CAZyme Information: MGYG000003208_03987

Basic Information

• Species: Pseudomonas_E extremaustralis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis
• CAZyme ID: MGYG000003208_03987
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1372	MGYG000003208_70|CGC1	152228.23	5.8498

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003208	6254364	MAG	United States	North America

• Gene Location: Start: 14519; End: 18637 Strand: +

Full Sequence      

MDDQMAYRIMQRFIGLPLEQRKVYLQKMLQEGVSPANLPIPQVRLEATALPLSYAQERQW
FLWQLDPQSAAYHIPSALRLKGRLDIVALQKSFESLIARHESLRTQFRQVGEGMRQEIQP
TYAVVLEPETLAESQLKARVEQAIAHPFDLARGPLLRMTLLRLSELDHVLVLVQHHIISD
GASMQVMVEEVVQAYTAYSRGLEFELPALPIQYADYALWQRSWMEAGEKQRQLEYWQGVL
GGDQPVLELPLDRPRPASRSFRGAALDVVLDDQLAAGVRALAQREGATSFMVLLASFQAL
LHRYSGQRDIRVGVPTANRNRVETQPLVGFFVNTQVLKADVDEHTSALALLRQTRQRVLE
AQAHQDLPFEQLVEALRPQRSLSYSPLFQVMFNHQNRGTAHESEPGTSGLVLEGLDWESR
TAQFDLILNVSEEASGIGASFGYATDLFDAATVERMARHWRRLLGAMVAEPEALVDTLVM
LDAEERRQIVATWNATTTAYPLEKTVHQLFEEHAECTPHRPALAFGAMQLSYDALNRRAN
RLAHALITRGVGPDSLVGVAMERSVEMVVGLLAILKAGGAYVPVDPEYPKERQCYMLEDS
AVNLLLSQSHLTLPVTDNVQRIDLDGDGQWLDVYDEANPSVAVSGEHLAYVIYTSGSTGK
PKGAGNSHAALTNRLCWMQQAYALGASDTVLQKTPFSFDVSVWEFFWPLLSGARLVMAAP
GDHRDPAKLVEVIKREGVTTLHFVPSMLQAFLQHGPVGSCSSVKRIICSGEALPVDAQQQ
VFAKLPQARLYNLYGPTEAAIDVTSWTCVDEGKDAVPIGKPIANLGCHILDGHLEPVPIG
VLGELYLTGKGLARGYYRQPVLTAERFVASPFGAGERMYRTGDLARYRPDGVIEYAGRID
HQVKLRGLRIELGEIEARLLEHQWVRETAVLALDGTQLVGYVVLDEPLPHWRETLAAHLS
TYLPAFMVPAQWVLLENMPLSPNGKLERKALPRPEAGSQQRNYAAPHTALEQQIAQIWQQ
VLGVDRVGLDDNFFELGGHSLLLLVVKERLALQCGLVLTVNQLMTRSTVRALARSTLDER
EPSLIVDLNGCKGGPSLFLFHPSFGSVHCYKAIGMALRLEMPVQGIICRALMDPQSPVPT
WDAMVEDYARQILVTQPGGPYYLAGWSLGGNLSLQVAAYLEARGADVAFLGCIDAPPPMR
VKAFWDRDKWLKPAVESLGPGDKRVELLTVMLPESAQAITQAWQDIEHAGTAADQQWKAF
CEWAHLALGEVFVSLRDELRQGGELEVSWALKHMLDERLKDADYSPIAAPVSCWWAAQSK
SANDRHVICSALEEGIGHGVHASVVIDTTHDRIVDNPEFIASFVSALKGARH

Enzyme Prediction     

No EC number prediction in MGYG000003208_03987.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	30	1369	2615	3950	peptide synthase; Provisional
PRK12316	PRK12316	0.0	1	1074	1	1082	peptide synthase; Provisional
COG1020	EntF	0.0	270	922	1	641	Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].
cd19531	LCL_NRPS-like	0.0	49	471	1	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd17655	A_NRPS_Bac	0.0	508	995	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	6.79e-280	5	1194	1557	2784
BAZ00088.1	1.06e-245	52	1198	2247	3417
BAZ75991.1	1.06e-245	52	1198	2247	3417
BAY90071.1	2.30e-244	52	1198	2238	3408
BAY30132.1	4.62e-244	52	1198	2249	3419

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P1J_A	3.12e-287	51	991	7	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]
6OYF_A	1.85e-261	51	907	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]
6P3I_A	6.11e-253	51	907	4	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg [Eleftheria terrae]
6MFZ_A	3.97e-186	5	1080	746	1801	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A	9.05e-168	5	995	746	1716	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D9XF49	7.48e-251	35	1073	90	1144	Phosphinothricin tripeptide synthase PhsB OS=Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) OX=591159 GN=phsB PE=1 SV=1
Q70LM5	2.10e-244	30	1078	6219	7272	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
Q70LM6	4.41e-240	50	1074	3633	4669	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
O30409	3.34e-238	51	1345	5211	6463	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
Q70LM4	2.22e-236	50	1079	3639	4674	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD 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 MGYG000003208_03987.