CAZyme Information: MGYG000000977_01073

Basic Information

• Species: Clostridium sp900539375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900539375
• CAZyme ID: MGYG000000977_01073
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2101	MGYG000000977_9|CGC1	244451.37	5.1707

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000977	2927434	MAG	Australia	Oceania

• Gene Location: Start: 53341; End: 59646 Strand: -

Full Sequence      

MSLEEIEKFKEYYNKNSNLEIYDNLTINELFNESVLRNPDNIALVKGNEKLTYKDMDILS
DKVSLYLREKYNIKENENIAIIGGNSFERFINLFAVLKLGCTYVPIEYKAPISRIEGIIK
KAECKVVLSEKSFKNINDRLIDDNIIEKENICSLSKEEIQNLKYGKEKINIDGNRNCYII
FTSGSTGEPKGVKIRDKSVINFSKYVIDKYEIKEEDSVLALSSFAFDASVLDTFPILFVG
GTIHIIEDDIRMDINNINKYLESKKITLMFMTTSMYELFDGLDNNSLRIVFTGGEKLNKV
SKNNYKLINIYGPTETTVACTMYEVLDKEYENIPIGTSVDNMKILIIDEEGNLNPLKEPG
ELCVEGIGLSIGYLDNEKETKKRFVPSILDKNRIMYKTGDIAKWNENYEIEFVGRKDEQI
KHRGFRIELNEIKKMVMEYKEIKDVAIIYNDEVENKYIACFYCSDKEINNKDIKEFLLKN
IPEYMIPNKFIKVNKIPLNNNFKVDKKSLLALIKDKKEKIDIDKKDNNIEEVLKEMWSKM
LSINLEDISIDDNFIEGGGHSILAIKLIKDINEKYNINLSMIDFLKEPNIKNLEEIINKQ
IKNYKKDDENIVFKHNEKERFKPFELNDLQQAYLLGRKSEFELGNLATHCYTEFECDDYD
HERFKEVIRKVFYNHDMLRCRFSDDGYQYIDENYKLKDIEYNDISNFSKEEQKAFLNKVK
EEMTTKIIDYTKENLVQLRVTKIGEKKAIIHFYYDGLVVDGWSQEILFSQTDKLYSNKDY
KLPDEKVLFRDYINYLKELKKGNEYEKCKKYWQNRIKDLPPIPDLPTKQNNNSSNKLPEV
RKFSRALSIEDYNKLEKISQKNGITVFITLLTVFGKTIARYCNKQRFLINVPEFNRYDVE
EGVNNLVGECSSFLLFEIDNRGNKSFLESARDNEKTLWELHENKLFSGADVLKEIAKVSG
SIENNYVPIVFTSLMDVCNEYSLKKFKKKYVQTHTSQIWIDSVVMQCNNEVQFNWDCVLD
IFEGELLDSMLDTFIITLKELINNEESWTRKNELYIKEEYKKVIEEANNTKHSIKYEKFV
DLLENSRMVNEKKTAISTINKSYTYEELFNTVKGIANLLSECGIKKNDNVSILMDKKMEQ
IASILGVIYCGATYIPITTDASKERLKHCISETESKLLIVDNNTSKLFNIDDIKCKIINI
DNYKFDKDYSFFKPIGADLEDNMVIIYTSGSTGMPKGVMVTQRGLINCIKYTNETFNVNK
EDKILSLTNYSHDMSVYDILGILSAGGEIVLPEAERVKDPEHWLELIEKHGVTLWNTVPA
MMEMMLEIMDMKNEGDISSIRVTIFGGDVLKPAMVKKLRERIKNAKIMNVGGPSETTIWN
INHEVTIEDEGKTRIPYGKPIWNTKYFILNENLEICPKGVIGTMFVEGDGVSKGYINNKE
KTSQVFITNPYTGNVMYNTGDLGLYLQDGSIDFIGRKDFQVKINGKRIELGEIEYYADLF
EGIESAIAKISSEDKKVINLYYKSTIEIDNNTLRKFLEKKIPDYMIPKNYMRIEEIPLTL
NGKINKDKLPEIKNKVNVKYDEEKLTSIQKDILEIYKEIINIDSAEINDNFFTLGGDSLK
AIKLLRKVSQKYKVSLNLTDIFKCPSIYKLSILIEKNLNETDNYIKKTNKNTAPLSISQE
GIWFINKGIDENEDQRYNIISTFEINNNVNLDLLKKSIELVIENNIPLKTVIREKDYKPY
QTIDFNGKYEVKIEKKYDYLPNKEIRKIVEAQEAKTHFDISTFPLFNIRILESCEDKNLL
VINIHHIIADAYSINIILEKIQEYYKLLKGNENIEKNKDDINYIDYLIWQNEELEKGKYD
DELNYWKDKLKGNLNIIDLSEKNITFGSFKGNVRKVNIDEDVIKRFKEICKDNGMTLFAG
FTTVLYMFINYLTYESDISIGCGVSGRGRSEIEKTIGNFAGALLLRCNIDENKGFSSIAK
DVKKTVDEAYRYQSLPYEKVIKEINLDRQYFTLPYKILIDYIENEDKGKDGIFSSFNYSK
LIAPADFCLFIQSNNGVHNLSFTYKEELFSDYEMAEFELLFKNIINEIVKNPEKKFVCYD
L

Enzyme Prediction     

No EC number prediction in MGYG000000977_01073.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	5.15e-171	27	1830	514	2332	peptide synthase; Provisional
PRK12316	PRK12316	4.72e-167	27	1872	2005	3831	peptide synthase; Provisional
PRK12467	PRK12467	8.07e-145	675	2094	100	1543	peptide synthase; Provisional
cd05930	A_NRPS	8.34e-135	1093	1569	3	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	1.83e-132	39	509	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	1.24e-150	27	1656	1011	2664
BAZ00088.1	6.74e-86	774	1678	282	1207
BAZ75991.1	6.74e-86	774	1678	282	1207
AFZ04852.1	5.09e-84	774	1651	287	1180
BAY90071.1	2.26e-78	3	2094	555	2666

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	2.07e-184	26	1651	206	1794	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	1.69e-174	26	1571	206	1714	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]
7LY7_A	8.16e-164	623	1656	10	1018	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	8.38e-164	623	1656	10	1018	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
6LTA_A	6.21e-113	623	1654	56	1098	ChainA, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTB_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTC_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_B Chain B, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O68006	8.34e-296	24	2005	36	2001	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064	1.45e-221	26	2101	1507	3564	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	6.24e-217	26	2101	1507	3565	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q04747	5.68e-207	4	2094	445	2510	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
O30409	3.94e-204	27	2089	1502	3539	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC 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
1.000041	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000977_01073.