CAZyme Information: MGYG000002817_03042

Basic Information

• Species: Paenibacillus_B sp900539405
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
• CAZyme ID: MGYG000002817_03042
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2248	MGYG000002817_15|CGC2	249418.37	5.3558

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

• Gene Location: Start: 116554; End: 123300 Strand: +

Full Sequence      

MSAIPFTTEQLTGYDAHTFEIPSAIVDGLEQLTRTRSVTLEAAVGVAWSGLVARYHNAEE
VVLHAMASRSRDGVLVAVRPEETLWSAAEALCGQLQTGGEDSGASGDITTCCWCQDAEVP
GKTRAEISAGDLHARILGREAAFLGPFLFTIYYRPERFSLDAATRMGQQLNQMLREAAQA
PDKPIGEWNLLTKEEIRRYIERHNRTQYPYPKDRTVPSLFEEQAARTPDEPAIIEEGRQF
TYKELNETANRLAHYLRAQGVALEQAVGILAERTAEMVIGILAIIKAGGAYVPIDPDHPQ
DRIQYLLEDSGARLVLTSAGLSGRLPADAVQVPLEATAWADQPGHNPEPAGSAEDLIYII
YTSGSTGRPKGVMVTHRNVVRLVKNTNYVSFQPGDRMLQTGSLVFDASTFEIWGSLLNGI
GLVLVDKTTILDSRQLDEALRRFGVTTMFLTTALFLQLVDRNPAIFKPVRQLFVGGELMS
PKHFYRAAQECAPIRLSNIYGPTENTTFSTCYELKEEREGPIPIGTPIGNSTIYVVNAHG
KLQPPGATGELWVGGDGVARGYLNRDDLTEKMFIDSPFVPGERIYKTGDLVRLCEDGQLE
FVGRKDHQVKIRGYRMELGEIEARIHSHSQVKETLVADFEEAPGQKALCAYVVAEGGLDA
AGLRAYLAQQLPEYMVPGYFMFLERMPLTINGKIDRAKLPRPERQERAAIHYAAPTNGTE
RKLAAIWEELLGIEPIGIDDHFFELGGHSLKVAQLQARIYETFQVNISFKLLFEMPYIRS
LASLIAQLEQGGFEAIESAPDKPHYRLAPAQQRMYALQQRADIGMAYHVPLLYRLPGDCE
PERLERALRKLVERHEALRTSFHWEDGEVVQRVHPAVDFAMQRLEADGRTAQEAAASFLR
PFRMEEAPLLRAAWIRFAEGEAALLLDVHHIVFDGTSLSLLTEELAALYAGRELPAQTLH
YKDYAAWQAERELREQEAGEAYWLRMLEGELPVLELPTDFPRPPMQTFAGDIVRAALPAA
DAAALKKLASERGTTLYMALLAVYNLLLAAYADKEDIIVGCAVAARTHPDLERMMGMFVN
TLPIRSYPEGGKSFADYLAELKESLLAAYEYQTYPLDKLVDRLSYPRDMSRNPLFDTVFV
MQNMGNTTLELGGAACEAIPYHNGTSKFDVTLEAVEREDAVLLNFEYNTALFRRDTIERL
AGHFLQLVQEAVRKPEALIGELDMITARERERIVAEFNRTQADYPREATIHGLFEEQARR
TPDCTAVTDPQRSLTYAELNAEANRLAHELRRRGVRREQAVGVLTERTAEMIVGVLAIMK
AGGAYVPIDPDYPADRVDYLLEDSGAKLVLASGSLAGQLPPHIARVGFEAAAHGPSDEEG
AAIDPDSVNEAEDLAYLMYTSGSTGKPKGVMVTHRNVIRLVQNTNFVSFREDDCILQTGS
LVFDASTFEIWGALLNGLRLVLVDKMTILDETALAEAIQRHGVTMMWLTSPLFTQLAEKN
PELFRPVRTLLVGGDVLSPKHIYRVREASAPITIINGYGPTENTTFTACYEIAGERPGSI
PIGKPIANSTAYVVNAFGKLQPIGVPGELWAGGDGVARGYLNRSGLTAEKFIDSPFRPGE
RIYKTGDLVRWLPDGNIEFLGRKDHQVKIRGFRMELGEIEAQIRTHPQVKDVLVSVREEA
PGQKALCAHIVAEGALTAADVRAYVLTGLPDYMAPSYYAFLERMPLTTNGKIDRSKLPEP
EKLEGASGSMVAPENEIEQKLADAWQEVLGLAQVGVEDNFFDIGGHSLKAITLVARLKQE
FIVDVADIFAYPTVRQLACRIEYRPNHLQEKLARIRERYAAAPNGEAPAVAEARRRYRSG
IEGRIPSEAERRTEYRHVLLTGATGYLGAYLLHEIISRTGSEISVIVRGRTPDEARGRLA
DKLAYYFGPDWFPAHAARIHPVNGELSAERFGLETGDYERLAREVDCIVHAAANVKHYGH
YDDFVRSNVTATERLIDLALERTPKAFHHVSTMSVGMGTIDGRAEALFTEDDGDLGQQHH
NVYVKTKFEAELRIQEARARGLQASIYRVGNIVCHSDTGHFQENIADNAFYNTLKSYLGL
GAVLASEPDTDLSFVNQVSAAIVTLFDKPALYNGTYHVYNPHLISLADLLAAHPGTTVKP
LAAGPFFEELYARFEREENREAVESVLLHNGWMDEASNGTIFVHTAERTAALLARLGFAW
TKPAAAEFRRLLAHAEAVGFLPQASSRK

Enzyme Prediction     

No EC number prediction in MGYG000002817_03042.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05930	A_NRPS	0.0	1262	1737	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	150	1007	1510	2390	peptide synthase; Provisional
PRK12467	PRK12467	0.0	153	1818	452	2160	peptide synthase; Provisional
cd05930	A_NRPS	0.0	228	699	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.
cd12117	A_NRPS_Srf_like	0.0	219	699	2	483	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	166	1822	961	2663
BAY30132.1	3.44e-192	715	1818	2144	3291
BAZ00088.1	3.55e-191	715	1818	2142	3289
BAZ75991.1	3.55e-191	715	1818	2142	3289
BAY90071.1	6.67e-189	715	1818	2133	3280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	0.0	211	1755	202	1724	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	211	1818	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]
6MFW_A	1.24e-197	211	1229	202	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	1.20e-196	211	1229	202	1205	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
5U89_A	5.30e-192	193	1235	4	1072	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
P39847	0.0	151	1818	401	2070	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	151	1822	402	2077	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	153	1821	1432	3104	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	149	2213	2979	5049	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P39846	0.0	147	1821	404	2076	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB 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
1.000075	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002817_03042.