CAZyme Information: MGYG000001518_03664

Basic Information

• Species: Gorillibacterium timonense
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Gorillibacterium; Gorillibacterium timonense
• CAZyme ID: MGYG000001518_03664
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
764		86867.04	4.9006

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001518	5263339	Isolate	not provided	not provided

• Gene Location: Start: 1224156; End: 1226450 Strand: +

Full Sequence      

MMNTVLSKEHLELLQQLNNTKLEYQTDKTIHQLFEEQVCRNPDQVAASYDRCRMSYDELN
KKANQLARQLRCEGVGPGTVVGLLAGRSLDMLVGVFAVMKAGGAYLPLDPAYPQARIMQM
IEDSETKVILTHQSVEISLAYTGKVLQIDNPSLYETDDSNLEHVNESTDMIYLIYTSGST
GKPKGVMIHHQAVHNFIEGMTRLIPFSPGSFIVSLTTISFDIFVLESLLPLTKGMSIVIE
DPRQFPLTLNGQKIHALQTTPSTMKLILDRDESVAYIKELDFLLLGGEPLPEKLLRDLRE
ITSARIFNMYGPTETTVWSSVKEVTDSQIITIGRPIANTQLYILDDEGNRAPSGEAGHLY
ISGDGLSQGYYRNRELTENRFVDNPFIPGKRMYKTGDIGKLLPSGEIQFLGRADQQVKIR
GFRIELGEIENILSQHPYVDECVVEAKGAQDHERYLVAYYRSEHALVVSELIVHLKGQLP
DYMIPGFYIKLQEMPLTPNGKIDRKRLLEPDRTRPYMSVPYSAAANGTETLLKEIWEQVL
RLDQVGMNDNFFDLGGNSILLAQMYRQVEQAFDVKLDIADLFAFPTVAKLSQLLTNMSSS
WDGLNSQPDEYERQEWFFLEEYVRLFTSAETEITAYDMALSLFLFVLHEGYGQERVTVRS
ALLEAEEVSIQMPNHQMERLEELFRSVSRQRLQRLAEPEGEWVVTCRMTSNEWIRLVLSR
DDDKLHLHARSRYATVKNKDVSSLFDSYFTLTQGLLKTGEVNGQ

Enzyme Prediction     

No EC number prediction in MGYG000001518_03664.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	32	511	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.
cd05930	A_NRPS	0.0	42	507	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	9.63e-172	42	507	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.
cd12117	A_NRPS_Srf_like	3.74e-168	32	507	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.
PRK12467	PRK12467	1.20e-161	6	642	491	1147	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFZ04852.1	3.54e-127	8	594	564	1183
QND46664.1	9.92e-112	7	594	2052	2662
AFY93865.1	1.61e-109	24	597	327	932
BAY30132.1	1.03e-106	9	604	2689	3306
BAZ75991.1	8.61e-106	4	604	2684	3304

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AMU_A	1.09e-124	17	540	28	555	PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis]
5U89_A	1.70e-124	6	590	3	598	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
5ES5_A	2.29e-116	27	600	202	770	Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis]
6MFX_A	1.93e-114	27	666	204	837	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	5.16e-114	27	666	204	837	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9I9	6.81e-136	5	590	238	837	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
O30409	5.21e-135	9	617	1481	2093	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P40806	9.05e-133	29	608	1155	1741	Polyketide synthase PksJ OS=Bacillus subtilis (strain 168) OX=224308 GN=pksJ PE=1 SV=3
P0C062	3.61e-132	17	625	28	641	Gramicidin S synthase 1 OS=Brevibacillus brevis OX=1393 GN=grsA PE=1 SV=1
P0C061	9.87e-132	17	625	28	641	Gramicidin S synthase 1 OS=Aneurinibacillus migulanus OX=47500 GN=grsA 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001518_03664.