CAZyme Information: MGYG000001712_00907

Basic Information

• Species: Bacillus_A thuringiensis_S
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A thuringiensis_S
• CAZyme ID: MGYG000001712_00907
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit D

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2054		233731.82	6.45

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001712	5736823	Isolate	United States	North America

• Gene Location: Start: 893791; End: 899955 Strand: +

Full Sequence      

MNTNLKLSNRPEHTVQKLFEQQVIQNPDSVALVYKDQQLTYKELNEKVNQLAFYLQKRNI
GPESMVGVYIERSLEMIVSILGIIKAGGAYVPLDPAYPTKRLEYILKDANIQVLLTQNHP
TQWIPKEIDCINIKEHEMNISREKNINPTIEVKPDNLAYVIYTSGSTGKPKGVLIEQKSL
CNFIISSINLTKMNSDSRNIQFASLSFDASVFEIFTSLVSGGTLYVCSQHDIMPVEPLTQ
FLQKNKITHALLPPTVLNLLDESVFKDLQVVISAGSACSEQVAKRWMQNHLFINAYGPTE
TTVYTVAGIYKGDGAPPIGRSIPNVEVYVLNEAKKLVPIGTVGELYIGGIALARGYLNQP
ELTKASFIPHPFKNSSNDRLYRTGDLVKYLPDGNIEYIGRADKQVKIRGFRIELGEIETI
LGNHPDIKEVTVVAQEDSFGDNILVAYIVGEGDTQEWRKHVGVHLPNYMVPAHFIKIESL
PLTVNGKVDKDALPAWASIIQTNEGYIAPRNRVEQKMVEIWSEVLGIDSSAIGINDNFFE
LGGHSLLATKITSRLGVDFSILVQIRDIFEYPTIKHFSKRLTFLLGKTGEIDVFTPLQSV
KREQYEPLSFAQQRLWIMDKIVTNSALYNVPIAWRLKGKWNIEMLKKGYNAIIHRHEILR
TVFHEVDGKPVQIVQQDITVPLSVIDLRYLSPEDKTSKIENISKIEAKKPFDLSQGPLLR
THLIIMDNKELVLLCTIHHIIFDRWSLDTFINEWMSFYQAFLENETEKLPPLPVQYIDFT
KWQKSWLTEDIIQKQIAYWGKELRGLLPILELPLDYPRPIIQSYNGDTYQIVIPNKLLEK
IKVFNSKEGVTLFATLLASYQGFLSRYTNQKDILVGSPIANRNYPGVEDLIGFFANTVVY
RADCSNNITFKELVQQIKKKMLDAQENQDVPFEKVIEAIQPERDMSYSPLFQTMFVFHNQ
LKELPKLLDHSVEKIPRHMNGAKFDITIAMEEIPTGLQVDFEYNTDLFKVSTIKRMAQSF
EIWLDEILQFPEEPIENLRILTKNEEKQLLHEWTNIEGNYQKDVVIQELFEQQVIQNPDS
VALVYKDQQLTYKELNEKVNQLAFYLQKRNIGPESMVGVYIERSLEMIVSILGIIKAGGA
YVPLDPAYPTKRLEYILKDANIQVLLTQSHLTQWIPKEIDCIDIKEHEMNISREKNINPT
IEVKPDNLAYVIYTSGSTGNPKGVLYEQKGLCNFINASINFTKLNTGSKVVQFSSIAFDV
SLYDIFATLVSGGTLYVCGQQDIMPVEPLTQFLLEKKITHAFLPPTVLNLLDESKFEELQ
TVISAGSVCSEQVAKRWVKNHLFINAYGPTEASVATIDIYSGKGTPPIGRSIPNVEVYVL
NEAKKLVPIGTVGELYIGGIALARGYLNQPELTKASFIPHPFKNSSNDRLYRTGDLVKYL
PDGNIEYIGRADKQVKIRGFRIELGEIETILGNHPDIKEVTVVAQEDSFGDNILVAYIVG
EGDTQEWRKHVGVHLPNYMVPAHFIKIESLPLTVNGKVDKDALPAWASIIQTNEGYIAPR
NRVEQKMVEIWSEVLGIDSSVIGINDNFFDLGGHSLKIMSTLVKTFSEGWNVTIKDYFEL
KTINNIAKKIQYGYKVNSHSDTLDIKLTTPPKKLKKTKRHEFSNNSKILLTGATGFLGIH
LLEQLLDTTECKIYCLVRGENKQEANNRLLHMLKFYFKNKFVSYQSLVNQRIFIVQGDLA
KQNMGLENELYKELHQQISTVIHAAALTKHFGEYSEFERANVQAVKELLAFVGDTKDLHH
ISTTGVAGQFVLNETETIFKESDFYVKQNYKDNVYVKSKFLAEYEIFKAILTGTDATIYR
VGNLTNRYIDGQHQYNFTENAFMSKLKFILQYGIVTDVLLSSEVEFTPVDYCSKIITGFV
TSNEIHENSKNCVNHIYNHLTLNLNVLVKLLNSMGYPIKVISETEYQQFILELSKDKKKQ
EDIQNLMTFEEPKDNCYKPINLDSTETQKTLKLLGIQWPIINIEYIQQIINYMTSVTGSN
SVAKLFKQSYTLKN

Enzyme Prediction     

No EC number prediction in MGYG000001712_00907.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	18	495	2	488	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	27	493	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.
cd05930	A_NRPS	0.0	1078	1543	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.
cd17655	A_NRPS_Bac	0.0	1068	1545	1	488	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.
PRK12316	PRK12316	0.0	579	1627	20	1081	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	15	1631	1011	2663
BAY90071.1	6.71e-255	417	1627	2018	3280
BAY30132.1	6.57e-254	487	1631	2128	3295
BAZ00088.1	8.85e-254	478	1631	2109	3293
BAZ75991.1	8.85e-254	478	1631	2109	3293

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	3.20e-311	12	1627	204	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	2.58e-292	12	1544	204	1713	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]
5U89_A	1.93e-207	11	1050	22	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6P1J_A	9.54e-196	607	1543	7	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]
6MFW_A	2.35e-177	12	1021	204	1181	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70LM5	0.0	15	1630	5644	7270	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
P39847	0.0	4	1636	454	2079	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P45745	0.0	14	1647	459	2120	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q70LM4	0.0	19	1977	3050	5014	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P27206	0.0	7	1630	455	2081	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
1.000042	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001712_00907.