CAZyme Information: MGYG000001436_04995

Basic Information

• Species: Paenibacillus_F sp000411255
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_F; Paenibacillus_F sp000411255
• CAZyme ID: MGYG000001436_04995
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2189		242842.22	4.7631

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001436	6290841	Isolate	not provided	not provided

• Gene Location: Start: 2252005; End: 2258574 Strand: +

Full Sequence      

MSQVKIKDIYPLSPMQEGMLYHSMLDRDSEAYFQQNIITVGEVLDRELVQKSLQLLIERY
DIFRTVFVYKETERPLQVVLQEREAPSVHTDDVSGLSEARKTAALEQFTGSDRTNGFDLE
KDVPLRLALFKWSETTCKLVWSFPHIVMDGWCLGIVANDFFSLYTSLRDGIRANLEPVYP
FSSFIQWLENQNREEAAAYWSKYLDGLENETTVPGFSRAEGNTPFRLEHHSLKLDAALTH
KMEQIAKRQQVTVSTVFQTAWGVLLQGYNNSTDVVFGTVVSGRPEEIKGIENMVGLFINT
IPLRISGEKSESFAALLSRVQSDWMESNAHSYLSLADIQAQSQLKHNLIRHLVVFENYPI
SEELIGTGDETGEGGRTDGESAKNSLRITEVDGFEQTNYELTLTVIPGRELEIKFSFNAE
IVGHAGIRAIAGHLHQVLEQITETPDIPLDSINLLTDEECGQLRAFNDTGASYPAEKTMH
GWFELQAAMTPEKIAVIFGEKRLTYRELNVRANRLARQLRLKGVEPDSVVGILCERSIEL
MVGLLAILKAGGAYLPIDPGHPQERIDYMLADSGAVLVLAQKDLLERAPAGAETVELDAE
NLLTGDGSNLSRGSGPEHLAYVIYTSGTTGNPKGVMIEHRALINRLHWMQKRYPLDEKDV
ILQKTPYSFDVSVWELFWWGAYGAKVVFLEPGAEKDPAQIARAIDKYNVTTMHFVPSMLS
VFLDHAESRLEPGALASLRYVFASGEALNPQQANRFNSLFYRTNGSRLINLYGPTEATID
VSYFDCSFGKSPLDRVPIGKPIDNIRLYITDNVGRLQPVGVAGELCIAGTGLARGYLNRP
ELTAEKFAAADFDPSGRIYKTGDLARWLPDGNIEYLGRLDHQVKIRGYRIELGEIEAALL
RHPMVKEALVMDRTDGQGQKVLCAYLVCGPDPAPETVLLRESLAAKLPGYMIPSYFVFLP
EMPLTSNGKVNRRALPAPDTVWDESGYIPPEGEMEEALAAIWKEVLGVEHLGAGDSFFDR
GGHSLKAALLVSKIHQRLQVDLPLRQVFESPTIRSMAEAIRKEAYSAHQAIEPAEPRDVY
PVTSAQKRLMVLDQLEQESTAYHIPHVLISRVPLDRRRLQTVFEKLIARHEPLRTSFEQI
ESDIVQRNHPEVVFEVEEISLSGAEETSLTELGGSGETKEKSGIEEIPAFSGLWEIVKTD
EEIAPENTGGNGASDHPENRTAVQDILTPAEKEALDRVIEGFIRPFNLAEAPLIRVGAAD
LTCGGTALLIDLHHIIADGVSMAVIANEFNRLYAGEELAPLKIQYKDYAVWQQKRSSSGV
LDAQEAYWMEKLSGELPVLNFPTDYMRPPLQSFEGDQFVFKLESSETEALKQTAARAGAT
LYMVLLASFNTLLHRYTGQEDIIVGSPVAGRTHADLQPLIGMFVNTLPMRSFPAGDKTFS
QLLEEVKQTALQGFQNQEIPLETILDKLSLKRDLSRNPLFDTMFIFQNLGIEEIGQPGEL
FQSYEFGHAVAKLDLTLQAEENETGGIDFHFEYAPGLFRKETVQRLAGHYLRILEAAVRN
PDMKLSAIDMLEERERHMLVESFNDTTAAFAYDKTIHRQFEEQVTLTPDAPALLFGDQVF
TYRQLNEKANSLARTLQSHGVGPDRLVGLLTERSPSMMIGLLAVLKAGGAYVPIDPDYPA
ARVAYMLEDSEARVLLTEGALAEGLQTAGAVISLDEEGVYSGETGNLEPASKPHHLAYVI
YTSGSTGNPKGVMLQHRSVSNFFTGMREKIEFVPGRKILALTTVSFDIFVLETLLPLTCG
MSVVLAETLHQTEPGALSGLISVHGIDTLQITPSRLQMLLGSPEGASSLKNVRNILVGGE
AMPTALLRSLQEFPDLNIFNMYGPTETTVWSAVQNLTNAASIDIGRPIANTQIYIVDAGG
KLQPAGVPGELCIAGEGLARGYWNRPDLTAEKFVPCTFGKGGGRMYKTGDLARWLPDGSL
EFLGRLDHQVKVRGYRIELGEIETALVHHEAVEEAVVLAREDVSGGHTLTGYLVVKTEIP
AAEIRTFLGQSLPDYMIPAAFAQLEKFPLTPNGKTDRKALLGLDAVQTSAADYVAPGDEI
EEQLAAMWAGILSATRVGVHDNFFELGGHSLKASLFVAQVREQWGIELELRQLFRQPTIA
EIAEHLRKELDEIRRLEEILREIEALEQV

Enzyme Prediction     

No EC number prediction in MGYG000001436_04995.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	11	2163	51	2160	peptide synthase; Provisional
cd05930	A_NRPS	0.0	1608	2080	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	491	975	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.
PRK12467	PRK12467	0.0	1081	2166	51	1097	peptide synthase; Provisional
PRK12467	PRK12467	0.0	1070	2163	2637	3669	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	6	2169	557	2665
BAY30132.1	3.49e-229	181	2168	300	3296
BAZ00088.1	1.66e-225	181	2168	300	3294
BAZ75991.1	1.66e-225	181	2168	300	3294
ACX49739.1	4.18e-205	11	1867	11	1844

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	0.0	474	2080	202	1712	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	0.0	474	2163	202	1794	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
2VSQ_A	1.79e-241	2	1061	5	1040	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.35e-203	1078	2080	4	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	5.56e-198	474	1575	202	1205	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
P39847	0.0	3	2168	4	2075	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	1	2166	1	2076	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	6	2171	7	2073	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	7	2166	5	2107	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q70LM4	0.0	5	2163	2577	4669	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD 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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001436_04995.