CAZyme Information: MGYG000003687_05490

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_05490
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
853		95081.75	5.7103

Genome Property

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

• Gene Location: Start: 6171; End: 8732 Strand: -

Full Sequence      

MFEKAESEAGALLLHMLRRIAFTDEERGTIQMAFEKETLFWNEKFGSDDYTLTRLPYSKA
PSSLTPIMTTVGGTLSEEVAQRVLQMSKGAPLATFMILLAGVQSLLYKYTGASDILVGMP
VVRKPTETRRSVNHTIILKNSLSAGATFKTLLSELRTSLPEAIQHQHIPFLKMTEKLDLQ
YADGITVVHTLVSLKELHLDEIGQNVVTDCSFEFSLTGGTIQLALSYNEHLYDSEFMTRV
VGHLNRLLAVGLHELELEIVRADMLSEDEKFQLLQSFNDTEKDYPRDRTIHQLVEEQAKR
VPEATAVVFEGRRLSYAELNERANRLARTLRSVGVLPNQLVGLMARRSLETVVGILAVLK
AGGAYVPIDPEYPEERIRYILENSNAQLLLTQRELLQQVPFEGTVLALDDEQAYSDDGSN
LEPASGPNDLAYVIYTSGTTGKPKGVMLEHRGLVSLKLMFADRLGITEHDRIVQFASLSF
DASCWEMFKALYFGAALYIPTAETILDTRLFESYMNEHAITAAILPPTYSAYLNPDRLPS
LTKLVTGGSAVSAEFVQQWKPKVHYFNAYGPTEASIVTTLWDADEEQSERRVIPIGRPLA
NHRIFILDTHLQLVPPGVDGELCVAGVGLARGYLNHPELTAEKFVEHPFAPGERLYRTGD
LARWLPDGNIEYLGRIDHQVKIRGFRIEIGEIEEQLLKIDSVQETIVIAREGKSGQELCA
YLVAGHPLTLGELRSALAQKLPNYMIPAHFVQLPRMPLTPNDKIDRKALPAPEGNALTGG
AYVAPRNEAERTLADVWQAVLNADRVGVTDHSSSWAETRSSPFKYLRGFIKPGTSWKSGI
CSNIRLFHSSACM

Enzyme Prediction     

No EC number prediction in MGYG000003687_05490.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17652	A_NRPS_CmdD_like	0.0	302	770	1	436	similar to adenylation domain of chondramide synthase cmdD. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
cd17649	A_NRPS_PvdJ-like	0.0	302	770	1	450	non-ribosomal peptide synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. 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.
cd17651	A_NRPS_VisG_like	0.0	294	770	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.
cd17646	A_NRPS_AB3403-like	0.0	291	769	1	488	Peptide Synthetase. 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.
PRK12316	PRK12316	0.0	35	810	237	1040	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFZ04852.1	1.29e-142	31	811	314	1139
BAZ00088.1	3.26e-135	12	811	280	1134
BAZ75991.1	3.26e-135	12	811	280	1134
BAY30132.1	4.42e-135	12	811	280	1136
BAY90071.1	9.26e-134	75	811	352	1133

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AMU_A	4.59e-183	269	803	20	557	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]
6MFZ_A	2.38e-151	30	811	937	1754	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
5N82_A	1.21e-148	284	676	33	427	Crystalstructure of an engineered TycA variant in complex with an beta-Phe-AMP analog [Brevibacillus parabrevis]
5N81_A	1.50e-146	284	676	33	427	Crystalstructure of an engineered TycA variant in complex with an O-propargyl-beta-Tyr-AMP analog [Brevibacillus parabrevis],5N81_B Crystal structure of an engineered TycA variant in complex with an O-propargyl-beta-Tyr-AMP analog [Brevibacillus parabrevis]
6P1J_A	1.50e-144	95	769	253	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9I9	8.03e-214	34	811	4	798	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
O30408	1.08e-203	33	811	2269	3067	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1
Q9R9J0	1.04e-196	33	811	3	791	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1
P09095	3.36e-194	284	811	23	555	Tyrocidine synthase 1 OS=Brevibacillus parabrevis OX=54914 GN=tycA PE=1 SV=2
O68008	5.50e-179	71	811	1261	2020	Bacitracin synthase 3 OS=Bacillus licheniformis OX=1402 GN=bacC 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_05490.