CAZyme Information: MGYG000002465_02029

Basic Information

• Species: Yersinia massiliensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia massiliensis
• CAZyme ID: MGYG000002465_02029
• CAZy Family: GT2
• CAZyme Description: Dimodular nonribosomal peptide synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2422	MGYG000002465_11|CGC1	266041.24	5.0145

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002465	4872451	Isolate	Finland	Europe

• Gene Location: Start: 42230; End: 49498 Strand: -

Full Sequence      

MSEDSTPIFADAAIVELPLVAAQPGIWFADQLSQQKTLYTVAHYIELAGSLDRMLFSRAV
SQGLSEADTLHARFFHGVDGPMQRIPLQCKATDIPKLVWLDLSSRADGRQAALALMQDDI
DADLLADGDEPLYRHWVIRVPDEQGKPVWLWYQRYHHLVIDGFSFTAITRRIADIYTALQ
QGKPIGESPFTPFSDVVSEYLAYAGSETEQRDKQFWLQHTADLPAAISLSAINSPIRAEQ
AASRVLRQRIDIDSALFSCLTQQGAEQRLTAADMAMALLMSYFARMSGERRLSVGCPFMR
RLGSAALSATGPVVNVLPLQVNLQPEMNLLDVARAVASELKRVRKYQRYEADQLRRDLGM
VGSQRSLYGPVLNFKLFDFALNLGEITGITHTLASGPVDDLEIDLYLENGELTLEILANA
ERYDHASLQAHGERISYLLQQLATQAAIPIGNLILTPTQELQSIDSWAKGPQFSLPAGVV
SVLDIFQQQVSAQPDAIAVRCGDQSLTYHQLSARVAQLGRALIARGIGAEDVIAIGLPRT
VDSLVAILGVLSSGAAYMPLDLDYPMDRLALMCEDATPRILLAHQSTESVLSPLNAMGEM
PIVCLDDVHFQRECAAYAIQPISNIERRQPMLGDHLAYMIYTSGSTGRPKGVMSTHGGLV
NLLVAHRTYLYGPAMAAFKQQNTRRMRAGHTASFSFDSSWEPLFWMMMGCEMVIFDEEMR
RDAYALVQLMDQAPIDTMDITPSFFTQMIDSGLLELGRHRPAFIMIGGEAATPRLWDLLK
QHPELNVVNFYGPSEYTIDTLGANTTVSPQPVVGRPVANTEVYLLDSQLAKVPVGSVGEL
YIAGQGLARGYLNRPDLTAARFVANPFRHGEVMYRSGDLMRWTAQGQLDFVGRIDHQIKV
RGFRVELGEVENALVALPEVSSAVVIAQAIGATHRLIGYCSVPDAQLRDSEDLNARLMRQ
LAATLPDYMVPALLMVLDEMPLTVNGKIDRQALPSPQHRQQSSRLEPSAYLEQLTPQETL
LCTNIASLLRLDCIGAEDDFFQLGGDSILAMALGSALRRAGYRLTPREIFALRTPARMAQ
ALQPLIEKGTEPTLAMPTAHILPEKLWQAASEKYGPIADILPVLPLQQGLLFHAQLGQEA
NNYNAISRFDLQGELNIERLRDALESLLQRYPQLGAIFDSELHPESLQILPQIHGNARRW
PWRQHDLSALTPHQQMAETQRLEREGLARDLMSDTAGTLQPLLVATLIRYSSERHSLVII
AHHLVGDGWSSAILLHDLLHLYGNSEKSGNSETYDKSAKLPPLSVSYGDLIRRMTARDLR
QDRSVWQQALQGATPTILYPESNAAGPVSEWVIELDSKLESALTALQRREGITLNTLLQG
VWATLLGVLSGRDDVVFGSPVSGRFSEIEGIEQHVGLFSNTLPVRVKLQPQLPLLTQLAA
LQQQQIQLLEHDGLGLGEIQRLAGANTLFDTLLVVENYPENNQLHQQSFNGLRCDALNNR
GYTHYPLTLLVLPGERLHLQLEYRDAVTDPQQIAQRLVMLLEHLVWQPELPLSALDLLTH
DEKNLIASANDTAIALPKLTLCDLMNQQAQSTPQAVALLDIDETLTYQQVNQRVNALAAI
LRQQGVQSGDRVAVALPRSVNLSLALMAILAAGAAYLPLDTGYPADRLAYMIGDAKPRLI
ITVSSLAERFIGQAPLLQLDQQDLLVTATLLEVVIAPESPAYLIYTSGSTGRPKGVVISH
GAIVNRLLWMQNEYPLGGDDVVLQKTPCSFDVSVWEFFWPMITGARLVMAPPEAHRDPDA
LRTLIEDYGVTTAHFVPSMLAAFVSAMTAQDKPCQSLRRVFCSGEALSRELSVLYQDIFS
APLHNLYGPTEAAVDVTYQPAYGDALAQVAGNSVPIGKPVWNTQLRILDSMLRQVPVGVA
GDLYLCGVQLAQGYYDRPDLTASRFVADPYDHGQRMYLTGDIARWLPDGAVEYLGRSDFQ
LKIRGQRIELGEIESALLALPQVQQAVVHARTLVGVEGALAGADSRQLVGYIVPTNGAEN
SDMELLRQQLSEQLPAHMVPAVIVSLNAFPLSANGKLDRKALPAPVNQAGHGGRAPHAGL
ESVIAGLFANLLGVESVNADDDFFALGGHSLLAMRLAADLRRELQQPVAVGQVMVASTVA
TLAAALSQPSSEMSAGKAGFSEVLPLRSGHGHPLFCLHPASGFAWQFSLLPRYLPGNWPV
LGIQSPRPDGAIATCQDMDSLCDHHLATLRQVQPQGPYHLMGYSLGGTVAQAMAVKLRAQ
GEEVAFLGLLDTYPPETQDWNAPIEAEALEEVERERALFMAAAGDEQEEKREMFAQIQAN
YDDAVGLLSGAKTPVYEGETTLFVATQTLPDGESPEEIWRPYAKQLQTYSLDCSHITMMS
PETLKVLGPILQRVFKGIRSLS

Enzyme Prediction     

No EC number prediction in MGYG000002465_02029.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17646	A_NRPS_AB3403-like	0.0	1583	2082	2	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.
cd05930	A_NRPS	0.0	1593	2082	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.
PRK12316	PRK12316	0.0	1127	2171	56	1098	peptide synthase; Provisional
PRK10252	entF	0.0	10	1082	1	1045	enterobactin non-ribosomal peptide synthetase EntF.
PRK05691	PRK05691	0.0	473	2142	5	1681	peptide synthase; Validated

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	7.15e-268	4	2291	537	2784
ACX49739.1	4.89e-181	14	1849	7	1846
BAY30132.1	3.15e-158	1002	2295	2131	3419
BAY90071.1	2.24e-157	1015	2295	2132	3408
BAZ00088.1	8.72e-156	1002	2295	2129	3417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JA1_A	1.59e-314	1115	2412	1	1290	EntF,a Terminal Nonribosomal Peptide Synthetase Module Bound to the MbtH-Like Protein YbdZ [Escherichia coli K-12],5JA2_A EntF, a Terminal Nonribosomal Peptide Synthetase Module Bound to the non-Native MbtH-Like Protein PA2412 [Escherichia coli K-12],5T3D_A Crystal structure of holo-EntF a nonribosomal peptide synthetase in the thioester-forming conformation [Escherichia coli K-12]
6MFZ_A	6.44e-213	452	2142	177	1774	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	1.40e-203	452	2085	177	1715	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]
6P1J_A	5.78e-160	1118	2082	3	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]
2VSQ_A	6.25e-140	1117	2293	9	1149	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0E7C4	0.0	18	2422	20	2834	Vanchrobactin synthase VabF OS=Vibrio anguillarum OX=55601 GN=vabF PE=3 SV=1
P45745	0.0	11	2411	3	2369	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q8XBV9	1.60e-313	1121	2412	5	1288	Enterobactin synthase component F OS=Escherichia coli O157:H7 OX=83334 GN=entF PE=3 SV=1
P11454	4.41e-313	1121	2412	5	1288	Enterobactin synthase component F OS=Escherichia coli (strain K12) OX=83333 GN=entF PE=1 SV=3
P29698	1.04e-296	1121	2412	5	1276	Enterobactin synthase component F OS=Shigella flexneri OX=623 GN=entF PE=3 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
1.000048	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002465_02029.