CAZyme Information: MGYG000002356_00089

Basic Information

• Species: Bacillus_A wiedmannii
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A wiedmannii
• CAZyme ID: MGYG000002356_00089
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2021		231843.14	5.0138

Genome Property

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

• Gene Location: Start: 7028; End: 13093 Strand: -

Full Sequence      

MMIGILAILKAGGAYLPIDPTHPSDRIQYILENSGTSLLLTNGTLPKNLMFSGEIMPLAE
SAFSFSNRENLPVLNTSRDLAYVIYTSGTTGQPKGVMIEHRSLVNRLNWMQKNYSLGEKD
VILQKTPYTFDVSVWELLWWSIAGAQLVFLAPKEEREPDKILEAIERYGVTTMHFVPSML
HVFLDYLGVTGNGYKAASLKQVFTSGEALKSTHANTFHELVKGVKLVNLYGPTEATIDVT
YFNCPPEEISSIPIGKPIDNTKMYIVDSHLCMVPVGVMGELCISGDGVARGYLNNEPLTA
EKFVDHPYEPGTKLYRTGDLAKWLPDGNIEYLGRMDSQIKIRGFRIELGEVEKSLLTIEG
IEDGVVVVKENHDDKHLAAYYLGHAAYSVEELRNKLKAFLPEYMIPTYFVKLDHMPMNAN
GKIDRKALPEPNYDSLVSTRYEAPQNELQEKLVTIWSDVLKKETVGIHDNFFEIGGHSLK
ATVVTNKVYQVLQMDVSLRVFFDHPTIKELSDYLEGQAEHRYERIPVCAEQDVYETSSAQ
KRMYMVQQLEKGTVYNMPILFTIEGDIEPERLEGTFRKLVNRHESLRTYFADVDGEIVQK
IHPDFSFTMGRRDGSGWTVEALMRDFVRPFELNQAPLFRAELAESDEVAYIMVDMHHIIS
DGVSIERLLTEFNEIYNGEELEPLRIQYKDFAAWQNTFLKSEELKKQEAYWIQQFSDDIP
VLNLPYDYKRPVMQNFEGDERRFTFDEEQTEALRKIANETGSTMHMVLLSAFYILLSKYS
GQEDIVIGTPVAGRPHAELQNIIGMFVNTLALRNQAEGEKGYLEFLEEVKQNSLLAYDNQ
SYQFEELIDKLQVNRDTSRHPLFDVMFTMNHREEVGVRKSEGLQLKPMLQASNQSKFDLT
LHVTENHRTLKGSFEYSTSLFKRETIGRMVQHFIEIVANICRNKDARLSEIEMMTEAEKH
QVLHAFNDTKADYPREKTIVQLFEEQAARTPDLIAVKFENETLTYNELNQRSNQLARVLQ
KKGIKAESIVGLMVDKSLELVVGILGILKAGGAYLPIDPKFPEDRKEYMIKDSGLELLIT
SNEFNRTEKEAINIALEDEAIFSGPSGNLPLINKPEDLAYIIYTSGTTGNPKGVMVEHKN
VVRLMINDQIQFDFSEKDVWTMFHSSSFDFSVWEMYGALLYGGKLVIVSDLVAKETIKYL
SLLKDEKVTVLNQTPTAFYNLMKIELQYSSKDLCLRYIIFGGEALKPAMLDEWLKKYSET
KLINMYGITETTVHVTFKEIGIKEVRDGTSNIGKPIPTLTALVVDKHLTIQPIGVPGELC
VGGAGVTRGYLNREQLTKERFVQNPYINNEKMYRSGDLVKLLSNGEIEYLGRIDHQVKIR
GFRIELGEVENRLVSHERIKEAVVLAKEDEQYQKYLCAYIVCQKNLDKSELKAYLKERLP
EYMIPSYFMEMDMIPLTNNGKVNRNALPEPDATGLISSDYEAPQTVIQKDLVAVWKNVLG
VSSIGIHDNFFDLGGHSLKATAVISEIHKVLHIEVPLKEIFMNPTIKELSRFIETSAENP
YEKIEPCMESEFYETSSAQKRMYTFQQVEKKSTTYNMPGIFELEGEVHHDQLENAFKQLV
QRHEGLRTYFETVDGEILQKVQPFQQFHLDYKMIQETDVTEMTKRFIQPFELDKAPLFRV
EILENNSDKYLLIDMHHIISDGVSMSILIKELTKLYNGESLEPLRLQYKDFAYWQNGFLQ
SGDLDKQESYWKNQFQGEVPVLHLPYDYERPSKQSFIGETIYFELDEKTTAELRNVAKEQ
GVTLHMLLLSAFNILLSKYSGQEDIVVGVPVAGRPHADLQNIMGMFVNTLAMRNLPGKEK
VLREFIAEVKENSIQAYDNQSYQLEELIRAIHFKREQGRNPLFDVLFDMTNLDIHSDIQL
NGGTLKPRMFESEIAKFDLTLVGLEREQNIEMCFEYSSMLFKKETMDRAIRDLKKIIYSI
TTNLDITLSQISIRTKEERELILQEEKSLDEIKNQEFSFTF

Enzyme Prediction     

No EC number prediction in MGYG000002356_00089.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	1	1871	2066	3946	peptide synthase; Provisional
cd05930	A_NRPS	0.0	1	428	50	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	1	1871	1194	3102	peptide synthase; Validated
PRK12316	PRK12316	0.0	525	1564	4094	5150	peptide synthase; Provisional
cd17655	A_NRPS_Bac	0.0	981	1471	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	2.27e-295	16	2005	1	2061
BAY30132.1	5.28e-198	661	1551	273	1178
BAZ00088.1	2.48e-196	661	1551	273	1176
BAZ75991.1	2.48e-196	661	1551	273	1176
BAY90071.1	2.35e-192	442	1556	2131	3286

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	1	1561	268	1812	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	0.0	1	1473	268	1718	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]
6MFW_A	4.41e-201	970	1985	198	1192	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	6.12e-200	970	1985	198	1192	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
5U89_A	3.03e-186	956	2009	4	1077	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
P45745	0.0	1	1554	521	2108	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q04747	0.0	2	2004	529	2528	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	4	2005	529	2521	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	1	1966	526	2527	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P39847	0.0	1	1848	527	2381	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
0.867500	0.131308	0.000655	0.000201	0.000121	0.000240

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002356_00089.