CAZyme Information: MGYG000002817_05106

Basic Information

• Species: Paenibacillus_B sp900539405
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
• CAZyme ID: MGYG000002817_05106
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1486		171164.9	5.6961

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

• Gene Location: Start: 10018; End: 14478 Strand: -

Full Sequence      

MNVAEVQLNPLTDAQRRIWNTELLYPNTALCLLAGTIKIKGKIDIHILEKSVNLVIQNND
ALRIRLIQHNNEINQYVEKYTYQKFQFLDFSESQDMNHIYDTLHGYNKTSMELLNSNLFQ
FIIFKANNNEYGYTIKIHHIISDGVSIEMMLRQIHENYSLLVQSKVDSNRRMPSYIDYIY
AEHDYKSSERYQIDRNYWLSEFQTIPDNYELKPYNPIITSTIGNRKNLVIKGALYQRLQQ
FCQQNRINMLAFFQAIIFIYLYKATNNHDIVIGTNYSNRTTKKEKDTMGMFTSTVALRLH
VDPQEEIISFIQRLFMKNSKNLRHQKYPYNELIKELRKIHNINHLHRLFGIAVEYRTFNF
IELNRMETEYEYQFCGDEANDLVVHIIEKLKESNITIHFDYRTFVFDDRQMDKLINHFLK
IADYMLEHSREKVGSVFLISEEELTQINDVFNNTKAEYPKDKTIHELFEEQAERVPDQIA
VVYEGKTLSYKELNQRSNRLARRLRAEGVAVDQRIGIMVERSLEMIVGILGILKAGGAYV
PIDTEYPADRICYMLDDSGANLLLTQSHLQGRIAFEGTILCLDESCSYDEDGSNLEPAAG
SNDLAYVIYTSGTTGKPKGVMVEHRGLCNLKVMFEETLQITEKDRIVQFASLSFDAACWE
IYKALLLGATLYIPTAATIRDYSLFEAFMDKHKITASIMPPNYVNYLNPEHMPSLTKLIT
GGSASSVELVEAWKDHVKYFNAYGPTEASIVTALWSSTEEGTGLKSVPIGRPIQNHQIYI
LDGNGDAAPIGMVGELCIGGVGLARGYLNRPELTAEKFVSNRFAPGERMYRTGDLGRWLP
DGNIEYLGRLDDQVKIRGYRIEIGEVESALLSVGDVKEATVVAHQDEKGEKTLCAYFVAN
QSYSVSEIKGVLSEKLPQFMIPSYFVQLEQMPITANGKIDRKALPVPDGKLQTGTEYVAP
RNTMEATLTEIWQEVLGLKQIGVKDNFFDLGGNSLKAMNLVANLSKGINVNTMLRDVFSY
PTIEQMAFFILEKEQELYIPIPVAAKRDYYPLSSAQKRMYILSQMEGNDVAYNIPFILEI
EGPLKREKVNSALKQLIERHESLRTSFEILNGEPMQRVHDNVNFDVTTIELEREDVENYL
REFIRPFQLTQAPLLRVSLLQLGKEHYIMMIDMHHIISDAVTIDIFLNEFFKLYEGEQLP
ELRIQYKDYVYWHLEQQHRGNLKKQEGYWLNVFEGEIPVLDMPADFERPLKLSYEGALHN
FNIDEEVYKGLKKIVEQTGSTLYMVLLAAYTILLSKYTGQKDIIVGTPIAGRNHADLKGI
VGFFVNTLVIRSYPLGEKTFLEYVYEVKDTMLNAYENQDYPFEQLVEKVNFKKAANRNPL
FDTMFAVQNLDQLEFKRKDLDVKPLALEHRVAKFDLTLFFNVGQTNLSGSFEYCTKLFKR
NTIKLISNHLMDILSTVVGKSNIKLSEIKLNDHEDVNSIELFELNL

Enzyme Prediction     

No EC number prediction in MGYG000002817_05106.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	466	948	1	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.
cd05930	A_NRPS	0.0	476	944	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.
PRK05691	PRK05691	0.0	10	1470	677	2164	peptide synthase; Validated
cd12117	A_NRPS_Srf_like	0.0	466	944	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	468	945	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	8.14e-217	263	1470	812	2049
ACX49739.1	5.46e-169	10	1483	11	1524
BAY30132.1	5.84e-157	11	1032	2249	3296
BAZ00088.1	4.69e-156	11	1032	2247	3294
BAZ75991.1	4.69e-156	11	1032	2247	3294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFW_A	2.85e-214	455	1443	198	1173	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	1.54e-213	455	1443	198	1173	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFY_A	7.92e-209	455	1443	198	1173	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]
6MFZ_A	4.51e-208	455	1443	198	1173	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
5U89_A	1.10e-203	441	1470	4	1061	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	11	1485	8	1487	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P0C063	0.0	3	1485	1056	2532	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
P0C064	0.0	3	1485	1056	2532	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P27206	0.0	5	1478	2	1489	Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
Q9R9J0	0.0	10	1482	3893	5361	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 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
1.000034	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002817_05106.