CAZyme Information: MGYG000003687_02220

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_02220
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1548		173468.15	4.565

Genome Property

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

• Gene Location: Start: 78725; End: 83371 Strand: +

Full Sequence      

MAGGQTEGELETAAGAEMMERDNLSEGVSLKSDSPPDSEAASEPATGLRLHTVLALDNES
LYTGDTTDVDHINEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAAYRRDYRLSEFPVR
LLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDFSRLHGWIRDYQITVFESTPALIV
PFMQHVHEQGLDMSSLELLITSSDSCSVTDYQVLQERFGADIRIINSYGVTEAAIDSSFY
DEELLKLPSSGHVPIGQAWLNARFYIVDSQLNPVPIGVLGELCIGGAGVARGYLNRADLT
AEKFVANPYVPGERLYRTGDLARWMPDGHVDFIGRMDDQVKIRGFRIELGEVEAQLLAVA
GIEKAIVTAWENEDGDKDLCAYVVASEALNLPELRSTLQPKLPGYMIPTYVVPLDRFPLT
PNGKIDRKALPAPEARLEGGTEYVAPRTELEEQLVRIWQSVLNHHQIGIQDNFFEVGGHS
LRATTLMAKIHQELNHKLALRDIFQYPTIEQLVQVMGEDRTQQTYVSIPVAEEREYYPVS
SAQKRMYVLSHLEGGEVSYNMPGALIIEGSLDKKRLEQAFRQLIARHEALRTRFEMVDGE
VIQWIESSAPFSVEYVQASEEETPQYVQDFVRAFDLAQAPLLRVQLIENGPGRHVMLYDM
HHIISDGVTEGIIVQEFSQLYEGQELPPLRIQYKDYAVWQHADMQSERLRAQESYWLKTM
SGEIPALDMPTDFTRPAVQRLEGTRFEFAIRMEDSEQLKQLAAQTGSTLYMVLLAAYSTL
LHKYTGQEDIIVGTPIAGRPHAELGSLVGVFLNTLAIRNYPCGDKTFLDYLQEVKEHALR
AYEHQEYPFEELVEKLNLTRDTSRNALFDTMFELKTFEQQEFELEGLTFKPYPTDNPTSK
FDLTLDAVEQPEGILCSLEYSTALYKPETIARFAQHFTELIRAITLHPQQPLAALDMVTV
EEKAQILYGFGDVGVSEVAAEAEVLFHAYVEEQAQLVPDHVAVVYEEQQLTYRQLNERAN
QLTRRLRKEGIGRESIVGILSERSVDMLVGVLAVWKAGGAYVPLDADYPSERIRFMLEDS
GATVLLTQTSLQERTQAWLNESQGALGEGKTEGELETAVSAETMERDRLNEGVSLKSDSK
SGREAASELATGLRLHTVLALDDESLYTGDVTDVDHINEPHDLAYVIYTSGTTGRPKGVM
IEHRSLVNTAAAYRRDYRLNQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRI
DPSRLYGWIRDYQITVFESTPALIVPFMQHVYEHGLDMSSLELLITSSDSCSVTDYRVLQ
ERFGADIRIINSYGVTEAAIDSSFYDEELSKLPSSGNVPIGQAWLNARFYIVDSQLNPVP
IGVLGELCIGGIGVARGYLNRADLTAEKFVANPYVPGERLYRTGDLARWMPDGNVDFIGR
MDYQVKIRGYRIELGEIETAIQRVPGVRQAVVIDRTDERGHKYLCGYITGETELRIEEVQ
ATLEAGLPAHMVPARLMRLETIPLTSNGKIDRKALPEPEGSIHTGAAM

Enzyme Prediction     

No EC number prediction in MGYG000003687_02220.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1020	EntF	0.0	753	1465	4	642	Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].
cd05930	A_NRPS	0.0	998	1535	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.
cd17655	A_NRPS_Bac	0.0	991	1539	4	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	75	1541	2145	3544	peptide synthase; Provisional
cd17650	A_NRPS_PpsD_like	0.0	998	1535	1	447	similar to adenylation domain of plipastatin synthase (PpsD). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	3.04e-281	78	1547	1161	2588
BAY30132.1	1.15e-184	446	1536	2144	3208
BAY90071.1	2.29e-183	403	1536	2075	3197
BAZ00088.1	7.61e-183	436	1536	2124	3206
BAZ75991.1	7.61e-183	436	1536	2124	3206

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	5.10e-293	62	1542	331	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]
6MFZ_A	3.46e-292	62	1546	331	1723	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	2.05e-193	537	1535	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]
5U89_A	1.20e-180	67	967	161	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6OYF_A	6.25e-165	538	1449	4	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
P39847	0.0	78	1539	606	1994	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P27206	0.0	53	1539	1625	3028	Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
P39845	0.0	62	1538	570	1997	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P39846	0.0	62	1544	584	2001	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	75	1548	605	2003	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3

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
1.000047	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_02220.