CAZyme Information: MGYG000001514_03665

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_03665
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3542	MGYG000001514_12|CGC40	401751.83	4.9695

Genome Property

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

• Gene Location: Start: 2335911; End: 2346539 Strand: -

Full Sequence      

MSQSKELQMVLPLIPMQKGMLYHYLLDRDSNAYFEQMAFQFTGKLELPLFEESYNYILQR
YDAFRTVFIHEGIDEPVQVVLKERKGSIQSANIAHLSNTEKEAFIEDYMKQDREKGFDLS
KDILFRISVLELDSNCCHVIISNHHIIMDGWCLGKVLNELFTVYHQLKNKQPVQLGKVYP
YSHFVRWLAKQDKEEALDYWRSYLDGYAEKASLPQESSAADGFEQQLDDCYLSRELTAAL
NELSKMYQVTLNNTVQVIWAILLQRYNRCDDIVFGSVVSGRPSHIEGVEEMVGLFINTVP
VRVQASPNQAFSDLLKQVWKQFVASENYHYVSLADIQAASELKQELLDHLLVFQNYPIDT
QLDHHEVQRDAAAVQDFRSFEQTSYDFNVTIVPGEELRLNFNYNGLKYSRDAVANIGEHF
RHIAEQVVGDPDIYLNRIELITEAEKLQILQQFNATARSYELNQTTPQLFEQQAEQYPDQ
TAVVFKQEKLTYRELNERANQLAGWLRKKGVQPDSIVGIMLDRSLDLLIAVMGVLKAGGA
YLPIDPQYPQERVQYILDDSETSLLITDRNSVSTAAFHKEVVYMDEPEISKESIANPESS
SAPHHLAYVIYTSGTTGLPKGVLIEHRNLVNATYAWREEYGLDRKRMNLLQMASFSFDVF
AGDVSRTLLNGGTLVLCPAEAKLSPADTYDLLVNHNIHIFESTPALILPLMEYVYEHGKA
LPSLDLLILGSDSCSSVDFEKLLCRFGQDMRIINSYGVTEACIDSSYYEADSPRLNVKGH
VPIGRPLPNMKLYIVDADRRLMPVGIDGELCIGGAGVARGYMNKPELTAERFVPNPFVPG
ERMYCTGDYARWLPTGDIQFIGREDTQIKIRGYRIELSEITARLLEHSAIERAVVIAREE
GGQPAYLCAYIVPRAKWNAAELRAYLQQFLPEYMLPSQFLALEALPLTPNGKVDTRALPE
PEGGTESGTEYAPARNELEEKLVEIWEGVLNKRRIGIRDHFFVLGGHSLKATVLVSRIHK
HLGLELPLREVFQRPTIEQMAEYLQTAVNNSFEAIPIAPLKEFYPVSFAQRRMYVVSQLE
EHGINYNMPNVLRVEGPLDPIRLQASFRDLMQRHEALRTSFAMVDGELVQRIHEQPELRI
NFMAEEVSLEAQIDAFIQPFDLGQAPLLRVGVIRRSEQEHILLIDMHHIISDGLTTDILL
HDWLCLYENQGDALPKLRIQYKDYAQWQSEWLQSDSYKEQERYWLETLKGDIPVLNLPVD
YPRPAVQQFAGNVIEFSMDKELTAKLKELMREEETTLYMTLLAAYNLLLSKYSSQEDIMV
GSVVAGRHHSDLESVAGMFVNTLIMRNKVASSHTVQQLLQSVKDNCLKAFENQDYPYEEL
IEKLGVQRDLSRNPLFDTMFIVQSVEQQAQQPASVQQGLRVTPYPHEHHVSKFDLTLMAV
DAEDEVLFSLEYCTKLFNEDTVRRMAGHFCTIIGEIVRNKDKRVAEIELLTSSEREIVQY
EFNRTYAEFPKDTTIQALFEEQAKRTPDRTALLMGEERLTYSQLNERAAQLGYLLRSKGI
GTECIVGIMMERSFEMMAGVLGILMAGGAYLPIDPAYPAERINYLLKDSGTKLLLTCGPL
PNGLQFDGEILDLETSPPAFVEAGTLPRGNASDLAYVIYTSGSTGQPKGVMIEQAGVVNV
LFSLQQEYPLGEQDRYLLKTNYTFDVSVTELFGWIPGGGSLVILPPEDEKDPEKLISAIE
KNQVTHINFVPSMLQLFAAGEHSLERISSLKYILIAGEPLPHELVKKLYQRLPAGIRLEN
IYGPTEGTIYATKHSVGRECAQIPIGRPLDNVRIYILNQEQHLQPIGIPGELCIAGEGVA
RGYLNRAELTLEKFAENPYEPGQRMYRSGDLARWLPDGSIEYMGRLDHQVKIRGYRIELG
EITEQMRRHPAIKDVVVMPHAVSDGDTSLVAYLVSDQVWSITEVRQHLSITLPEYMIPSY
VIQIERLPLTASGKVDRNRLPKPDGLIRTHAAYVPPRTLLELQLERIWREVLGIKRAGIN
DSFFELGGHSLKATAMLSRMQRELQIEVPLRIVFQRKTIQELAAYIEEHDLQNKYSSIPA
VPEREYYPVSSAQKRIYMVSQVEEEDIGYNLPVVQPLSGDIDPVHFRAALEKMIVRHEAL
RTSFDIAEGELVQIVHPHAELAFEIIETDESKLQETITAFVRPFDLSAAPLARFALIKTS
ENRTLFLYDMHHIISDAASLSVFNQELLWIYENGELPPLRIQYKDYAVWQQQVLKADLLA
QQEQYWLKQFEGEIPVLDLPTDYPRPSVQQFDGGKVSFEWSSELTHELRKISAAHGTTLF
STLLAAFSILLTKYTGQEDNVIGTVLVGRPHSDLENLMGMFVKTVPIRSLPAGSKAFPVF
LKEVQEQILLAQDHQDYPFEELVEKLNVQRDLSRHPLFDVMITMLTVEAPDHMDDSSVDH
HETGEEYEFNISKFDLALDIIEEPGSLKLAFEYSTSLFKKSTIQRMAGHFTEIIYGIVSQ
AQVRIAELNMITQAEKRQILHDFNDTAMSYPSDKTIMQCFEQQVNSTPDHPMLYYKGEAH
SYAQVNGKANQLANRLRAEGVGRGSLVGIMAERSVEYIVGVLAVLKAGGAYIPVDPSYPR
DRIAHIFEDSQASLLLMNGRDVQRAPAGHTIVLLDDPLSYQGSADNQAMEGVSAYDRAYI
IYTSGSTGLPKGVIIRQNSVINLAQWFHNTYNLTKNNKVIQMTNISFDVSVLETLVTFLH
GGTLFIPDAEIILDRQAFYEYVNRHRIQVCQFVPVTLQELVAHSPRMESLQVLISGGDKL
EPSLVNQVVSKGYRLFNHYGPTETTVDVLHHPCALNEETVLLGRPFGNVHAYVLNALGQL
QPIGVPGELCIAGACVAEGYLNQPELTAAKFIDNPFVSGERLYRTGDAARWNEAGELEFL
GRLDNQVKIRGFRIEIGEVESRLLTHESIQEAIVIAKVIHGSKQLCAYVKSDQEMTTSQY
RAILEEHLPHYMIPSFFIRLESFPLTPNGKVDRKALPIPEGVIYRNTEYVAPRNATERKL
VELFAEGIGIPEAQISMHDNFFELGGHSLVILKLLAKTYVLQWPLTIKDFYICKNIEQLA
AKIDGTLAVEEEPTTGLHRPQTEWIQRKAQQPVQLSGEQAPLDHVLLTGATGFLGIHLLY
ELLTDTGAEIHCIIRGKDRFMAQQRLVKKLHFYFPDEADEQMNFWLARIHVYPGDVTKAD
LGLSPEVREQLGHSVDSVIHTAALVKHYGYYEDFYRMNVQGTAHVAEFCQSYNLRMHHIS
TTSVAGSIPQDRQTEMSFTESSFYIGQNYDDNLYIRSKFEAEGLIYEAMEKGLQASIYRV
GNLTGRYGDGAFQENMDENMFYNRLKSFIQIGIAIAEMAEQTEEFTPIDSCAEAILKIVR
TKEAAGNVFHIFNPRPTTYALICEALQEAGYKMEQLSEAEAASHLEELMKDESKHEWLSG
FMADRPDAEAEEAQINVDVAAPFTQHYLGQLGFDYPLVNQEYIQKLVNYMYKSEVKQDAI
NK

Enzyme Prediction     

No EC number prediction in MGYG000001514_03665.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	2558	3040	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.
cd17650	A_NRPS_PpsD_like	0.0	478	958	1	447	similar to adenylation domain of plipastatin synthase (PpsD). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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.
cd17646	A_NRPS_AB3403-like	0.0	1517	2000	2	488	Peptide Synthetase. 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.
cd19531	LCL_NRPS-like	0.0	1064	1479	2	426	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.
cd17655	A_NRPS_Bac	0.0	1518	2004	2	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
QND46664.1	0.0	542	3137	1	2675
BAZ00088.1	1.42e-318	194	3121	313	3290
BAZ75991.1	1.42e-318	194	3121	313	3290
BAY90071.1	1.42e-318	188	3120	306	3280
BAY30132.1	4.71e-316	194	3121	313	3292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	430	2086	171	1797	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	0.0	430	2007	171	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]
2VSQ_A	1.85e-229	13	1057	15	1052	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.19e-205	1064	2000	6	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
6MFW_A	9.12e-198	1508	2535	200	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	1064	3139	6	2100	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	1	3123	1	3104	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1	2386	1	2384	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	1	2387	1	2388	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	4	3124	3	3105	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
1.000071	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_03665.