CAZyme Information: MGYG000003072_00394

Basic Information

• Species: Paenibacillus amylolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus
• CAZyme ID: MGYG000003072_00394
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit D

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1235		137234.58	4.7707

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003072	7042795	MAG	China	Asia

• Gene Location: Start: 390797; End: 394504 Strand: +

Full Sequence      

MIENQPSSSHSMESSLPVLQIPLDFGRRQQSFSYQSAQITLHASLSRELKQKYGEQMVYP
VLLSAYAALLFRLSAEQELAIGILSPDQAASYLSLQIQGKLTFSQLCHQVSEQLKIEYTL
QNGGYPESFFMLNSVQLPQAPQILNWNVRDDQNMLILDLFYDSSLLKESTVLRYAEYYQT
LLLALVRDGEKAIGTVDILSASDRLLYREMNDTSVLEPENQTVHGWFEATAAAYPDLPAI
TSPSKSYTYRELNERANQVARVLLSNGLQKGEFVSIFMDRSLETIISLLGILKAGGAYVP
IDPEHPQERNSYIVEDTASSFVLTTEASYAQASSLFSSIATVRQILSVDGRLAGFAASNP
NLDIQPDDLAYIIYTSGSTGKPKGALIAHRGVINLGSVVQRDCDIQPGDVLTQFATYSFD
ASVWDTIGALFYGAELYLLSAEERVSVEEFASAIERTGTTIITILPTIFFNQLASYLSDE
GFHKLAKVRIITVAGEALYGEQVRAFQRKFGNQIDIVNVYGPTECTVATTTHRISEQVPE
HVVNIPIGKPIHNYKVYIVNEEQQLCPAGVPGEVYIATPALAKGYLNQPERTAQAFIENP
FAIGEKIYKSGDIAKLLDTGLLEYVGRSDSQLKIRGHRIEIGEIEDHFARLDQIQNVAVI
PKKESDGQNMLVGYFTSKDGSTLSVSDIKAELTEKLPSYFVPKWICQLDEMPIAPTGKIN
RKAMVSLPHVERHEDRPDRVMPETETESIILDAWKEILQHDDFGVEDSFFNIGGDSLRVI
HVLVILKPHYPQLNIADFFAEKTVRALARRVEVLSLSAVEVTDSVVTDGMITQLSEHPVE
LTPQLGYPLIREPEHVLLTGATGYLGSHVLQQLILNSSTRIYTLVRRPSNGITAMERLTN
VLEGYFGKQLTDQLSSRVEIIEGDLEQPHLGLSAEQRAYVQDRIDRVIHCAADVRHFGDA
DQFAKTNVEGTVALLDLIRSKPGASFHHVSTMGIPEDLALSGQWESSLQYDRFPADLHVD
NLYSDSKLEAEKVLMIAAEQGVPVSIYRAGNLTCHSETGRFQSNIDSNAFYRMIKAMLLL
GKAPAADWMVDFTPINYASEAIVHLALRQDTAGRVFHICNPEPIRYDELIRSVNRAGYEV
ETLPFADYTRWLFDASISKEPEALQLAIAQLEGDGAKDSAYVYACPVTTAYVEPAGISCA
KTDDRFISVMLDYAVQIGYFPSAIRRHNGTSTAME

Enzyme Prediction     

No EC number prediction in MGYG000003072_00394.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05930	A_NRPS	1.57e-171	235	724	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	2.05e-156	227	724	3	486	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.
cd12117	A_NRPS_Srf_like	2.63e-153	226	723	2	482	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
PRK12467	PRK12467	1.20e-142	17	808	1317	2160	peptide synthase; Provisional
TIGR01733	AA-adenyl-dom	3.11e-141	248	659	1	409	amino acid adenylation domain. This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAY90071.1	1.24e-109	17	809	327	1175
BAY30132.1	8.05e-107	17	809	328	1178
BAZ00088.1	2.03e-105	17	809	328	1176
BAZ75991.1	2.03e-105	17	809	328	1176
AFZ04852.1	3.42e-103	17	808	333	1180

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSQ_A	8.75e-107	118	780	358	1007	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFZ_A	7.86e-105	144	808	1146	1794	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
4D4G_A	2.20e-104	221	765	30	572	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]
1AMU_A	2.29e-104	210	758	28	555	PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis]
6P1J_A	9.85e-102	12	724	203	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70LM4	1.11e-142	12	1218	3836	5075	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
O30408	1.10e-123	15	811	2284	3110	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1
P39846	1.20e-123	15	811	1243	2076	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P09095	5.10e-122	219	808	25	595	Tyrocidine synthase 1 OS=Brevibacillus parabrevis OX=54914 GN=tycA PE=1 SV=2
O68006	1.60e-115	19	807	1871	2683	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 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
1.000004	0.000029	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003072_00394.