CAZyme Information: MGYG000002762_01835

Basic Information

• Species: CAG-485 sp900554845
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900554845
• CAZyme ID: MGYG000002762_01835
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2415		265352.86	4.7289

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002762	3275168	MAG	Netherlands	Europe

• Gene Location: Start: 686; End: 7933 Strand: +

Full Sequence      

MRQSPLSQSQLGIYLGSAYREDLAYHIAYAFKFPADTDVSRLEAALKKVMACHPALNVAI
VTDENGEAMMEWDGETLPEIPVKSMTDAEFEDLKRHLIKHIDVPGEGMCRFEIVRAESAV
WLTMLVHHIIYDGSSMRVFLRDLDIAMKGGDPEKETFTCFDFAERELASRSGAEFEAQKE
YYSKTFGDFDSDGAAIYPDAKGEFGFSHKVFRLTTPVSEFKGGSAVANAAMGIALGAFTG
RDDVMFTTVFHGRNTHDTDNTIAMIVRTLPVRCHLGKDVTGAELIGEMRRQRDDTRAKDL
FSFSDFAAMTGYEQNVLFGYQGRLLNMDSLCEGMTLERLDAGDTGVPVAIQMYVSDQGID
VDVIWRSDIYSEVALDRLVATLDLALSQLCDPSNASRPVSEFSIVGEAAENELKQLENCP
ALDFDRSVPLEGVIAAVAREVPEKLALVTDDKSYTYGELDRISTVMAQNLVAQGVEKGMV
VGVMIPRSEWMALIPLAVMKAGAAYMPLDPTFPEERLTFMTDDASVKVILTVDGLADKVL
PSYGGRIIDAASLAEGEAKPVTEWPAAPASPFVVLYTSGSTGKPKGVTLTRGNILNYSHD
YVNIVQLGLEDRVPAYANFGFDAHMMDLYPTLMSGATLYILNEELRHDLDAMHDYFVKNE
ITVVFLTTQIAWQMITLYEFPSLRWLACGGEKLPPVGKLPFRFANLYGPTECTVIATYFM
PQGETDGSVIGRPIPGYGLRVLDKHGRRVPRGVPGELVILGAGVGVGYLNRPELTAEKFV
TIEGERAYRTGDLVRWNEDGDIQFMGRMDGMVKLRGLRIELGEIEAVATRHPSVRQFAAA
VKSVGGNDQLVGYYSVKDGSDVSPQELRDFMSEDLTEFMIPAAVMKLDKLPMNQNGKIDR
KALPVPEIEVSEEIVAPETDDEKEMSEIVAGVLGHESFGVTTNLLKVGLTSLLAMRLVAT
IAKRRDVRITSKEAMADPTVRGLIRALTNADRGSAPAKTAAKRKYYPITENQRGVLIDWE
RNRDALQYNVAQAIKIKSGTDLNRLKEALATAVKAHPALGARFVNRNGDIMQQRLEQDMV
RVEELELDHEPAREDMQALVRPFDLFNDPLYRFVIVRHGKDAWLFMDFHHIVFDGVSAMV
FFDSLAKAFSGQDVPEEEYSAFEWADDEAALLRSAEYEEAEEWFEKLLGDTETTVYSHSS
VAEAVPQGTLLRVSKEVDASDIDKFCSVNAVTPSNFFLSAFMQTLHRLTRNETVAITTVN
NGRNDVRLVDDIGMFVKTLPVVSRKSAANAGKTSPVEMALQLQQQFNTTRGFDFYPFTEI
VRKFGLRPEIMYVYEGGVSLDAAEGPLSEEKIPVSLDTAKVPLTLLIFTPAPGKYRLELE
YDASLYSNADMAVLLDMLGSAVTKNPSSKVVKDATLLSPAQNALLEAVRDGESGEVEYTS
YHGAFERQADKRPDAMALVACDRSLTFAELDENANRIANALRRAGVDRGDKVVVLLPRDS
RLITAIYGVMKSGAAYIPCDPEYPVERIKLITEDSDAKFIITTAGKLESFPGKAIDVDTL
LECPETSRPNVEMQPDDPAYLIYTSGSTGRPKGVVIHHGAATNYLYGYRKLIYSPMGENE
PKVNMLIVTISFDASHVDLGTSLTSGHTLVLANEEECKDVAMLADLMKRTGVEAFDATPS
RLAAMLELPEFRDAISTCKLLNIGGEAIPGSLLPKLDAAGFKGLTVNEYGPTETTVGSNH
AVLQSGKPVTVGPPFYNYREYICDAWGGELPIGGIGELVIAGRSVGKGYHNLPEKTAESF
ITFNGAPAYRTGDLARWLPDGDVDVLGRIDHQVKLRGLRIELGEIESVANAFPGVKMSVA
NVCKIQNVDHLCIWYEGQGVDQEELRTHLTRHLTDYMVPDSFNPVDKIPVTPNGKLDRKH
LPEPVLEKLAEYVEPAPGTESAIAEAFRRTLGLERVGANDDFFKIGGTSINAIKVVAVLS
SEGIKISYKDLFATKTPRVLAAHLNNTADIPAPEAEAESAAATEEFADILRANSVKAFND
GERQSVGNVFLTGATGFLGVHILHDLLINTGATVTCVVRSSKYFDASSRLRTLLFYYFGE
TFEELWNSRIFVVEGDLTEKATLASLDAGTIDTVINCAASVKHFAPGNEIERANVDTVRN
LVEWCSAHNRRLVHVSTVSVAGEADVKVASERVLNEQTLDLGQSLANQYVKSKYDAEKII
LGAVRDAGLNAKIMRVGNISPRESDGEFQANFQSNAFMGQLRAYLALGCIPYEHLDAPCE
FSPVDQLAHSILELATTPAPNVVFHPLNNHHVPMADVIGVMNRILPKAIECVEPDVFQER
LNGMMAGESEKVTLLQPLVAYQSADGKTTFVGCSTGFTNGMLFRLGFRWSPTSTDYIRNF
ISAIAGLGYFDPAVE

Enzyme Prediction     

No EC number prediction in MGYG000002762_01835.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	24	2002	71	2161	peptide synthase; Provisional
PRK12316	PRK12316	0.0	5	2001	1558	3619	peptide synthase; Provisional
PRK05691	PRK05691	0.0	24	2002	697	2773	peptide synthase; Validated
cd05930	A_NRPS	1.79e-160	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.
cd05930	A_NRPS	8.70e-147	1453	1921	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	5.49e-202	4	1977	564	2634
ACX49739.1	6.83e-129	5	1715	11	1846
BAY30132.1	7.66e-82	25	969	2269	3276
BAY90071.1	1.72e-81	25	969	2258	3265
BAZ00088.1	5.74e-80	25	963	2267	3268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	9.14e-198	442	1979	219	1772	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	4.75e-186	442	1924	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]
6MFX_A	3.86e-103	442	1398	219	1177	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	6.94e-103	442	1398	219	1177	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5U89_A	4.63e-99	438	1430	34	1076	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
P0C064	1.28e-230	5	2007	1063	3125	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O68006	1.17e-229	5	1993	1673	3718	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C063	8.61e-227	5	2007	1063	3126	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O30408	1.86e-224	25	1996	1085	3102	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1
O68007	4.97e-221	5	2004	77	2129	Bacitracin synthase 2 OS=Bacillus licheniformis OX=1402 GN=bacB 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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002762_01835.