CAZyme Information: MGYG000002356_02951

Basic Information

• Species: Bacillus_A wiedmannii
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A wiedmannii
• CAZyme ID: MGYG000002356_02951
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1016		115410.56	4.7371

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002356	5414628	Isolate	Netherlands	Europe

• Gene Location: Start: 89; End: 3139 Strand: +

Full Sequence      

MEGQSLTYKELNDKANQVARVLRQKGVQPETIVGLMTERSSEMIIGLMGILKAGGAYLPI
DPAHPVDRIGSVLSDAKVDLLVTYGDIPSTLPYAGHVIDLTDQSIYQEEKTNLDVEMTSR
HLAYVIYTSGSTGVPKGVMVEHQQVNNFIHGMVNETQLGSYESILCLTTLSFDIFGLETL
APLTKGLTVVVSNEEESKEGEKLAALIERNEIEVMQSTPTRLKMLMENERFRFAMKKLKT
LFVGGEELSETLWNEVKGLDFPVFNMYGPTETTIWSTIKHMKETDSITIGKPIQNTQVYV
LDRHNQLVPEGVLGELCISGDGVARGYFNREELTREKFVPNPFVPGERMYKTGDLVRWLP
TGELAYAGRIDHQVKIRGFRIELGEIETQIISHPQVKEAVVAAKEDEQNQKYLCAYVVSH
ETLDKSGLKAYLKERLPDYMIPSYMMELDNIPLTNNGKINRTALPEPDINGLISGDYEAP
QTALQETLVTIWRDVLGVETIGIHDNFFDLGGHSLKATVVMSDIHKLLQIEVPLKEIFTS
PTIFELSGYIEKSTVNVYETIKLCEEQDFYETSSAQKRMYSVQQLDKGSTAYNMPGIFEL
EGEVDQNRIGTVFQQLVKRHEALRTSYETVDGEIVQKIWPTEEFQIISREHSATDIADIA
KSFIQPFELERAPLFRVELAVVSSKQYLMIDMHHIISDGVSMSLLLKEFTKLYNGESLEP
LRIQYKDFAQWQNAYLRSGGLDQQAAYWKKQFQGNVPVLHLPYDYERPVIQSFEGDSVHF
ILDEEMTEGLREVARKEGATLHMILLSAFNILLSKYSGQEDIVVGVPVAGRSHADLRNMM
GMFVNTLAMRNRPEKEKTFKGFLKEVKENSLQAYDNQSYQLEELIENIAVKRDISRNPLF
DVIFNLNNIEYEVDLKLDGVELKQVNLESDLSRVDLSLTGFESDSEIHLKLVYSTKLFKK
HTIHRAMEDLGTILTKVSQDSSTVLEEIQLFNIDEEKYILNEKNEMNNLRNAEFSF

Enzyme Prediction     

No EC number prediction in MGYG000002356_02951.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	2	468	19	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.
cd05930	A_NRPS	0.0	2	464	9	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	0.0	2	1004	534	1564	peptide synthase; Provisional
PRK12316	PRK12316	0.0	3	1004	2026	3047	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	0.0	1	464	18	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
QND46664.1	7.95e-181	2	1005	1031	2064
AFZ04852.1	1.20e-131	2	552	606	1185
ACX49739.1	2.07e-124	6	978	486	1498
BAY30132.1	7.61e-114	2	547	601	1177
BAZ00088.1	1.67e-111	2	547	601	1175

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U89_A	1.86e-208	2	1000	46	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFW_A	3.95e-197	3	988	228	1188	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	2.17e-196	3	988	228	1188	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFY_A	1.06e-192	3	997	228	1207	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	4.99e-192	3	997	228	1207	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0C063	2.54e-286	4	1000	1530	2528	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
P0C064	8.81e-286	4	1000	1530	2528	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O30409	5.91e-276	1	999	2558	3560	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
O68008	8.15e-270	2	1005	3022	4022	Bacitracin synthase 3 OS=Bacillus licheniformis OX=1402 GN=bacC PE=3 SV=1
O68006	1.99e-267	2	1000	2147	3135	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 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
1.000074	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002356_02951.