CAZyme Information: MGYG000002490_03142

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_03142
• CAZy Family: GT2
• CAZyme Description: Dimodular nonribosomal peptide synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
609	MGYG000002490_29|CGC2	68099.93	4.9045

Genome Property

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

• Gene Location: Start: 81849; End: 83678 Strand: +

Full Sequence      

MLFGKTEHMRNGLINKTIYSLFEEMARRVPHYTAITCKDETMSYAELSNKVNSLAAGLRI
EKVRKQDIVALTMGRSIDVIAGMLAILKVGAAYLPIDPEYPERRKNDMLTDSRASFLLTH
SGLEAAGEHVKVLYIDELYTANPEYNENECVEPAADDLAYIIYTSGSTGQAKGVMIEHKS
VVNFFNGMAEVIDFSEGKKILALTTISFDIFVLEALLPLTRGLTVVMADEEMQKNPRLLA
DFIRHHDIDMLQATPSMMRLLASCDNEPFECLRGLKEIMIGGEAFPQSLLDPMRRKTSAK
IYNLYGPTETTIWSTVSDATAKNDIDIGKPILNTQVYIMDESNYPVPAGEEGELCIGGSG
LARGYAHRPELTAERFVPNPFVPGERMYKTGDRVKLLPDGNLQYLGRIDNQVKIRGHRIE
VEEVEGALMEHPYIQQAAVASWEDQENNKYLCAYVIAEHELHPGALREFLSHSLPDYMIP
SYFIRLDHMPYTLNGKIDRKALPFPEKIQLANEGHVPDRAGEDADILSKIKAIIRANAEI
GLPLEEIGPHSHLSDLGIHSITFIKMIVAIETVFDFEFPSEDIDAAQYVTVQDVVAYVES
KASKATIHN

Enzyme Prediction     

No EC number prediction in MGYG000002490_03142.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05930	A_NRPS	0.0	30	502	1	444	The adenylation domain of nonribosomal peptide synthetases (NRPS). 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	21	502	2	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.
cd17655	A_NRPS_Bac	0.0	21	506	2	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.
cd12116	A_NRPS_Ta1_like	0.0	30	502	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.
cd17646	A_NRPS_AB3403-like	1.27e-174	21	502	3	488	Peptide Synthetase. 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
AFZ04852.1	1.41e-117	15	507	583	1079
QND46664.1	1.49e-100	18	595	2075	2650
BAZ00088.1	3.66e-98	15	594	578	1174
BAZ75991.1	3.66e-98	15	594	578	1174
BAY90071.1	4.67e-94	15	589	2696	3276

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U89_A	7.21e-124	21	604	29	608	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
1AMU_A	3.30e-123	5	506	32	527	PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis]
5ES6_A	2.37e-108	14	503	201	679	Crystalstructure of the first two domains of the initiation module of LgrA [Brevibacillus parabrevis],5ES7_A Crystal structure of the F-A domains of the LgrA initiation module soaked with FON, AMPcPP, and valine. [Brevibacillus parabrevis]
5ES5_A	5.75e-108	14	567	201	736	Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis]
6ULZ_A	5.33e-107	14	503	203	681	Adenylationdomain of the initiation module of LgrA mutant P483M [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45745	1.08e-124	17	554	459	999	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
O68006	2.32e-120	16	583	2125	2674	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
Q9R9I9	6.01e-119	16	599	261	842	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
P0C061	2.48e-118	5	599	32	609	Gramicidin S synthase 1 OS=Aneurinibacillus migulanus OX=47500 GN=grsA PE=1 SV=1
P0C062	2.48e-118	5	599	32	609	Gramicidin S synthase 1 OS=Brevibacillus brevis OX=1393 GN=grsA 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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002490_03142.