CAZyme Information: MGYG000000258_00635

Basic Information

• Species: Ruminococcus_E bromii_B
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E bromii_B
• CAZyme ID: MGYG000000258_00635
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2443	MGYG000000258_1|CGC8	274725.38	5.027

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000258	2177930	Isolate	China	Asia

• Gene Location: Start: 668730; End: 676061 Strand: -

Full Sequence      

MSNLINLLDTYKGEKRELYPLTPSQMGVYLSCMHNPKGTMYNIPCTYVFDKGSLDTDRLI
NAVKKAVDNHPVMKIFIDNSTGSPMMKPRDSVEFDIPVVQVDNLEQAGKDFVKPFELEKD
VLFRFAIFECGDKSMFAMDFHHIISDGTSVSVICNDIALAYDGKELEPEKISQLNLSVFE
EKLEETEEYQKSKNYYDSIFSAVESKSEITEDFAENSEVEDKPNGSFELSTDGKFSVEDV
RNFALANQITPYTVFLGAYEYAVAKFTNQSETTVCTVTHGRFNKRLKNTVGMMVRTLPIH
ANIDEEDTVSDYLKKIRRSIKETVANDWFPFMKLASDYDLSADIMLAYQADIFNTFKIGG
QTLKLKLVPLKSAISKLNVMVFESETDFELRFEYRNDLFKEETIRSFADSFLKIVEQFLK
KSKLCEVELANENQLAELDNFNKTEFPFDDSKTVVDLFEEQCKKTPDKTAVVYKEKKFTY
AEIDEITNRIAGYVHSKGIGKEEVVSILIPRCEYMPIASIGVLKSGAAYQPLDPSYPPER
LQFMIKDANAKLLIADENLLELLPDYSGDILLTKDIPNLPKSDAVFTKPSPDDLFILIYT
SGSTGTPKGAMLEHKNVRSFCDFHIRNSDIDEHSVVSAYASYGFDACLSEMYPALIGGAE
LHIIEEDIRLDLVRLNRYFEDNGITHAFMTTQVARQFATEIDNHSLKYLLTGGERLVPLE
PPKNFELINGYGPTECTVYITTQPVDKLYHRIPVGKALDNIKLYVTDKYGRRLPTGALGE
LCASGQQVSRGYLNRPEQTAKAYEKNPYCNENGYERLYHTGDIVRLTDEGKVDFIGRNDG
QVKIRGFRIELSEVDKIIRKYDDITNTAVIARKLDGGGQCINAYIVADRKIDIQKLNEFI
LEHKPPYMVPAATMQIDKIPLNVNGKVDKRKLPEIKAESSKKKNSAPRELTFLEKKISAI
IEKIIGHSDFDISENLINAGMTSLSVIKLAVELNKAFGFEAQVKKMMKGCSVLSIEDELQ
EFMFSGTANPQTVKKEEKKEHKALYPLSKTQLGVYIDCMKNPYSTLYNIPSILTFSKSVD
AQKLADCVVKVIKAHPYIMTHLSLENDDIEQAYVDSAKPNVPVEKLTEEQLENYKKDFVK
PHNLMKAPLFRISVAETEKAVYLLSDFHHLIFDGASVALFFEQLKTLYEGGNIEPESYTY
FDYAENEIKAESSDEFRNAEKFFDNMMKNFESASEITADLRGHAEDGALASQAVPVDMAR
VENFCSQHGITPAHLFLAGTFYAVSRFVNSRNVYISTISNGRSDMRLTNCFGMFVKTLAL
GIEIENITSLEFVEKSKAVFTDSIENEIYPYAQLCAKYGYAPNIMYEYQLGVVDNLEIDG
KAVVRDYLEMNTAKFKTAVHIEDYKGKPSVVVQYNDALYSGELMRTLAKSVLCAVEHIIE
NPNGKIRKVSLLDNAAIAQLESFKSTEIAPVKTKLLHKMFEEQVAKTPDRIALSACDGKL
TYKELDRLANITANSLIEKGLEKGGKVLILLERTSKFFISLFGILKAGGAFIPSCPDYPK
ERIDSIIEDSDADFVITDGELLGVYDRTVDVSKLLSGNNEENPNVDVQPDDLAYLIYTSG
STGKPKGVMLRHIGIANYLAYSDSNIQVKEVVDNCHAYGSVTTISFDMSLKETMLSLCNG
LTLVFASEEQTVNPMSLAEFFKENNVDAFNSTPSRLLQYMELDEFAEAMANCKVILSGGE
KYPDKLLRVLREKTNATIINTYGPTEITVSSNAKNLTNADEISIGKPLRNYTEYIVDSDN
NLLPIGVVGELLIQGCGVALGYNKLPEQTAKAFIKFNGERTYRSGDYAKWTPDGDVIILG
RTDNQVKLRGLRIELGEIEKCLTAVDGIKSGIALIRKVGKADAICVYYTADRQIEPNEIK
SELAKSLTDYMVPSAYVQLDKMPLTPNGKVNTKVLPEPKSNKSESGRLPKNELEKTFCDI
FAEILELDNVFADDNFFDLGGTSLTATRIVISASKKNIEVAYSDIFANPTPQTLAKFVSK
DDSAEDDLENLSDYDYTNINKVLEKNNIDTFKNGELQKLGNVLLTGSAGFLGVHILYELL
HKYNGKVYCMIRDKNNNPAENRMNSIYYYYFEESLKERYPDRVTVISGDVTSRESFDKFI
DKDINTVINCAANVKHFSKGTDIEDVNLYGTLNVLAFCKKANARLVHVSTMSVGGMFVGE
QGPVDKLKENQLYFGQHEGSKYTLSKFLAERAILEEVSKGFNAKIMRVGTLAARNSDGEY
QINFTTNTFMGRLKSTLLIGKYPYEAMEMPFELSPIDFVAKAILLLAQAPKDCTVFHPFN
NHTLIMGDLYTEMNKIGLHSQGAEYEEYMIALDRAEQDPEKAKILSSMIAYQNMAHGQKT
FTVGKSNTYTMQVLYRMGFVWPVTSLDYMKRFINALRGLGFFD

Enzyme Prediction     

No EC number prediction in MGYG000000258_00635.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	13	2035	1551	3619	peptide synthase; Provisional
PRK12467	PRK12467	0.0	35	2035	66	2160	peptide synthase; Provisional
PRK05691	PRK05691	0.0	20	2047	677	2784	peptide synthase; Validated
cd05930	A_NRPS	5.16e-160	466	932	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	3.52e-150	1488	1955	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	1.51e-200	16	2040	558	2664
AFZ04852.1	3.36e-86	1388	2035	497	1180
BAZ00088.1	1.40e-85	910	2015	2105	3268
BAZ75991.1	1.40e-85	910	2015	2105	3268
BAY90071.1	4.11e-85	1259	2036	358	1175

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	4.20e-223	452	2041	205	1800	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	2.02e-209	452	1958	205	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	1.33e-121	452	1459	205	1205	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	2.42e-121	452	1459	205	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	2.80e-99	452	993	203	739	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	1.47e-304	12	2041	1665	3732	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064	7.83e-272	15	2045	1058	3129	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O30409	2.41e-270	16	2040	3128	5192	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C063	5.31e-270	15	2045	1058	3130	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O68007	1.72e-261	15	2044	72	2135	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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000258_00635.