CAZyme Information: MGYG000004334_00774

Basic Information

• Species: Ruminococcus_E sp002493635
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp002493635
• CAZyme ID: MGYG000004334_00774
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2421	MGYG000004334_9|CGC1	272843.54	4.7919

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004334	2103818	MAG	Israel	Asia

• Gene Location: Start: 39902; End: 47167 Strand: +

Full Sequence      

MNKQNMNVLSKTEYGIYFDYMNNPSSIAYNIPFFLKLSKNVDIAQLKQAVKASIDNHSYI
KSRITVGDDSVIYKFMSDEPAQVEVKQLQDSEFDKKSLVHPFDLLGERLYRCCIFDLDSY
VMLFFDVHHIIFDGFSAEVFMNDIDRAYNGLPLESELITANDFSNEEAEILKTDELDRAK
EYYNSVFGDCELDSVMINDKNDGKPAAKALRYEFDSFNADEIRKYCRKIGIKTSAFFCGV
YGYLLARFSGADESLFATVYNGRNEKLVRTCGMFVKTLPVYCDFKKSKSVAEFLKELDKQ
LDCNRKYDLYSYADICSDLQISPSTIFAYQGDMFSNVNLCGEDIFVDIIDAPDAKSNVTA
EISRNHGKFSMKFEYRSDLYEESSIINFLKSFEKAVTDFIDKDNIDDIDITDDEQLKLLD
SFTNTEKDYEKTDIVTLFRRQAEQNPNNAAVVYLDKSYTYKEVDEISEKIGAYIKSLGIG
KEDVVSVLIPRCEYMVFASLGVSKSGAAYQPLDPSYPQERLEFMMSDADAKLLIAGKDLL
KLVPKYKGKVLFIEDISNLAECDKITANPNPKDKFIMLYTSGSTGTPKGCMLEHRNLVSF
CNWYKNYYNLTNASRVAAYASYGFDANMMDMYPALTTGACVYIIDESIRLDLLALDEYFD
KNGITHSFMTTQVGRQFALETKCKSLQHLSVGGEKLVPIKPQNDFCFYNVYGPTECTIFT
TAFPVHKNFDRVPIGKALDNTKLYVVDKYGRRVPPCVPGELWVAGHGVSRGYLNRPEQNE
KTYIKNPFTDAQGYERVYRTGDIVRFLPDGNIDFIGRNDGQVKIRGFRIELSEVERIIRE
FPEIKDATVAAFDEPGGGKFIAAYIVSDKQIDIDKLNDFIIANKPPYMVPAVTMQIDKIP
LNQNQKVNKRALPVPEKKTENIQMPENEVQQRIFDCISEVTGSNSFGINTDIFYAGVTSI
GAIKLNVLLSKEFDTVIKINDLKENSTILKLEKFLSNAQKSENFEILSDYPITQTQNGIF
VECAANPDSTIYNIPYLFKLSDKVDTDRLKTAVENTINAHPYLKTKLFINDNSDIRALRN
DEDAPMVDIVECAQLPDASQLVLPYKMLDSNLYRAKIFRTADSNYLFLDFHHIICDGTSE
AVIIEDINGFYEGKAVETESYTGFEAALDEEKSRKTDAYAKAKEYYDSIFSGCDSDFLPA
KDKNEPLPSVGRCEIESDLPIESVKEYCDKNSITLNAFFNGVFGLVLSKYNYKDEALYTT
IYNGRSDSRLSRSVTMLVKTLPVHCNTDGERKILDLLSEMKDRLMQSMSNDIYSFAEISR
AYDIKADIMFVYQGDSFEFDSIGGEIAENIPLTLNAAKAPISINVFIRNNKFVFVSDYRS
DMYSENVIQGISQCIGTAAEEFLNKTYLKEVSILSDKSKEILNSFNDTEVPIEQTTCNKL
FERQVAANPDKTAVIANKISLTYQQLNENANRIAHSLIDFGVKPDDMVGVMMPRTVYAYA
ARQGVLKAGGAFMPLDPKYPDDRISYILEDSKSKIIVTTTQTANERKALFEKCGVAVLTL
EEMLKSDKIDNPDITVSPSNLCYCIYTSGSTGKPKGVMIEHHSLVNFVDYNRINVQSCEF
CDNMSVSLALAALTFDVSVLEESLPLYHGTTIAMANEDEINNPILLAQMLVENKVDVMKC
TPSYMNNMLDVSQVVKSLKNMKAIDIGAEAFPAPLYDKMRKAGITAKIHNGYGPTEATIT
TSMDVVESNVITIGKPLCNTKVYILDKHRNILPPYVPGELTVLGECVGRGYVGKEELTKD
KFITFENLPAYRSGDLAFWGYDGKIHFMGRMDNQVKLRGLRVELDEIENVMNDYPAVLRS
VVLVKENPQAGQFLCGYFTASESVDKESLTKHMKRSLTHYMIPSVLIQLDSLPLTNNGKI
DKKALPEPEFTVEKKDYVAPKNDLQKKLCDMFAGALGTDKVGINENFFEIGGTSLSASKI
AMKAMTENLPVAYGDIFDNPTVEMLERHILNQNNKQTHTKENQPEIVIDEENKALRYNTA
QFVDEVIYTDIENVLLTGSTGFLGIHVLMQIIEHTDSAVYCLVRHSETVDVEQRLKRMLV
YYFSDSMDDLFGTRIFLIEGDITDKDTISSLEKYDFKTVINCAACVKHFTNDDTLERINV
KGVENLISFCVKTGKRLVQISTVSVAGININGKFPREKVLYENELFFGQDLSNKYIDTKF
RAEKAVLEAVANDNLDGKIIRVGNLMSRHSDGEFQINSVTNGFMRNLRAYAAIGKFPVSL
MDDIVEFSPIDVTAAAVMCLAGTNSKFTVYHACNGHKVEMGDVIAALNSCGIKIDVVKDS
EFNSALKDALKDDKKNMLVSGLISYLSSDSEKSEAYIGYNNSFTNKALYRLGFKWPITNE
TYLKNAFEALDTLGYFEGRFE

Enzyme Prediction     

No EC number prediction in MGYG000004334_00774.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	9	2005	52	2159	peptide synthase; Provisional
PRK12316	PRK12316	0.0	41	2007	1590	3620	peptide synthase; Provisional
PRK05691	PRK05691	1.68e-180	16	2007	685	2773	peptide synthase; Validated
cd05930	A_NRPS	3.55e-157	446	912	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	6.23e-156	1449	1925	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	1.07e-194	2	2003	556	2656
ACX49739.1	6.58e-106	9	1712	12	1840
AFZ04852.1	5.93e-95	1378	2012	523	1186
BAY30132.1	2.74e-88	8	995	2248	3294
BAY90071.1	1.20e-86	8	991	2237	3279

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	5.70e-242	426	2005	200	1793	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	1.83e-226	426	1932	200	1719	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	2.20e-132	426	1388	200	1173	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	5.43e-132	426	1388	200	1173	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	5.79e-108	426	1003	198	772	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
O68006	3.53e-269	28	2020	1693	3740	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064	1.82e-254	25	2009	1080	3122	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	3.56e-253	25	2009	1080	3123	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O30409	2.10e-249	25	2009	1074	3111	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
O68007	7.68e-245	25	2017	94	2137	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
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004334_00774.