CAZyme Information: MGYG000001453_00487

Basic Information

• Species: Aneurinibacillus aneurinilyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus
• CAZyme ID: MGYG000001453_00487
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1525	MGYG000001453_31|CGC1	175011.8	5.4929

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001453	5302959	Isolate	not provided	not provided

• Gene Location: Start: 29340; End: 33917 Strand: -

Full Sequence      

MNSEVNYPLSHPQKRIWYTEILNSGTSLCHLGMLVKIHNQVDYLLLNQAINIVISESDSL
RMRLKQQGDQEPLQYIAEHQEREFDVLDFSSENDSGAFENWIDQKIQEPFNLFESDLFYF
SLIKVSDDENAVFCNVHHIISDGLSMNLMGNRIIDHYLHLLKGKETHKNFGNSYIQFLNN
EESYLNSDRFEKDENFWLEEFETTPAITGIKSYHPYLTSTKSLRETFVVPNELKCKIEEF
SQSYGISLNSIFVAALMLAFQRWTSTDDVVVGVVYGNRTMKVEKDIMGMMVNLVPLRMNI
EHEEEALAFFKRVAKKQMKVLRHQKYPFNLLSEKIKKTNKSFDRFFGITIDYRPLNLMDQ
VDYELHWMPNGHEASDFAIHIEHRLDSGDLALLVDYREKLFALQDITDFVNCMLVLLENI
SNDPMQKIKNINILSEKEKEKILVTFNETNVDFSLNKTIHQLFEEQVIRHPEEIAVVYEE
QRLTYRELHERSNQLAHYLQQQGVGPESLVGLCVERSLEMMVGILGILKAGGAYVPLDPT
YPEQRLHYIVEDARIQVLVTQERLQGQQWLPETIQTICLDRDHEKMAQESVMSPVTGVTA
KNLAYVIYTSGSTGNPKGVMVEHHHVTRLFKATEHWYQFDEKDTWTLFHSYAFDFSVWEM
WGALLYGGRLVVVPYWISRSPKDFYHLLVKEKVTVLNQTPSAFRQLIQVCEQEEGEDRRF
VLRYVIFGGEALKPASLLPWFERYGDKQPQLINMYGITETTVHVTYYPLTREDALLSSGS
TIGKRIPDLQVYLLDANRQPVPIGVAGEMYIGGEGVARGYLHRPELTAERFISYPLGDQS
KRLYRTGDVARYLPNGDLEYLGRIDHQVKIRGYRIELGEIESTLHTHPLVKEATVIVRED
EPGDKRLVAYVVGEGSAAEWRGHLQARLPGYMVPAHFVAIEAFPLTANGKVDHKALPAPT
PQKTEEGYTAPRNECEQALVSIWKQVLGVKQVGIHDNFFEAGGDSILSIQIVSRANQAGW
KFTPKQLFEHQTIAELAQVAEEAQDIQAEQGVVTGDVLLTPIQEWFFEQGQPHPHHWNQS
MLLRTRERMEVERLEEALQAMVIHHDALRLRYDLLPNGRWKQRNEGIEEQTILTVIKLDE
TPQEEWHHVIQREMDTAQASLHLQQGPLMRAVYFDEGENGSGRFFWTIHHQAVDGVSWRI
LLEDLQTVYSQAKEGQKIHLPAKSTSFKEWSERLYAYSQSGISQEVEEYWRKQSEIEVST
LPKDYAVEEAREASAEQVTVVLGEKETHALLQEIAVTHRAHMNEVLLAALVQATADWTGH
PVLSVDVEGHGREEILEGVDLSRTVGWFTSIYPVHLDMKGAKTPVEALKAVKEQIRQIPN
KGVDYGILRYLHPGIGSIFQSQPKPSISFNYLGQFDQTFSQEAMFTQETGFARVDHAPES
KLSHLIEVVGIVTDGKLQLTWIYSREQFAIATIQEVAENMLRKLDLLIHSSATEAAFTVS
DFALANLTENEMNKILSKMTKKRGK

Enzyme Prediction     

No EC number prediction in MGYG000001453_00487.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10252	entF	0.0	8	1054	9	1059	enterobactin non-ribosomal peptide synthetase EntF.
cd17644	A_NRPS_ApnA-like	0.0	458	957	1	465	similar to adenylation domain of anabaenopeptin synthetase (ApnA). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. 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.
cd17643	A_NRPS_Cytc1-like	0.0	471	956	1	450	similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. 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	8	1513	1730	3245	peptide synthase; Validated
PRK12316	PRK12316	0.0	7	1491	1557	3024	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAY90071.1	1.04e-222	183	1038	304	1175
BAZ00088.1	1.64e-215	225	1038	349	1176
BAY30132.1	1.64e-215	225	1038	349	1178
BAZ75991.1	1.64e-215	225	1038	349	1176
AFY93865.1	9.30e-180	431	1017	305	905

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6N8E_A	2.45e-155	8	1011	31	1042	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]
6P1J_A	4.31e-150	7	956	6	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]
6MFZ_A	3.83e-148	1	1037	780	1794	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	1.31e-141	436	1484	4	1045	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
4D4G_A	1.99e-130	457	995	30	573	Understandingbi-specificity of A-domains [Planktothrix agardhii],4D4H_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D4I_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D56_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D57_A Understanding bi-specificity of A-domains [Planktothrix agardhii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70LM5	3.00e-318	8	1513	1075	2596	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
Q70LM6	8.78e-315	1	1524	3627	5154	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
Q70LM4	3.99e-287	8	1514	1058	2570	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P39846	1.72e-274	7	1521	1056	2559	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P27206	6.62e-253	7	1516	2101	3584	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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001453_00487.