CAZyme Information: MGYG000001083_00117

Basic Information

• Species: CAG-873 sp900755985
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900755985
• CAZyme ID: MGYG000001083_00117
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2420		266902.03	4.9733

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001083	2200570	MAG	Sweden	Europe

• Gene Location: Start: 590; End: 7852 Strand: +

Full Sequence      

MRTSKLNQSQLGIYLDSAFREDTAYVLAFVLGLKVGIEAKQLKRALEMSIACHPALKSAI
ISDANGEVRMEWDDNGLPDIPVKTMSEAEFNEYKAKMVRHIDIPGPQTCYFEIIQSGNSV
WLAMQLHHIAFDGSSMTAFMHTLNTALEGDIPRAETLSCFDFAEREAAARTGAEYESQRD
YYVRTFGDYDADGASIYADAKGEPGLSRKVYTLNTSLSAFKGGAAVANAAMGITLGAFTG
RDDVLFTTAYHGRKTSEMANTVGMFVRTLPVRCHIGRDVTVADLISEMKQQRGDTRAKDL
MSFGDFVRMTGYKQEVLFGYQGHILNYEPLSNVLSCQRIDKGETGLPLTFEMYLTDTGIE
IDAAWRSDMYSESAIDRFTETFDHVLAQLLNPANQQSPVTGFSLMDEVSEERLMHIESVP
ALDFDRTVPIEGVVARVAREIPEKTAVVTDDSSYTYAEIDRLSTVMARQLEARGVCPGMT
VGVMIPRSEWMVLIPLAVMKTGAAYMPLDPTFPEERLAFMTEDASVSIIVTVGSLADKVL
PSFGGKILDAAELANEDSPRTDRWAANPGSPFVVLYTSGSTGKPKGVTLTRANILNYCHD
YIKIVALGTEDRVPAYANFGFDAHMMDIYPTLMSGATLYILGEEIRHDLDAMHDFFVKNE
ISAAFLTTQIAWQMITLYEFPSLRWLSCGGEKLPPTGKQPFRFANVYGPTECTVIATYYL
PQGDTDGSVIGRPIPGYELRVLDRHGRRVPQGVPGELVILGVGVGVGYLNRPELTAEKFI
TIDGERAYRTGDLVRWNEDGDLRFIGRMDGMVKMRGLRIELGEIEAVATRHEAVRLFVAA
VKTVGGNEQLIGYYAVKEGRDVEPDQLREFMSADLTEFMIPTALIKLDKLPMTPNGKVDR
KALPVPDIGVAEEMIPAATDDEKEMSKIVAGVLGHESFGVTTNLLKVGLTSLLAMRLVAT
IAKQRNVRLTSKAAMADPTVRGLIKALEAESREARGKSQELRGKRKYYPITENQRGVLID
WERYREALQYNIARAIKIKSDTDIDRLKKAIQKTVKAHPALDTRFVNRNGDIMQQRLDHV
KVNIGEIVLDHEPSREDMQSLMRPFDLFNEPLYRFVIVHHGDDAWLFMDFHHIVFDGMSA
MVFFESLSKAYAGQELPVEEYSAFEWADDEAAMLRSAEYEEAETWFEKLLNDTETTVYSH
SSVAEPVVPGTLLRVSCEMEAADVDKFCKDNAVTPSNFFLSSFIQTLHRITRNETVAITT
VNNGRSDVRLVDDIGFFVKTLPVVSRMSPKQAAVTSPANMTHDLQEQFNTTRGVDFYPFT
EIVRKFGLRPEIMYVYEGGVSLDAADGPLADENIAVALDTAKVPLTLLIFTPAPGKYRLE
LEYDASLYSNADMSLLLDMVCTAAAGNTSAATVKDAVLLSTAQEIKLKDVRDGESGEVEY
SSYHGAFELQADAKPDATALIACDRTLTFAEFDAEANRIANALRAKGVDRGDKVVVLLPR
DSRLITAIYGVMKAGAAYIPCDPEYPVERIRLITEDSDARCIITTSDKLASYPGKAVDID
SLLQCADTARPGVEVHPDDPAYLIYTSGSTGRPKGVVIHHGAVTNYLYGYRKLIYEPMGA
DEPKVNMLIVTISFDASHVDLGTSLTSGHTLVIADEEECKDVTLLAELMKRTGVEAFDAT
PSRLAAMLELPEFCEAIAECKLLNIGGEAIPASLLSKLDAAGFKGLTINEYGPTETTVGS
NHAVLQSDKAVTVGPPFYNYREYICDAWGGELPMGATGELVIAGRSVGKGYHNLPEKTAE
SFIIFKGEKAYRTGDLARWLPDGDVDVLGRIDHQVKLRGLRIELGEIESVANAFPGVKMS
VANVCKIQNVDHLCIWYEGPNVNQDELRAHLSRHLTDYMVPDSFNPVDKIPVTPNGKLDR
KHLPEPVLEKLAEYVEPAPGDESTIAEAFRRTLSLERVGADDDFFKIGGTSINAIKVVAV
LAQSGLKISYKDLFATKTPRLLAAHIANHDKTPAPVAPSAPVSESVEEFGEILRKNSIEA
FNKGERQAIGNVLLTGATGFLGVHILHWLLDTTDAKITCVVRGSAHFDASSRVRTLLFYY
FGDTYEHLWNKRIFIITGDLTEASTLAALDAEVINTVINCAASVKHFAPGNEIEHANVDT
VRNIVEWCSAHRRRLVHISTVSVAGDAEAATAARLTLTEQSLDLGQGLSNQYVKSKYDAE
KIILRAISDGKLEAKIMRVGNISPRNSDGEFQANFQSNAFMGQLRAYLALGCVPYSHLDS
SCEFSPVDQLSCSILRLATTPQANIVMHPLNNHHVPMADVIDVMNELLPRKIECVEPEVF
AERLNRAMNSASEKVTLLQPLIAYQSADGNTAYIGCSPKFTNEILFRLGFRWSPTSTGYI
RNFIKAIAGLGYFDDAMNPE

Enzyme Prediction     

No EC number prediction in MGYG000001083_00117.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	36	2003	1589	3619	peptide synthase; Provisional
PRK05691	PRK05691	0.0	122	2014	803	2782	peptide synthase; Validated
PRK12467	PRK12467	0.0	122	2021	177	2182	peptide synthase; Provisional
cd05930	A_NRPS	4.16e-152	1455	1923	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.
cd05930	A_NRPS	5.69e-152	442	903	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	1.56e-199	121	2016	686	2672
ACX49739.1	4.40e-135	6	1717	12	1846
BAY30132.1	1.82e-87	34	969	2280	3276
BAY90071.1	1.78e-85	34	969	2269	3265
BAZ00088.1	2.66e-84	37	963	2279	3268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.00e-205	442	2008	219	1799	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	1.12e-193	442	1926	219	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]
6MFW_A	1.60e-109	442	1400	219	1177	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	5.19e-109	442	1400	219	1177	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
5U89_A	2.03e-98	438	1151	34	768	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
O68006	8.43e-238	9	2011	1677	3734	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
O30408	4.52e-225	13	1998	1073	3102	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1
P0C064	1.37e-224	15	2010	1074	3126	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O68007	4.02e-224	23	2011	96	2134	Bacitracin synthase 2 OS=Bacillus licheniformis OX=1402 GN=bacB PE=3 SV=1
O30409	1.98e-222	6	2006	3133	5190	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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001083_00117.