CAZyme Information: MGYG000000392_01837

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_01837
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2422		273365.45	4.9457

Genome Property

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

• Gene Location: Start: 9942; End: 17210 Strand: -

Full Sequence      

MNNNKKTALSKTEYGIYFDYLNNPGSIAYNIPLFLKLDKDIDITRLKQAVEAVIENHPYI
KSRLTADSDGVVYKLSSDEPAVVEVKEMHDADFDKKSLVYPFELLSERLYRCCIISLDSY
VMLFCDFHHIIFDGSSAKIFLNDVDRAYNGLPLEPEHFTGNDVSDEEEERLKTDELKAAK
EYYNSVFGGIELDSVMLNDKNDRKPLAKAVDYEFTSFNADDIRKFCRKNGIKTSTFFCGV
YGFLLAKFSGAEESLFATIHNGRNEKLSNSCGMFVKTLPVYCNFSKNESIVQFLKNLDSQ
LQDNRKYDLYSYADICSDLKINPPTIFAYQGDIFRNINFCGKEIFADSIDVPDAKANIAA
ELSRINGRFSLRFEYRADLYEEESAESFLKSFEKAVTEFIGKENINDIDITDSEQLALLD
SFNNTERDYEKTDIVTLFRRQAEQNPDNTAVVYLDKSYTYKEVDEISERIGAYISSLGIG
REDVVSVLIPRCEYMVLASLGVLKSGAAYQPLDPSYPQERLEFMMQDADAKLLIAGKDLL
KLVPNYNGKVLLIEDIPALPPCEKIKENPNPENLFIMLYTSGSTGTPKGCMLEHRNIVSF
CNWYRNYYNLTPQSRVAAYASYGFDADMMDLYPALTTGAAVYIIDEAIRLDLLAIDKYFN
ENKITHSFMTTQVGRQFAVEIDNSSISELSVGGEKLVPLAPPKNHKMINLYGPTESTVCI
TAFELDRLYERVPIGKALDNTKLYVVDKQGRRLPPCVPGELWVAGHGVSRGYLNRPEQNE
KAFIRNPFTDEKGYERVYRTGDIVRYLPDGNIDFVGRNDGQVKIRGFRIELSEVERIIRE
FDGIKDATVAAFDEAGGGKFIAAYVVSDEKVDIQKLNEFILANKPPYMVPAVTMQIDRIP
LNQNQKVNKRALPKPEKKAQNSEPSSKPMTLLEKKIHSIIAKILGNDKFSVTENLLFAGL
NSLSVIKLAVELHKEFGFEANVKQMMKECSVISIEDQLQEYLMSGALAKITAETKQKAYK
SLYPLSKTQLGVYLDCMKNPYTTLYNIPSFLKFTKSINAEKLADSAKKVILAHPYIFTHL
TTQNDDVEQVYPDSRQLDIPVKKMTENELEFLKKEFVKPFNFSKSPLFRILVVETERNIY
LFADFHHIIFDGASYNVFLNQLKAAYEGAEIKSEDYTYFDYIDDEIKAESSEEYSKAEKF
FDEMMKNFESASEITPDIGSQGDNGKLAEVNVPFDLAEIEAFCNKNGVTPAQLFLAAAFY
SVSRFTNSRNVYLSTISNGRSDMRLTDCFGMFVKTLPLGIEIEDISTLEFVKKSKSVFTG
AIENEIYPYSKICSKYGFAPNIMYEYQIGVTDDLKIDGEAVERNFFDMEITKFKTAIYIE
NYKNQPRIVVRYNEELYSKDLMQTLVKSIFNTAMHIISAPDSKIRKISLLDDSQIDELNS
FSLTRIAPVETKLLHKRFENQVEKTPDNNAITACDGTLTYRELNRRANVTANELIARGLK
KGGRVVVLLSRTSKIFSTIFGILKAGGAFIPTCPDYPQERINSIIEDSEADFVVTEGELV
NAYDKTIDVDLLLGGENCETPQVDVSPEDLAYLIYTSGSTGKPKGVMLRHIGIANYLSYS
DANPQVKYIVDNCKAYGSVTTVSFDMSLKETVLSLCNGLTLVFASDEQTVNPIALAKFLK
ENKVDAFNSTPSRLLQYMELDEFAEAMADCKVILSGGEKYTYKLLKLLREKTNAKILNTY
GPTEITVSSNCKDLTNADEISVGKPLLNYVEHIVDVDNNLIPVGVVGELLISGCGVALGY
NKLPEQTKKAFIEFNGERTYRSGDYAKWTRNGDVVILGRTDNQVKLRGLRIELGEIEKCL
SNINGIKSAVALIRKVNNADAICAYYTSDVQFDAEFIKNELKKSLTDYMVPAAYVQLSEM
PLTPNGKINTKLLPEPQSSEKKTGAKPTTALEKTMCDIFSKVLELDKVYADDNFFDIGGS
SLTVTRVIILANKSGIEIAYGDVFENPTPAALAKLCEKDAPKNDFEDLGNYDYSNIENVL
LNNNLDSFKNGDMQGIGDVLLTGAAGFLGIHILYELLHRYSGKVYCLLRDKHNNPAEDRL
NMIFFYYFEESLKENYSDRLTVLSGDVTDRESFDKFLDFNIDTVINCAANVKHFSKGTDI
EDVNLYGTLNVIDFCKQADARLIHVSTMSVGGIYVGEQGEVTHLKENQLYFGQQTTSKYT
LSKFLAERAILEEVSKGFNAKIMRVGTLSARNSDGEYQINFTTNTFMGRLKSNIIIGKYP
YDMIETPFELSPIDFVAKAILLLSQTPKNCTVFHPFNNHMLMMGDLYMEMDRIGLHSQAA
ETEEYEKALEEAKQNPEKAKILSSMLAYQNMAHGQKIFSVGKSNKYTMQVLYRMGFHWPV
TSLDYMKRFINALRGLGFFDFN

Enzyme Prediction     

No EC number prediction in MGYG000000392_01837.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	23	2013	66	2160	peptide synthase; Provisional
PRK12316	PRK12316	0.0	9	2020	1559	3626	peptide synthase; Provisional
PRK05691	PRK05691	4.76e-179	23	2013	692	2772	peptide synthase; Validated
cd05930	A_NRPS	3.67e-163	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.
cd12117	A_NRPS_Srf_like	2.91e-152	437	912	2	483	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	2.37e-203	9	2018	563	2664
ACX49739.1	6.30e-101	9	1737	12	1856
BAY30132.1	1.07e-89	3	974	2243	3270
BAY90071.1	7.09e-89	3	974	2232	3259
BAZ00088.1	6.17e-88	3	1000	2241	3294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	5.49e-229	437	2013	210	1794	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	9.62e-219	437	1939	210	1718	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	2.69e-133	437	1430	210	1201	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	6.64e-133	437	1430	210	1201	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	4.28e-108	437	1000	208	766	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	4.20e-267	28	2015	1693	3728	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
O30409	4.01e-253	28	2025	3152	5199	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C064	1.87e-250	28	2018	1083	3124	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O68007	1.48e-244	28	2019	97	2132	Bacitracin synthase 2 OS=Bacillus licheniformis OX=1402 GN=bacB PE=3 SV=1
Q04747	6.49e-241	21	2018	1070	3106	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3

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
1.000077	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000392_01837.