CAZyme Information: MGYG000002490_03372

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_03372
• CAZy Family: GT2
• CAZyme Description: Dimodular nonribosomal peptide synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2402	MGYG000002490_30|CGC3	262605.22	5.0878

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002490	6537383	Isolate	Japan	Asia

• Gene Location: Start: 146544; End: 153752 Strand: +

Full Sequence      

MHDLDGGRWPLSGAQSGIWFAQQLDPDNPIFNTGEYIDIRGPVDPDRFETAVRQAVMEAE
ALHARFEEDQDGPWQTIVPSSDWTMHRIDVSSEEDPHAAAEALMKHDLAQPVDLRRGPLF
TEALFKLAPDRFYWYQRIHHIVIDGYGFSLLTRRAAQIYTALAHDLPFSEGAFGSWRSVL
KEDAAYRASERLERDRQFWLARFPDHPEAASLGDRTQRTSRSFLRQSMELPSSVMDAWQA
AASGMGTSWPDAVLAAAALYVHRLAGTDDVILGVPMMCRLGSAALRVPGMVMNLLPLRAA
VRPDMSVSELVGQISGNMREIRRHQDYRHQDLRRDLKLVGDNRRLFGPLINIMPFIEELN
FAGYRGSIRNLAAGPVDDLTIHVSCGSSGSGPRIDFDANPAIYDAGELSAHLRRFLHVLD
KLAASDPGQPIGRLDLLLPEERLQVVDAWNDTAHRLAQWSVPALFEEQAASTPDAVAAIF
EDTSLRYADLNARANRLAHLLIAHGAGPDRIVALALPRSLEMVIAILAVHKAGAAYLPID
PDYPPARIAYMLNDAAPMCLVTVQEADSRLSGSGPMPKILMDEPATRDRLERQAEHNPND
ADRICRLSPLHPSYVIYTSGSTGRPKGVLLTFEGLANLLLCMRGRFALDDRDRLLSVTTI
SFDISVMEVLLPLTTGASIDIAPKDTILDPQALARIIKETGATIMQATPTLWQALAASHP
GSFDGLTVITGGEALPIGLKLALQDLDCEVNNQYGPTETTIYSTAALLGPERTGKPSIGG
PIWNTRLYVLDAALQPVPPGVAGELYIAGAGLARGYLGRPELTAERFVADPFGPPGTRMY
RTGDLVTWLADGSIDYLGRADHQIKLRGFRIETGEIEDLLVRHADVAQAAVIVREDRPGE
RRLAAYVVPASPSGIDPDALRRYAAGQLPDYMVPAAIVMLDAMPLTPNKKIDRKALPMPD
SGQAAAGRGPRTPQEEMLCALFAEALGLPRVGIDDDFFALGGHSLLAGRVILRIRESLGA
DLSIGSLFEEPTVAGLVRRLDDSREARPAMRRAKREDDIPLSFAQRRLWFLYRLEGPAPT
YNIPLVARLSGELDIRALEAALGDVADRHETLRTVFPNDASGASRQLILDAGEARPRLIL
TKTSEAELPERLKEAVRYRFRLADEPSLRAELFELGPNEYVLLLLLHHIAGDGWSLSPLT
RDLSAAYAARSRGEHPAWPPLPVQYADYAIWQERLLGSGGDADSLMARQLEFWTRTLTGL
PEELDLPADYPRPAAASHQGGTIRFHINKELHGQLLDLARAGKASLFMVLQAALAVLLTR
LGAGTDIPIGSPITGRNDDALDGLVGLFINTLVLRTDTSGDPSFRELLARVREVNLNAYA
HQDVPFERLVEAVNPVRSRSRHPLFQIMLVLQNTPAPALDLPGVAASLQLESADTAKFDL
TVELQERRDANGGPDGLDGMVEYSADLFKRSTADALAARYVRVLESAAAAPDKPMGQLDI
LMPEERRRILTEWSAPEAAAQPPVTIPELFEAQAIRSPEAAAVVHEGSALSYEELNLRAN
RLAHLLMAEGVGPEQLVALALPRSIEMVVGVLAVLKAGAAYLPLDPDYPAERIAYMLEDG
APLCMVTNAQVSSRLPEAGGLPRIVLDEAAVHERLREQSSANPSAQERNGLLSPLSPAYI
IYTSGSTGKPKGVVIPHQNVVRLFASTRHWFRFGAEDVWTLFHSYAFDFSVWEIWGALLH
GGRLVVVPHTVSRSPDEFLRLLAQEGVTVLNQTPSAFYQLMQAEREQPGLGQTLSLRYVI
FGGEALELGRLEDWYRRHPDHAPRLINMYGITETTVHVSYNELDRDSAAPGASSLIGGPI
PDLRVYVLDGALQPAPPGTAGEMYVAGAGLARGYWGRPGLTAERFVADPFGPPGSRMYRT
GDVAKWLADGTLDYVGRADHQVKIRGFRIEPGEIEAVLARHPEVAQAAVVVREDRPGDKR
LAAYVVFAAGASLGPSELRRHAASQLPDYMVPSAIIGIDALPLTPNGKLDRQALPAPELA
LESDGGNPRTPQEEVLCDLFAEVLGVRRVGIDDSFFELGGHSLLAVRLISRIREALGREL
GIGSLFEAPTVAGTAERLDMDGGHSALQVLLPLRTYGAQLPLFCVHPAGGLSWCYAGLMK
HLGMDYPIYGLQARGIAQAEELPKTLEEMTSDYIEAVRSIQPHGPYRLLGWSLGGNVAHA
MAVQLQEEGEEVSFLAMLDAYPSHYLPIREEPDEEEALTALLALGGYDKDSIGGVPLTVA
NAIEILRSDSSALATLDEATILNLKKTYENSVRLLGAYTPRRFEGELLFFRSTIIPDWFD
PIEPEMWIPYIGGRIDRHDIACRHKDLCQPGPLAEIGATLLAKLNSANGAAARQDGRELI
HE

Enzyme Prediction     

No EC number prediction in MGYG000002490_03372.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF038078	NRPS_MxcG	0.0	8	1046	4	1049	myxochelin non-ribosomal peptide synthetase MxcG.
PRK12316	PRK12316	0.0	9	1046	4103	5145	peptide synthase; Provisional
COG1020	EntF	0.0	1287	1962	1	642	Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].
cd19538	LCL_NRPS	0.0	1058	1491	1	432	LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains. 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. 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.
PRK12316	PRK12316	0.0	1056	2258	1554	2726	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	9	2261	561	2805
ACX49739.1	0.0	10	1775	11	1816
BAY90071.1	4.88e-240	961	2249	2124	3414
BAZ00088.1	7.10e-240	971	2249	2140	3423
BAZ75991.1	7.10e-240	971	2249	2140	3423

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U89_A	0.0	438	1510	3	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFZ_A	3.32e-268	464	2111	210	1790	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	5.77e-252	464	2038	210	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]
6P1J_A	7.09e-213	1057	2034	4	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]
6N8E_A	4.52e-185	1034	2295	12	1250	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70LM5	0.0	9	2112	5187	7264	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
P39846	0.0	9	2121	11	2079	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P39845	0.0	9	2111	6	2070	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P39847	0.0	9	2111	11	2066	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P27206	0.0	9	2116	6	2079	Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4

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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002490_03372.