CAZyme Information: MGYG000002356_04756

Basic Information

• Species: Bacillus_A wiedmannii
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A wiedmannii
• CAZyme ID: MGYG000002356_04756
• CAZy Family: GT2
• CAZyme Description: Dimodular nonribosomal peptide synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2385	MGYG000002356_46|CGC3	268156.02	4.7703

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002356	5414628	Isolate	Netherlands	Europe

• Gene Location: Start: 82811; End: 89968 Strand: +

Full Sequence      

MPNSQKVRHSLSSAQTGMWFAQQLDPLNPIYNTGEYVEINGNINQEIFELAVRKVVTEAE
VLHVRFEEDEIGPWQVIEELQFHMHFIDVRKEEDPEETAKIWMKNDLYMPVDLKTDKLFT
EALIQVENNRFFWYQRIHHIVMDGYGFSLLSQKVAKEYTSLIEEIRKNEKPFGSLAKVVQ
EDMEYRESKQFQEDRTFWLEKFADEPDVISLAKRAPRTSNGFLRETAYLSSSSTKTLLED
INVSLTNWPEFIVAVTSIYMHKLTGANDIILGLPMMGRLGSASIYTPSMVMNLVPLRITV
TPNITLAELLQQVSKEIREVRRHHKYRHEELRRDLKLLGENQRLFGPLVNVMPFDYGLNF
AGNRGITHNLSAGPVDDLSINVYKRFDENELMIHFDGNPLVYSDSELALHKERFMNVLEL
VINDYEKDVSIGNINITLPEENHKVLFEWNETKEAEDLITLPLLFEKQVQKNPNKIAVTC
NGVDLTYKELNERANELAHYLVEEGIGPNQFVALVFPRSIEMVVSMLAVLKAGAAYLPID
PEYPAERINYIVNDAKPACIITHSSVASTLVIENDIKKIELNSEKMKLALNTYSYMNIPL
RNDDSLLNPAYTIYTSGSTGNPKGVIVPMKALSNFLLAMDDMFSLHENDHLLAVTTFAFD
ISALEIYLPLISGASITIAQKEVIQEPSVLTALLQEERVTIMQATPTLWQALVTEYPERL
QGLNVLVGGEALPAHLANILKELGCSITNLYGPTETTIWSTFKNIDENEIGIPPIGKPIW
STDVYVLDAGLQTVPPGVIGELYIAGEGLANGYLGKPELTAERFVADPYGKPGKRMYRTG
DLVKWRNDGVLEYMSRADHQIKIRGFRIELAEIEMVLQRHEYIQQAVVMVREDRPNDKRI
IAYIVVEGSEGINLSEIRSYVSESLANYMVPSAFVVLEELPLTPNGKVNRKKLPAPDFNE
MNKERVARNPKEEILCDLFAEVLGVSRISIDDNFFEMGGHSLLASRLMARIRETLSVELG
IGKLFESPTVAELVKQLDQAKTARPAIKKVSRPNEVPLSFAQRRLWFLNCLEGPSPTYNI
PLVVRISGKLNEEALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMIITKTC
KDELESVLVEAVRYSFNLDVEPAVRLQLFTVNENEHVLLILLHHIVGDGWSLQPLTRDFT
AAYKARCQGNRVQLETLPVQYADYALWQQQLLGDETTEESLISTQLEFWKKELEGLPDQL
ELPTDYQRPIETSYRGETIHFQIDAGMHSRLVELARKNGVSLFMVLQAGLSALFTRLGAG
TDIPIGSPIAGRNDDALSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQSNLAAYENQDV
PFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEANFDAPDIKADLEIQSVGSAKFDLTFEI
SESNGVHGTPDGLHGLLEFSTDLYKRETVQQLVERFILLLDDAAKHPDQSIGTLEILTLA
ERNTVLEKWNGGFQIVPEMTLSQLFEKKVYINPNSIAVVFEDEKLTYEELNKKANKIARL
LIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCV
LTNSDVEIECDEELKILVDDVKTIKEIEKYSEDNIDEMERMKPLSPSHIAYVIYTSGSTG
RPKGVMIPHQNVVRLLGATDHWFQFDAEDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVP
HTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEIGQKLSLRYVVFGGEALEL
SRLEDWYSRHPHNAPKLINMYGITETTVHVSYIELDETIVSLRANSLIGCSIPDLKVYVL
DNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRK
DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHPKVEQVAVIVREDQPGDKRLVSYIVSS
NNEAIDTNEMRQFASDSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGP
RTPQEEMLCDLFTEVLSVPQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAA
PTVAGLAERLEMGNGQSALDVLLPLRASGDQLPLFCVHPAGGLSWCYAGLMKSLGTDYPI
YGVQARGIAKNEELPKSLEEMAADYLKHVREVQPHGPYRLLGWSLGGNVVHAMAAQLQNE
GEEVELLVMLDSYPGHFLPNTEAPTEEEALIALLALGGYDPDNMDGKPLTMESAVEILRK
DGSALASLEEETILNLKETYVNSVGLLGKYVPKVYNGDILFFRSTVIPDWFDPISPNTWL
NYLDGQIVQHDIDCRHKDLCQPGPLTEIGQVLAKYLQNKKGVSRV

Enzyme Prediction     

No EC number prediction in MGYG000002356_04756.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF038078	NRPS_MxcG	0.0	5	1043	1	1049	myxochelin non-ribosomal peptide synthetase MxcG.
PRK10252	entF	0.0	1054	2378	6	1296	enterobactin non-ribosomal peptide synthetase EntF.
cd17651	A_NRPS_VisG_like	0.0	1525	2027	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.
cd12116	A_NRPS_Ta1_like	0.0	473	953	1	470	The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase. 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 myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
cd19533	starter-C_NRPS	0.0	8	425	1	419	Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs). Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. 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 such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	430	2376	979	2929
ACX49739.1	1.74e-247	11	1767	12	1816
BAZ00088.1	8.40e-241	972	2377	2147	3562
BAZ75991.1	8.40e-241	972	2377	2147	3562
BAY90071.1	4.87e-240	972	2377	2138	3553

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U89_A	0.0	438	1506	3	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFZ_A	2.41e-267	433	2107	177	1794	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	5.92e-253	433	2030	177	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	8.64e-202	1051	2026	1	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	1.71e-166	1054	1938	1	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	9	2133	6	2088	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
Q70LM4	0.0	3	2111	2	2094	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
Q04747	0.0	4	2118	1053	3112	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P27206	0.0	9	2121	6	2092	Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
P39847	0.0	1	2107	1	2070	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC 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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002356_04756.