CAZyme Information: MGYG000003687_02211

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_02211
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit D

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2608	MGYG000003687_8|CGC2	294303.78	4.7935

Genome Property

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

• Gene Location: Start: 50412; End: 58238 Strand: +

Full Sequence      

MTQQDVQLFSLSQPQQRIWYTELLYPHRNTSTIIGTVKIRGTVRIDALQQAMNRVIAQND
SFRIKITAQDGIPYQYVEPFTAENIETLQVTPEEANEWLKRHNPQPFSLLDSQLYRFVIL
QLGVEETWFNFKMHHIISDGVSMNQAINEITGHYMNIVHGTGQDAPTKGNPYLDFIQVEQ
SYEQSDRYQKDKTYWTEKFADLPETTGLKSYNPLTLSTAARRESFILKHELYRGVTAFCE
EHKISIFTFFLAALYIYLHKVTGEQDLTVGTLYANRTSKKEKDTIGMFVSTVATRLLVEP
ESELLAFLQGVGKEQASILRHQRYPYNKIIQDLREQQSSLDIQRLFGASIQYRTLSFSRF
DEAIQQVDNDFCGDTVNDFDIHMVEMLDDDRLVLYLDYRTELFSEQEIARIIQQFLSVAE
HMVQGPHKRIEELSLISEEERVEIVDVFNATAVEYPHEAGIHELFEEQAARTPNQTAVVS
DNAHLTYGELNVKANRLAHTLRGNGVTAERTVGIVAERSVDMIVGMLAILKAGGAYVPID
PDYPAERVRYLLEDSGAELLLVQHAKQQPEDYTGIVLDLSDAAVYGAENNQDANNIHGEQ
NEASHADFTYYSNLKNDLLKESSSSVVDSTTGAHTFGNRLAYLMYTSGTTGQPKGVMVEH
RNVVRLVKNTNYAQLGADTRILQTGAVVFDASTFEIWGALLNGGQLVLVSQDVILDAPKL
KEAVRSHGITTMWLTAPLFNQLSQQDLELFEGVQELLVGGDVLSVPHINRVLEAHPSLRI
INGYGPTENTTFSTTHAIAGVQSEAVPIGRPIHNSTAYVVDRSMQLQPVGAWGELIVGGD
GVARGYRNRPDLTAEKFIDSPFRSGERCYRTGDLVRWNEDGTLEYKGRIDAQVKIRGYRI
ELGEVEAQLLKLEAVQEAVVIAREDEQGQKQLCAYVVTLADITASELRSALSQELPGYMV
PSYFVQMEQLPLTPNGKVDRRALPQPEGSVDSGEDYVAARNEVERILVSVWQSVLGIEQI
GVLDNFFHLGGDSIKAIQVSSRLLQNGYKLEMRELFQYPTIAELNGRVQRVTRVSDQGEV
RGNVALTPIQHWFIEQQPSNPEHYNQALMLHREDRLDETALHQTLQCIVEHHDALRIVFR
QNAEGGYEAWNRGVQEGELYNLEVVDYTQESDFAHLLESKASEIQSSIHLHEGPLVKLGL
FRCTDGDHLLVAIHHLVVDGVSWRILLEDLASGYEQALRGESVRLPNKTDSFRLWADQLS
TYATSAALEKERAYWEQVERAGAAQEALPKDYTRKSQAKPQLRDDRTLTVAWTVEETEQF
LKQAHRAYNTEANDLLLTALGTAVQEWAGIGQVLVNLEGHGREAILPDMDITRTVGWFTS
QFPVVLDMGEDRNVGQRVKNVKEGLRRLPHKGIGYGILRYLADRAEEATFVAEPEISFNY
LGQFDQDLKQNAFRMSPYSVGASMSDTLTKRYALDINGMITDGALELTISYSNKMFMKKS
VKKLADLLQESLREVLAHCVAKELPELTPSDLSFQGLTAVELDHIVEQTAAAGELENIYS
LTPMQKGILFHGFMEPQSGAYFEQATFDLQGSFQVEAFAESLNQLVGRHQIFRTNFYSGW
NEQPLQVVYRHKAAGFRFEDIRSMGQEEQDAYLADFAERDKAEGFHFSSGELMRVSILRT
GEESYRFVWSFHHILMDGWCLFLVVGEAFHTYFAILEDRKPELTPVTPYSEYIEWLDRQD
NAEAERFWSDYFAGFEQQTVLPQVKQLDGHAKAYEADKLSFTLGREVTERMNKLVKQKQV
TVNTFLQAAWGVVLQRYNNSRDVVFGSVVSGRSADIPGIDKMIGLFINTVPVRVHSEKEM
TFAGLMKQLQEQALASRAYETYPLYEIQALTEQKQDLVNHIIVFENYPVEQRMEQMGSRG
NNGFTIANASMSEQTNYDFNITVVPGDEIHVHLEYNAQVLERTAVEQIREHLLHMIEEAI
HRPDALVDELELVTTAEKAKIIDGFGSVGVAAWSDEKESELLFHAYVEEQAQLVPDHVAV
VYEEEQLTYRELNERANQLARRLRNEGIGRESIVGILSERSVDMLVGVLAVWKAGGAYVP
LDADYPSERIRFMLEDSGATVLLTQIGLQERAQGWLEESQWAMGEGKSEGVLETAVSAET
MERDRLNEGVSLKADSKSDSEAASEPVTGLRLRTVLALDDESLYTGDVTDVDHINEPHDL
AYVIYTSGTTGRPKGVMIEHRSLVNTAAAYRRDYRLNQFPVRLLQLASFSFDVFVGDIAR
ALYNGGTMVICPKDDRIDPSRLYGWIRDYQITVFESTPALIVPFMQHVHEHGLDMSSLEL
LITSSDSCSVTDYRVLQERFGADIRIINSYGVTEAAIDSSFYDEELSKLPSSGNVPIGQA
WLNARFYIVDSQLNPVPIGVLGELCIGGAGVARGYLNRADLTAEKFIANPYVPGERLYRT
GDLARWMPDGNVDFIGRMDYQVKIRGYRIELGEIETAIQRVPGVRQVVVIDRTDERGHKY
LCGYITGETELRIEEVQAALEAGLPAHMVPARLMRLETIPLTSNGKIDRKALPEPEGSIH
TGAAMWNRVLRWSKYWLRYGPQCLAWRP

Enzyme Prediction     

No EC number prediction in MGYG000003687_02211.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19543	DCL_NRPS	0.0	1558	1983	1	423	DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (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). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as 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. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
cd17650	A_NRPS_PpsD_like	0.0	2035	2572	1	447	similar to adenylation domain of plipastatin synthase (PpsD). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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.
cd12117	A_NRPS_Srf_like	0.0	463	983	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.
PRK12316	PRK12316	0.0	11	2578	52	2504	peptide synthase; Provisional
PRK12316	PRK12316	0.0	6	2591	2600	5086	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAZ00088.1	1.38e-207	194	2573	318	3206
BAZ75991.1	1.38e-207	194	2573	318	3206
BAY90071.1	3.32e-206	194	2573	317	3197
BAY30132.1	2.62e-205	194	2573	318	3208
QND46664.1	1.48e-174	537	2584	1	1517

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	1.97e-208	454	2579	200	1719	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]
2VSQ_A	2.66e-208	1554	2576	8	958	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFZ_A	8.73e-208	454	2583	200	1723	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
5ISW_A	8.08e-153	997	1550	1	558	Structureof the apo PCP-E didomain of the gramicidin S synthetase A [Brevibacillus brevis],5ISX_A Structure of the holo PCP-E didomain of the gramicidin S synthetase A [Brevibacillus brevis],5ISX_B Structure of the holo PCP-E didomain of the gramicidin S synthetase A [Brevibacillus brevis]
6MFX_A	1.55e-138	454	1405	200	1086	Crystalstructure of a 4-domain construct of a mutant 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
P39847	0.0	9	1545	1058	2548	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q70LM4	0.0	11	2583	1059	3541	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
Q0VZ70	0.0	11	2573	25	2975	Chondramide synthase cmdD OS=Chondromyces crocatus OX=52 GN=cmdD PE=1 SV=1
Q70LM5	0.0	11	2579	1076	3548	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
P39845	0.0	9	2594	6	2028	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2

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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_02211.