CAZyme Information: MGYG000003687_02213

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_02213
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1106	MGYG000003687_8|CGC2	124989.1	4.7184

Genome Property

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

• Gene Location: Start: 59602; End: 62922 Strand: +

Full Sequence      

MDFALDINGLIEDGELVFTIRYGTTQFRHETIARLGELLASGLREVIHHCVTQERTVLTP
SDVLLKQVTLDELEQLVEDTRDLGELENVYALTPMQKGMLFFSLMDENSAAYFEQASFEL
NGRFDVVTFGKSLDLLVQRHEALRTNFINSWKDEPVQVVFRNRSGQLYYEDLRGLEKEER
KARVEAFTLADKAKGFNLAEDALLRISILQTGDETYHFIWSFHHILMDGWCLSFMTQEVF
GSYLALRAGDEPVLEPVTPFSRFIEWLERQDREAALQYWRGYLADYEQQITLPQQKTLPK
SMQAGEYIAEDLDCEFQPELVAQIERVAKQNQVTINTLIQTVWGVLLQKYNNSTDVVFGS
VVSGRPGDIPGVEHMIGLFINTIPVRVQSEPGETFVELMKRTQRQALASNAYDAFPLYEI
QALTEQKQDLINHIMIFENYPVEQQVEQLGSDGQDPFTISNVVSTEETNYDLNVVVMPGE
GIKIRFMYNTLSFDQAGIERLYGHFARLLEQISLNPHVRVEELELLTAAEKQQIIAAFND
TACAFPSHQTIHQLFEEQVECTPDQVALVFEHRRLTYRELNERANSLARILQAQGVGPDK
LVGLMVQRSVEMIVGLLAVLKAGGAYVPIDPEFPSSRIQYMLEDSEATVLLTRRDLAEEH
HCHANALFLEDAALYQGENSNLESIAKPEHLAYVIYTSGSTGNPKGVMLQHRSVLNFITG
MREVIDFETSQTMLSLTTISFDIFVLETILPLLGGMTVVLGDHQHQVNPQALGELIAHHH
IEMLQMTPSRLQMLLGHEAGSRALQGVKAIMVGGEALPSKLLAALQEINGPRIYNMYGPT
ETTVWSTVQELTHAQQINIGRPIANTQIYILNANGELQPVGVPGELCIAGEGLARGYWKR
EELTAERFVNHPFAGDKADQERMYRTGDLARWMPDGNLEYLGRMDHQVKIRGYRIELGEI
ESQLLQVESVQEAVIMARTDETGQTQLVAYYVASQELGSSELRQELGQALPSYMVPSYFI
WLEQMPLTPNGKIDRKSLPAPEGSLHSGADYAAPRTVTERTLVAIWQSILGVPLSGFWTI
SLTWAAIRSRRFKSYRVRSRQATSWT

Enzyme Prediction     

No EC number prediction in MGYG000003687_02213.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	5	1076	1475	2535	peptide synthase; Provisional
cd17655	A_NRPS_Bac	0.0	553	1042	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
PRK12316	PRK12316	0.0	91	1072	51	1033	peptide synthase; Provisional
PRK12316	PRK12316	0.0	91	1076	2604	3575	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	0.0	553	1038	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAY30132.1	5.52e-164	96	1072	2253	3242
BAY90071.1	1.55e-162	96	1072	2242	3231
BAZ00088.1	1.30e-161	96	1072	2251	3240
BAZ75991.1	1.30e-161	96	1072	2251	3240
AFZ04852.1	2.49e-161	246	1070	293	1129

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSQ_A	2.93e-230	85	1071	8	986	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFZ_A	1.98e-182	48	1106	756	1778	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	2.50e-172	90	1038	6	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	4.90e-172	48	1045	756	1719	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]
6OYF_A	5.45e-140	96	952	9	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9J0	0.0	4	1076	1233	2298	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1
Q9R9I9	0.0	1	1070	1237	2299	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
P0C064	3.57e-264	86	1076	9	994	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	2.27e-263	86	1076	9	994	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q70LM6	1.61e-262	85	1098	5	1015	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000034	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
1065	1087