CAZyme Information: MGYG000002283_01241

Basic Information

• Species: Bacillus_A paranthracis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A paranthracis
• CAZyme ID: MGYG000002283_01241
• CAZy Family: GT2
• CAZyme Description: Dimodular nonribosomal peptide synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2385	MGYG000002283_1|CGC13	268101.99	5.0184

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002283	5102264	Isolate	China	Asia

• Gene Location: Start: 1212641; End: 1219798 Strand: +

Full Sequence      

MPNSQKVRHSLSSAQSGMWFAQKLDPLNSIYNTGEYVEINGNIHQDIFELAVRKVVMEAE
ALHVRFEEDEIGPWQVIEESQFHMHFIDVRKEENPEEAAKAWMKNDLSMPVDLKKDTLFT
EALIQVENNRFFWYQRIHHIVMDGYGFSLLSQKVANEYTSLIEETNKNEKTFGSLAKVVQ
EDMEYRESKQFQEDRAFWLEKFADEPDVVSLAERAPRTSNGFLRETACLSSSSTKTLLED
INISLTSWPEFIVAVTSIYMHKLTGENDIVLGLPMMGRLGSASIHTPSMVMNLVPLRLTV
TPNITLVELLQQVSKEIRDVRRHHKYRHEELRRDLKLLGENQRLFGPLVNVMPFDYGLNF
GGNRGITHNLSAGPVDDLSINVYKRFDQNELMIHFDANPEVYNGVELALHKERFMQLLEL
MINAYQKDESIGKINITLPEENHKVLLEWNETKEDDELISLPISFEKQVQKTPNKLAITC
DGVNFTYKELNERANELAHYLVEEGIRPNQFVALVFPRSIEMVTSMLAVLKAGAAYLPID
PEYPAERINYIVNDAKPVCIITHSSVSSKLVIENDMKKIILDDEETKLALHTYSRMNIEC
KNDVSILNPAYTIYTSGSTGNPKGVIVPMKGLSNFLMAMQQKFSLHEHDHLLAVTTFAFD
ISALEIYLPLISGASLTIAQKEDIQEPSALTTLLQEERVTIMQATPTLWQALVTDYPEKL
QGLNILVGGEALPAHLANKLKELGCSLTNLYGPTETTIWSTVMNIDERESGIPPIGKPIW
NTDVYVLDAGLQPVPPGVIGELYIAGEGLASGYLGKPELTAERFVANPYGKPGQRMYRTG
DLVKWRSDGVLEYMNRADHQIKIRGFRIELAEIEMVLQRHENIKQAVVMVREDRPNDKRI
IAYIVAEEKETIHLSEIRSYVSESLANYMVPSAFVWLEELPLTPNGKVDRKKLPAPDFNG
MNNERVARNPKEEILCDLFAEVLGVSRISIDDNFFEMGGHSLLASRLMARIRETLSVELG
IGKLFESPTVAELVKQLDRAKTARPAIKKVSRPNEVPLSFAQRRLWFLHCLEGPSPTYNI
PLVIRLSGKLNEGALQGAFYDVVEKHETLRTIFPNVLGSSYQEILHMENLNLEMIITNTC
KNELESVLAEAVRYSFNLDVEPAVRLQLFTVNENEHVLLILLHHIVGDGWSLQPLTRDFT
AAYKARCQGNKVQLETLPVQYADYALWQQQLLGDETTQESLISTQLDFWKKELKGLPDQL
ELPTDYQRPMETSYRGETIHFHIDAGMHSRLVELARKNGVSLFMVLQAGLSALFTRLGAG
TDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQANLAAYENQDV
PFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEAIFDVPDIETSLEIQSVGSAKFDLTFEI
SESHGVDGTPNGLHGLLEFSTDLYKHETVQKLIERFILLLDDAATNPDQSIGRLEILTLA
EKNTVLEKWNGGFQIAPEMTLPQLFEKQVHINPNAIAVVFENKKLTYEELNRKANKIARF
LIAKGIGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPADRISFMLHDAKPSCV
LTNSEVEIECNEALKVLVDNVKVIEEIEKHSEDNIDEMERVKPLTPSHIAYVIYTSGSTG
RPKGVMIPHQNVVRLLGATDHWFQFDGNDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVP
HTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENKEIGQQLSLRYVVFGGEALEL
SRLEDWYSRHPHNAPKLINMYGITETTVHVSYIELDESTVSLRANSLIGCSIPDLKVYVL
DHYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQ
DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHPTVEQVAVIVREDQPGDKRLVSYIVAS
NNEAIDMNEMRQFASGSLPDYMVPYAFVVVNEFPLTPNGKLDRKALPAPEFIISSSSRGP
RTPQEEMLCDLFTEVLSVPQIGIDDGFFDLGGHSLLAVQLMSRIKEALGIELNIGTLFAA
PTVAGLAERLEVGNGQSALDVLLPLRASGNQLPLFCVHPAGGLSWCYAGLMKSLGTDYPI
YGVQARGIAKNEELPRSLEEMAADYLKHVREVQPHGPYRLLGWSLGGNVVHAMAAQLQNE
GEEVELLVMLDSYPGHFLPNTEAPTEEEALIALLALGGYDPDNMDGKPLTMESAVEILRT
DGSALASLEEETILNLKETYVNSVGLLGRYVPKVYNGDILFFRSTVIPDWFDPISPNTWL
NYLDGKIMQHDIDCRHKDLCQPGPLTEIGQVLAKYLQNKKGVRRV

Enzyme Prediction     

No EC number prediction in MGYG000002283_01241.

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.
cd17652	A_NRPS_CmdD_like	0.0	1533	2027	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).
PRK05691	PRK05691	0.0	1	2107	670	2772	peptide synthase; Validated
cd12117	A_NRPS_Srf_like	0.0	1523	2026	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.
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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	262	2376	812	2929
ACX49739.1	1.47e-262	11	1767	12	1816
BAY90071.1	1.74e-251	972	2377	2138	3553
BAZ00088.1	1.91e-251	972	2377	2147	3562
BAZ75991.1	1.91e-251	972	2377	2147	3562

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	2.86e-278	465	2107	211	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	1.50e-263	465	2036	211	1722	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	1.52e-212	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	1.48e-176	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	2138	6	2112	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P45745	0.0	1	2377	1	2374	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P39846	0.0	9	2110	11	2076	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB 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	2108	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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002283_01241.