CAZyme Information: MGYG000003687_02215

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_02215
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
903	MGYG000003687_8|CGC2	101087.34	5.0743

Genome Property

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

• Gene Location: Start: 65828; End: 68539 Strand: +

Full Sequence      

MGRYGGSYPQDQTLSSLFEQQVANTPDQTAVIFGSEMLTYHELNERANRLARTLRAQGVQ
PDQPVGILVHRSLDMIVGIYAILKAGGAYVPIDPEYPADRIRFMLEDSGAKLVLTQAHLA
EQASLSFDGQVLVLDRQEQDGKHIYHEDGSNLEPLAGPHHVAYVIYTSGSTGKPKGVMVE
HHSVLNRILWMHNRYGLSAEDTILQKTAFTFDVSVWELFWWSMVGSKVSLLSVGGEKNPE
DIVDTIARDGVSTMHFVPAMLHAFLEYVEQQPREVMQAKLGTLRHVFASGEALPPQHVAR
FQRLVSTLTGAKLVNLYGPTEATVDVSYFDCEPDEEYAVIPIGKPIQNIRLYIVKEGTEQ
LQPIGVAGELCIGGVGVARGYLNRPELTAEKFVKDPFAGGEAGYERMYRTGDLARWMPDG
NIEYLGRIDHQVKIRGYRIELGEVETQLLQVKSVREAVVMARTDETGQKQMVAYYVAGQE
LGASELRSELGRELPSYMVPSYFVQLEQMPLSPNGKIDRKALPAPEGSLQTGADYAEPRT
AQERALVAVWQSVLGLQTVGILDNFFDLGGDSIKAIQIASRTFQAGYKLDMKDLFQYPTV
AALAPHMHEVRRMANQEEVSGETALLPIQHWFFAQERERPQHFNQAVMLYRAEGFEETAI
RQVMDHLVKHHDALRMVFRQTSNGYTAWTRAVEEGTLYTLETVDYREQETYAEALEAKAT
EIQSSMDLSAGPLVKLGWFRTTEGDHLLIAIHHLVVDAVSWRILFEDFSTGYEQAIQGEP
VRLPYKTDSFQTWAQELSSYANRPEAASDASYWKQLEQAKAEAARLPKDFAYEGSLNADS
EVLTVEWTEAETQQLLKQAHRAYNTEVNDLLLTALGLALHNWTGAGHVLVNLEAMAGKRS
CQR

Enzyme Prediction     

No EC number prediction in MGYG000003687_02215.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17651	A_NRPS_VisG_like	0.0	18	523	1	491	similar to adenylation domain of virginiamycin S synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. 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.
PRK10252	entF	0.0	11	604	457	1042	enterobactin non-ribosomal peptide synthetase EntF.
TIGR01733	AA-adenyl-dom	0.0	39	459	1	409	amino acid adenylation domain. This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
PRK12467	PRK12467	0.0	7	607	3090	3672	peptide synthase; Provisional
PRK12316	PRK12316	0.0	2	604	4541	5136	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	3.70e-140	7	604	2068	2659
AFZ04852.1	3.50e-132	10	629	582	1199
BAZ00088.1	6.51e-126	8	609	2702	3294
BAZ75991.1	6.51e-126	8	609	2702	3294
BAY30132.1	2.19e-125	8	609	2704	3296

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.52e-174	7	605	1219	1795	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFW_A	2.52e-160	6	827	199	978	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	9.70e-160	6	827	199	978	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6P1J_A	5.28e-151	8	522	462	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]
5ES5_A	1.59e-149	6	603	197	760	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9I9	0.0	8	893	257	1125	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
Q9R9J0	7.28e-271	8	893	259	1118	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1
P09095	2.97e-252	8	893	23	882	Tyrocidine synthase 1 OS=Brevibacillus parabrevis OX=54914 GN=tycA PE=1 SV=2
Q70LM7	2.14e-245	7	893	1216	2077	Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1
P0C061	2.28e-242	8	893	35	892	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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_02215.