CAZyme Information: MGYG000001514_03670

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_03670
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4748	MGYG000001514_12|CGC40	530907.9	4.8888

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 2380574; End: 2394820 Strand: -

Full Sequence      

MSKKRALDKKNVEDIFALSPLQQGVLYHTLHAPDDHLYVMQLNIKLTGSIQEALIIKAWQ
WMSEHHPVLRTVYRWKQIAQPVQVILRSQELNFHSMDWSRWGASEQAQRLEAFVQADRCQ
SFDLELSPFRVTLVKLKDDHYQMVITSHHILLDGWSLSLLLKEFWHAYQAFFRGESCIPQ
AQGSFKDYIKFLRSQPSKPSEAFWSNYLSGIAENTDLPLAKPASKAQKVNTRSASFKLSG
SILQELQRASKQNHVPLSAVYYGIWGLLLQRLTGKNAVFGTTVSGRNVQVPDVQTMLGML
INTIPLKSEPSANATLIQAIRDVRDALVERLAYETTALVDIAASCGLKKSEELFRSIVVL
ENFPVDHEMYHSDLLRMESIQEFSSNNYDLSLVIMPGAELKLEFKYNALLFDEEAIEQLG
TWFERLLLQFIHDAELEISRIELLADGDREKILHTFNDTHTAYPRERTISQLFEEQVAIR
GGDIAVSDGEREWTYAELNLRANRIARQLKAQGVGPEQVVGIMAERSLEMAAGILGILKA
GGAYLPIDPQYPLERISYMLEDSGSGWLLSASGWPEGLGFAGQRIPLDASLLEQGEGENL
PAAHRPEQLAYIIYTSGSTGQPKGVMIEQRSVVRLVKATNYVTFEPEDRLLQTGSLAFDA
STFELWGALLNGLQLHLAPQETLLSPGELKRVIRERGITLLWLTSSLFNQLSQADVELFR
GVRQLIVGGEALSPAHIEAVRQAHPGLKLVNGYGPTENTTFSTYYVIDKEHRESIPIGQP
ISNTTVYIVDGYQRLQPIGVPGELCVGGEGLARGYLNREELTKEKFVESPFRPGERMYRT
GDLARWTAEGTIEYLGRIDEQVKIRGHRIEPGEIAQAMLAQEEIKEAYVLVHHMQPSLAS
QGAEGGSAAHAASGEACLCGYYTAASPISAAELTQRLGDMLPSYMVPSFFIQLDELPLNA
NGKVDRRSLPQPDWARAVTSVYAAPESELETALVELWQEVLGVQRLGIDDDFFERGGHSL
KATTLIARIYKQFNLEVPLRELFRHATVRQLAHYMSSSMLPEAAETGYEAISPVEPRAYY
PASSVQKRLYAISQLEGAEVSYNIPQVLEITGELDEERFEQALQQLIRRHDSLRTSFELI
EGELVQRVQDVDAVCAGLSLKPEAASEEEAAARVQAFIQPFKLSEAPLLRAELLKLEEGR
HLLLLDMHHIVSDAVSMNVLLSEWMGLYEGASLPEPAIQYKDYAVWQQEQRQQERHAKQE
AYWLQELSGELPVLALATDKPRPPEQRFEGGQVAFEIGAELTRQLRELSARQGTTLYMTL
LAAYCVLLHKYTGQEDMIVGTPVAGRTRPELERVIGMFVNTLALRSYPQGAKTFTGFLQE
MKQTVLGAQEHQDYPFDELVEKLALHRDRSRNPLFDTMFVLQDGDHPLPAAANWTVREYP
CELRSSKFDMTLAARETEGRIQFQWEYGVHLYHGATVERMSRHFIRLLESIAERETAPLT
ELELLTSKEQEQLLYEFNATEAAYPQEKRIEELFAEQAQVRPEQTAVVAGEQSWTYGELN
ARANSLARELRERGVGPEQIVGILARPSLEMIAGILGILKAGGAYLPIDPQYPGERIRYM
LEDSGARLLLASSAAGEPEGPTSAPLGKPQGQASASTGERPGLASASLGEQLGLSSFTGD
ILDLEEEGLYQGDGSELALEDMNAGQLAYVIYTSGSTGQPKGVLVEHRSLVNLSVWHQQR
FAVRESDRSTKLAGFGFDASVWEIFPYLISGAALHIIDEATRTDIHALNAYYEREGITIS
FLPTPLCEQFMQLDNRSLRVLLTGGDKLNRFQKQRYLLVNNYGPTENTVVTTSQDVTALS
ANIAIGRPIANHSVYILGSDNRLLPIGVPGELCISGAGLARGYLNREELTREKFVESPFR
PGERMYRTGDLARWTAEGTIEYLGRIDEQVKIRGHRIEPGEIAQVMLAQEEIKEAYVLVH
HMQPSPATQGAEDGAAEHAAGGEACLCGYYTAASPISAAELTQRLGAVLPSYMVPSFFIQ
LEELPLNANGKVDRRSLPQPDWTRAVTSVYAAPESELETALVELWQEVLGVQRLGIDDDF
FERGGHSLKATTLIARIYKQFNLEVPLRELFRHATVRQLAHYMSSSMLPEAAETGYEAIS
PVEPRAYYPASSVQKRLYAISQLEGAEVSYNIPQVLEITGELDKERFEQALYQLIRRHDS
LRTSFELIEGELVQRVQDADAVCAELSLKPEAASEEEAAARVQAFIQPFKLSEAPLLRAE
LLKTGEDRHLLLLDMHHIIADGLSVYMLLEEWMSLYEGASLPEPTIQYKDYAVWQQEQRQ
QERHAKQEAYWLQELSGELPVLELTTDKARPPVQQFDGKRVMFTIGSSLAQRLRELSTRQ
GATLYMTLLAVYKIMLHKYTGQEELIVGTSVAGRTRPESERVMGMFVNTLALRSYPQGTK
TFTAFLEEIKQTVLGAQEHQDYPFDELVEKLALHGDRSRNPLFDVMFVMQNLGQIKKNYG
QLTIVPLEMEYPMAKFDITLTVEETGDNHLLGQLEYRTSLFDPATMERMTGHFLRLLEEV
AEQPALRLNSMALLTEEEHHQLVQVFNATSASYEAGQTLHSWFEEQVKNTPGRRAIRFGD
QQLTYSELNAKANCLGRILRERGVKPDRRVGILAEPSLELAVAVLAVLKAGGAYVPMDPD
HPLERMQYMVADSGMELLLTQQKFNHLADGLIDSVILIDSENQVTAAGGADAAEADLETI
SRPEHLAYVIYTSGTTGQPKGVLIEHRSIINALQWRNEEYAFTGQDKALQLFSFAFDGFV
LSFFTPLLAGVEIVLLDREQSKDARIIAQTIRDCGITTFICIPGLYAAILEGLNDDTQQP
PAALPLRIVTLAGDKPTAAMLKESSRLLPQVELVNEYGPTENSVVASCLRRMEQSKQITI
GKPIANVRLYVLNGCDQPLPLGVAGELCIGGAGLARGYLNRPELQAEKFTAASFDAGERL
YRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEARLLELEGVNEAVVTACTDPGG
DYSLCAYVTAASELPAVQLRQALAKRLPGYMVPAVIMQLERLPLNASGKVDRRSLPEPDW
AQASTSIYAEPESELETALVGLWQEVLGVQRLGIDDDFFERGGHSLKATMLIARIYKQLG
REVLLRELFRYPTVRQLAEHLSGTEQVVYKTIEIVEPRVYYPASSVQKRLYAISQLEGAE
VSYNIPQVLEITGELDEERFEQALHQLIRRHDSLRTSFELIEGELVQRVQDVDAVCAGLS
LKPEAASEEEAAARVQAFIQPFKLSEAPLLRAELLKLEEDRHLLLLDMHHIVSDAVSMNV
LLSEWMSLYEGASLPEPTVQYKDYAVWQREQRQQERHAKQEAYWLQELSGELPVLALATD
KPRPPEQRFEGGQVAFEIGAELTRQLRELSARQGTTLYMTLLAAYCVLLHKYTGQEDMIV
GTPVAGRTRPELERVIGMFVNTLALRSYPQGAKTFTGFLQEMKQTVLGAQEHQDYPFDEL
VEKLALHRDRSRNPLFDTMFVLQDGDHPLPAAANWAIREYPWELRSSKFDMTLTASEIEG
RLQFQWEYGVHLYHGATVERMSRHFVRLLESIAGRETAPLAELELLTSKEQEQLLYEFNA
TEAAYPQEKRIEELFAEQAQLRPEQTAVVAGEQSWTYGELNARANSLARELKAQGVGPEQ
IVGILARPSLEMIAGILGILKAGGAYLPIDPQYPGERIRYMLEDSGARLLLASSAAGEPE
GATSAPLGKPQGPASASTGERSGLVSASLGEQLGLSSFTGDILDLEEEGLYQGDGSELAL
EDMNAGQLAYVIYTSGSTGQPKGVLVEHRSLVNLSVWHQQRFAVRESDRSTKLAGFGFDA
SVWEIFPYLISGAALHMIDEATRTDIHALNAYYEREGITISFLPTPLCEQFMQLDNRSLR
VLLTGGDKLNRFQKQRYLLVNNYGPTENTVVTTSQDVTALSANIAIGRPIANHSVYILGS
DNRLLPIGVPGELCISGAGLARGYLNREELTKEKFVANPFRPGERMYRTGDLARWTPEGT
VEYLGRIDEQVKIRGHRIELGEITHQLLQLDQVRDAAVLTRQDPAGESILCAYLLTGGEA
DISQWRRQLAQKLPGYMIPHHFIRLEQFPLTPNGKIDYKALPEPELHPADMEGKPPGNEM
EALLVQVWKEVLGLAAVGVDDNFFERGGDSIKAVQIAARLHQQRLKLEVKHLFQYPTIEE
LSGYVKPLTAAASQEAVEGDVRFTPIQAWFMGQGFAEKQHWNQAFMLYREAGFEVKLVEA
SFRAILTHHDALRMVYLEEAGGIRQYNRGPDAEAVELTVQEWTGEAGAGLAAEVNRLQQE
LKLQTGPLVQLGLFHLPEGDHLLIVAHHLVMDGISWRILLEDFETGYRQASEGSDIRLPE
KSHSFQAWAEELERYANSKALLREKAYWSRTALETVPVLPQDGQAAVRRWGNAETVSAEL
DEQQTKQLLQEVHTAFKTEMNDVLLAALSLAIGEWSGHGRVPVQLEGHGREEILEGINIS
RTIGWFTTVYPVVLEVEQQQGLSYHLKQTKETLRRVPSKGIGYGVLKYMTSAEHKEDLQF
GAEPAISFNYLGQFDSSGSDRNDALFELSPLPTGQPISPSAPRSQALDVTGAVTGGRLRI
HLTYDREEYERQTMEQLAARYKETLLELIAHCLSRESTDVTPSDLGYNQLSLEQLDKVNS
LLKLKIKV

Enzyme Prediction     

No EC number prediction in MGYG000001514_03670.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17645	A_NRPS_LgrA-like	0.0	1532	2058	2	440	adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
cd19531	LCL_NRPS-like	0.0	3220	3633	1	424	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd17645	A_NRPS_LgrA-like	0.0	3673	4182	2	440	adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
cd17655	A_NRPS_Bac	0.0	1532	2061	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
cd17655	A_NRPS_Bac	0.0	3673	4185	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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
BAY90071.1	0.0	1261	4266	316	3284
QND46664.1	0.0	545	3198	1	2659
BAZ75991.1	0.0	1261	4266	317	3293
BAY30132.1	0.0	1261	4266	317	3295
BAZ00088.1	0.0	1261	4266	317	3293

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	0.0	1525	3124	202	1721	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]
6MFZ_A	0.0	1525	3221	202	1813	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFW_A	3.01e-212	1525	2577	202	1184	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	7.50e-212	1525	2577	202	1184	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
2VSQ_A	4.31e-201	9	1057	6	1041	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	2168	4743	6	2559	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	1080	4742	11	3600	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	2168	4743	11	2553	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	2168	4738	11	2553	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	1080	4747	10	3583	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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_03670.