1032	Bacitracin synthase 3 OS=Bacillus licheniformis OX=1402 GN=bacC PE=3 SV=1
O68006	1.52e-249	4	1059	4201	5247	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
Q08787	3.56e-247	1	1060	1	1050	Surfactin synthase subunit 3 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAC PE=1 SV=2
P0C064	9.79e-230	1	1057	1	1049	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	2.09e-228	1	1057	1	1049	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003687_00487.