CAZyme Information: MGYG000000392_00277

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_00277
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2425		272657.66	4.7284

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000392	2042501	MAG	Sweden	Europe

• Gene Location: Start: 296547; End: 303824 Strand: +

Full Sequence      

MIKNESNNKISLTKTEYGIFVESVNNPKSTAYNLPLFLTLDKNTDTEKLKSAIEAAFENH
KYLKTRLYLDNDGNVYKKISDEDLKIEVKEIADSDFNKADYIHPFDLQNENLYRITILKL
DSSVVLFCDIHHIIFDRYSLQVFLEDIDNAFNGVALVPEAYTANDVSQEESKRILTSELD
EAKAYYNSAFGGLEIDSIPIYDKKDETPSAKKLRHDFKTFDADKIREFSRSHGIKTSSFF
DAVFGFVLSKFSGADESLFTTVFNGRNEKLTRTCGMFVKTMPVSCNIQKTDEIEQYFKEI
NLQIENSRKYNLYSYADICSDLQISPQVLFAYQGDVLNKISFCGSETAVDFESSSDAKEI
ITCEIYRLNGNFYAELEYRADLYNEESMQILLSSFEKAINEFLTKSKLSEVNITDENQIS
LLESFNNTEKDYEKTDIVTLFRRQAEQNPDNTAVVYLDKSCTYKEVDEISEKIGAYISSL
GIGREDVVSVLIPRCEYMVLASLGVLKSGAAYQPLDPSYPQERLEFMMNDAGAKLLIASK
DLLKLVPNYKGKVLLIKDIQNLPDCSKISINPKPEDLFIMLYTSGSTGVPKGCMLEHRNI
VSFCNWYRNYYNLTTQSRVAAYASYGFDANMMDMYPALTTGATVYIIDEAIRLDLLAIDK
YFNENGITHSFMTTQVGRQFALEANCKSLQHLSVGGERLVPVNPQKDFSFYNAYGPTECT
IFTTAFSVHKNFDRVPIGKSLDNTKLYVVDKYGRRLPPCVPGELWVAGHGVSRGYLNRPE
QTEKSFIKNPFTDEKGYERVYRTGDIVRFIPDGNIDFVGRNDGQVKIRGFRIELSEVEKI
IREFNGIKDATVAEYDEPSGGKFIAAYVVSDEKIDIQKLNEFILENKPPYMVPAVTMQID
KIPLNQNQKVNKRALPVPQKQAEDIIPPQNEVQQKIFDCISEVVGSDNFGITTDIFYAGI
TSIGAIRLNVLLSKAFDAAIKINDLKENNTVIKLEKFLSESAKTKKYDILSDYPITQTQN
GIFVECAANPDSTIYNIPYLFKLSDKVDTDRLKKAVESTINAHPYIKTKLFINDNSDIRA
LRNDDEKPVVEIVECAELPDTSELVLPFTILNNKLYRAKIYKTNNANYLFLEFHHIICDG
TSEAVIIEDINSFYDGEAVETESYTGFEAALDEENARKTEAYTKAKEYYDSVFNGCDTEF
LPPKDKNEPLPSVGRCEIECDFPIENVKKYCDDNNITLNAFFNGVFGFVLSKYNYKDEAL
FTTIYNGRNDSRLSRAVTMLVKTFPVHCNINGESKITDLLLDTKNQLMESMSNDIYSFAE
ISRAYDIKADILFAYQGDSFEFERVGGEKAESITLGLDTAKAPLSIDVIIRNGKFVFLCE
YRADMYSESTIMGMADCLSVVSQEFLKKTYLKEVSMLSAQAEKEIESFNATDYPVSFVPV
HKLFETQAKQNGGNTAFIADGKKLTYSELNSEANRIAHSLIEKGLNVGEPVGIILPRTTD
VPIAEYGIMKAGGAFLPMLPDYPDERIDYCLRDSESRFVITTEEIRDERKGLFEDKPYTV
FTVNELLLNENAENPGLDIPVDSLAYIIYTSGSTGTPKGVMIEHRNLCNFVDANQLNYET
VNFVSYGNTALSVASISFDFSLMEIHIPLCNGMAVCMAGEEEIHNPLALFKLIKENHVDV
MSGTPSFISSFVDLPQAEEALKGIKMYDMGAEAFPPALYKKMRKASPEAVIVNGYGPTEA
TISCISKVMDGNGAVTIGKPAANVRAYICDTSGNIMPAGVKGELVICGDGVGRGYVNLLE
KTADVFINLNGRKAYRSGDLARYNQNGEIEFFGRLDNQVKLRGFRVELDEIESVINEYPH
ISRSIVLVKENPKSGQFLCGYFTASEKIDKDKLTEHMKRSLTYYMIPSVLIQLDTMPLTA
NGKINKKALPEPEFTAEKRKYIAPKNNLQEKLCKMFANALGAEKVGIDENFFEIGGTSLS
ASKIAMRALTENLPIAYGDIFDNPTVEMLEQHILKQQGKEVKAEEKENDVVLEGVDKALM
YNTAKYVDEVEYTDIGNVLLTGATGFLGVHVLYEIIKHTNSSVYCLVRKGRANSIENRLK
SMLVYYFSDAMDNLFGERIIPIEGDITDVEIIAGIDKYDFRTVINCAASVKHFSNDDSLE
RINVKGVENLISLCVKTDRRLVQVSTTSVAGVNVNRKFPPEKKIHENELYFGQDLSNKYI
DTKFRAEKAVLEAVANDNLDGKIIRVGNLMSRHSDGEFQVNANTNGFMRFLRAYAAIGKF
PVSSMDEAVEFSPIDYTAAAVMCLAGANSKFTVFQACNGHNVEMGDVVELLNRCGIKIEV
VKDKEFFESLNTALMDEKKNMLISGLISYASSDNDKTEEFIGYDNSFTTKALYRLGFKWP
IINEEYLANALNALATLGFFDGRFD

Enzyme Prediction     

No EC number prediction in MGYG000000392_00277.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	26	2009	66	2159	peptide synthase; Provisional
PRK05691	PRK05691	0.0	26	2009	692	2771	peptide synthase; Validated
PRK12316	PRK12316	0.0	82	2011	1643	3620	peptide synthase; Provisional
cd05930	A_NRPS	3.32e-162	449	915	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	2.98e-159	1454	1929	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	1.29e-204	131	2019	693	2668
ACX49739.1	8.33e-108	10	1715	10	1840
BAY30132.1	1.47e-99	921	2018	2137	3298
BAY90071.1	6.47e-98	921	2018	2126	3287
BAZ00088.1	1.27e-96	921	2018	2135	3296

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	9.77e-235	429	2017	200	1801	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	1.38e-218	429	1933	200	1716	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	1.10e-130	429	1394	200	1176	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	2.00e-130	429	1394	200	1176	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	9.92e-111	429	1002	198	768	Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0C064	2.21e-263	30	2013	1082	3122	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	2.91e-260	30	2013	1082	3123	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O68007	4.47e-250	12	2016	78	2132	Bacitracin synthase 2 OS=Bacillus licheniformis OX=1402 GN=bacB PE=3 SV=1
O30409	5.17e-250	31	2020	1077	3117	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
O68006	4.81e-249	31	2016	1693	3732	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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000392_00277.