CAZyme Information: MGYG000002482_01419

Basic Information

• Species: Ruminococcus_E bromii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E bromii
• CAZyme ID: MGYG000002482_01419
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2443	MGYG000002482_69|CGC1	274996.44	4.9064

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002482	2151595	Isolate	United States	North America

• Gene Location: Start: 33584; End: 40915 Strand: +

Full Sequence      

MSNLINLLDTYKGEKRELYPLTPSQMGVYLSCMHNPKGTMYNIPCTYVFDKGSLDTDRLI
NAVRKTVDNHPIMKIFIDNSTGSPMMKLRDSVDFDIPVIQVDNLEQAGKDFVKPFELEKD
ILFRFAVFECGDKSMFAMDLHHIISDGTSVSVICNDIALAYNGKELEPEKFSQLDLSVFE
EKLEETEDYKKSKEYYDNIFSAVESKTEITEDFAENSEVEDKPNGSFELSTNEKFSVEDV
RNFALANQITPYTVFLGAYEYAVAKFTNQSETTVCTVTHGRFNKRLKNTVGMMVRTLPIH
ANIDEEDTVSDYLKKIRRNIKETVANDWYPFMKLASDYDLSADIMLAYQADIFNTFKIGG
QTLKLKLVPLKSAISKLNVMVFESETDFELRFEYRNDLFKEETIRSFADSFLKIVEQFLK
KSKLCEVELVNENQLAELDNFNKTEFPFDDSKTVVDLFEEQCKKTPDKTAVVYKEKKFTY
AEIDEITNRIAGYVHSKGIGKEEVVSILIPRCEYMPIASIGVLKSGAAYQPLDPSYPPER
LQFMIKDANAKLLIADENLLELLPDYSGDVLLTKDIPNLPKSDAEITKPSPDDLFILIYT
SGSTGTPKGAMLEHKNVRSFCDFHIRNSDIDEHSVVSAYASYGFDACLSEMYPALIGGAE
LHIIEEDIRLDLVRLNRYFEDNGITHAFMTTQVARQFATEINNHSLKYLLTGGERLVPLE
PPKNFELINGYGPTECTVYITSQPVDKLYHRIPVGKALDNIKLYVTDKYGRRLPTGALGE
LCVSGQQVSRGYLNRPEQTAKAYEKNPYCNENGYERLYHTGDIVRLTDEGKVDFIGRNDG
QVKIRGFRIELSEVDKIIRKYDGITNTAVIARKLDGGGQCINAYIVADRKIDIQKLNEFI
LEHKPPYMVPAATMQIDKIPLNVNGKVDKRKLPEIKAESSKKKNSAPRELTFLEKKIAAI
IERIIGHSDFDISENLINAGMTSLSVIKLAVELNKAFGFEAQVKKMMKGCSVLSIEDELQ
EFMFSGTANPQTVKKEEKKEHKALYPLSKTQLGVYIDCMKNPYSTLYNIPSILTFSKSVD
AQKLADCVVKVIKAHPYIMTHLSLENDDIEQAYVDSAKPNVPVEKLTEEQLEAYKKDFVK
PHNLMKAPLFRISVAETEKAVYLLSDFHHLIFDGASVALFFEQLKTLYEGGNIEPESYTY
FDYAENEIKAESSDEFRNAEKFFDNMMKDFDSASEITADLRGHAEDGALASQAVPVDMAR
VENFCSQHGITPAHLFLAGAFYAVSRFVNSRNVYISTISNGRSDMRLTNSFGMFVKTLAL
GIEIEDITSLEFVEKSKAVFTDSIENEIYPYAQLCAKYGYAPNIMYEYQLGVVDNLEIDG
KAVDRDYLEMNTAKFKTAVHIEDYRGKPSIVVQYNDALYSGELMRTLAKSVLCAVEHIIE
NPNGKIRKVSLLDNAAIAQLENFKSTEIAPVKTKLLHKMFEEQVAKTPDRIALSACDGKL
TYKELDRLANITANSLIEKGLEKGGKVLILLERTSKFLISLLGILKAGGAFIPSCPDYPK
ERIDSIIEDSDADFVITEGELLNKYDLTVDVSKLLSGNNDEDPNVDIQPDDLAYLIYTSG
STGKPKGVMLRHIGIANYLEYSDSNIQVKEVVDNCHAYGSVTTISFDMSLKETMLSLCNG
LTLVFASDEQTVNPLSLAEFFKENNVDAFNSTPSRLLQYMELDEFAEAMANCKVILSGGE
KYPDKLLRILREKTNAIIINTYGPTEITVSSNAKNLTNADEISIGRPLRNYTEYIVDSDN
NLLPIGVVGELLIQGCGVALGYNKLPEQTAKAFIEFNGERTYRSGDYAKWTTDGDVIILG
RTDNQVKLRGLRIELGEIEKCLTAVDGIKSGIALIRKVGKADAICVYYTADRQLDPDEIK
SELAKSLTDYMVPSAYVQLDEMPLTPNGKVNTKVLPEPKSNKSESGRLPKNEIEKTFCDI
FAEILELDNVFADDNFFDLGGTSLTATRIVISASKKNIEVAYSDIFANPTPQTLAKFVSK
DDSAEDDLENLSDYDYTNINKVLEKNNIDTFKNGELQKLGNVLLTGSAGFLGVHILYELL
HKYNGKVYCMIRDKNNNPAENRMNSIYYYYFEESLKEKYPDRVTVISGDVTSRESFDKFI
DKDINTVINCAANVKHFSKGTDIEDVNLYGTLNVLDFCKKANARLVHVSTMSVGGMFVGE
QGSVDKLKENQLYFGQHEGSKYTLSKFLAERAILEEVSKGFNAKIMRVGTLAARNSDGEY
QINFTTNTFMGRLKSTLLIGKYPYEAMEMPFELSPIDFVAKAILLLAQAPKDCTVFHPFN
NHTLIMGDLYTEMNKIGLHSQGAEYEEYMIALDRAEQDPEKAKILSSMIAYQNMAHGQKT
FTVGKNNAYTMQVLYRMGFVWPVTSLDYMKRFINALRGLGFFD

Enzyme Prediction     

No EC number prediction in MGYG000002482_01419.

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	6.94e-161	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	1.73e-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	2.66e-206	16	2040	558	2664
BAY30132.1	1.68e-92	52	995	2279	3270
BAZ00088.1	8.50e-92	52	1021	2277	3294
BAZ75991.1	8.50e-92	52	1021	2277	3294
AFZ04852.1	2.42e-85	1331	2035	431	1180

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	5.80e-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	1.46e-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	2.24e-122	452	1459	205	1205	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	4.06e-122	452	1459	205	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	3.37e-100	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	6.52e-307	12	2041	1665	3732	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
O30409	1.31e-274	16	2040	3128	5192	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C064	7.03e-273	15	2045	1058	3129	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	3.54e-271	15	2045	1058	3130	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O68007	2.61e-263	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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002482_01419.