CAZyme Information: MGYG000001453_01839

Basic Information

• Species: Aneurinibacillus aneurinilyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus
• CAZyme ID: MGYG000001453_01839
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4450	MGYG000001453_109|CGC1	508876.32	4.9407

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001453	5302959	Isolate	not provided	not provided

• Gene Location: Start: 8853; End: 22205 Strand: +

Full Sequence      

MSTFKKEHVQDMYRLTPMQEGMLFHALLDKEKNAHLVQMSIAIEGTVDVELLSKSLNVLI
DRYDVFRTTFLHEKIKQPLQVVLKERPVQLQFKNISSLDEEKKEQVIRQYKYQDEETVFD
LTKDHLMRVAIFQTGKVNYQMIWSFHHILMDGWCFNIIFNDLFNIYVSLKEKKPLQLEPV
QPYKQFIKWLEKQDRQEALRYWKEYLINYSQSAAVPKKKVSINHTTYKPAQFHFAFDRAL
TQQLLRIANQSQVTLNIVFQTLWGIVLQKYNSTDDVVYGSVVSGRPSEISGIEKMVGLFI
NTLPLRIQTQKDQSFVELVKAVHQSVLLAQQYEYFPLYEIQNHTELKQDLIDHIMVIENY
PLVEELQKNSIMQKVGFTVRDAKMFEPTNYDMTVMVLPRDEISVRLDYNAAVYDIDFIKK
IEGHMKEVALCVANNPYVPVQDISLLTQQEKQHLLVELHDSMTRYPDKTVHQLFTEQVEK
TPDHVAIVFEGEKVTYRELHDRSNQLARFLREKGVKRESIIGIMMERSIEMIVGILGILK
AGGAFVPIDPEYPKERIDYMLDSVQLVLTQRQLKDKFAFTKETVVIEDPGILQELTEEMD
YINDSEDLFYIIYTSGTTGKPKGVMLEHRNIVNLLHFTFEKTNINFNDKVLQYTTCSFDV
CYQEIFSTLLSGGQLYLIRKETQRDVEKLFDLVKRENIAVLSFPVAFLKFIFNEKEFINR
FPICVKHIITAGEQLVVNNEFKRYLHEHNVYLHNHYGPSETHVVTTYTIHPEAEIPELPP
IGKPISNTWIYILDQEQHLQPQGVVGELYISGANVGRGYLNNQELTAEKFFADPFRPNEK
MYRTGDLARWLPDGNIEYLGRADHQVKIRGHRIELGEIEAQLLNCKGVKEAAVIDKADDK
GAKYLCAYVVMEAEVNDTELRNYLGKALPDYMIPSFFVTLDQLPLTPNGKIDRKSLPNPE
KVVNTNVKYAVPTNELEKKLAKIWEEVLGIPQIGIQDNFFSLGGHSLKAITLISRMNKEC
NVDIPLRLLFEAPTIQEISNYINGAKRENYVAIQPVPQQQYYPVSSVQKRMFILNEFDRS
GTAYNLPGVMFLDGKLNYKRLEEAVRKLVDRHEALRTSFHSINGEPVQQIHQNVELQIAY
SESTKDQVERIIAEFMQPFALEVAPLLRVGLVKLEAERHLFIMDMHHIISDGVSMQIMIQ
EIADLYKGKELPALGIQYKDFTIWHNHLLQSEAIKKQEAYWLDVFAEEIPVLNLPTDYSR
PTSQSFDGKRFTFSTGKQLMDDLYKVAKETGTTLYMVLLAAYNVFLSKYSGQDDIVVGTP
IAGRAHADVENMLGMFVNTLAIRSRLNHEDTFKDFLANVKQTALHAYENPDYPFDTLVEK
LGIQRDLSRNPLFDTMFVLQNTDRKSFEVEQVKVTPYVPNSRHSKFDLTLEVSEEQNEIL
FCLEYCTKLFVDKTVERMAAHFLQILRAIVGNPAIIISEIELLTEEEKQHILFEFNDTKA
TYPHMQTIQGLFEEQVEKTPDHIAVVWEEQTLTYRELNERANQVARILRQKGVQPDNIVG
LLVERSLEMIVGIMGILKAGGAYVPLDPEYPEDRISYMIQDCCVHIMLTQQHLLHLVHDG
FDCVVLDGESLYQGDSSNLNPVNQAGDLAYIMYTSGSTGKPKGVMVEHRNVIRLVKNTNY
VQVHENDRVIQTGAIGFDALTFELFGSLLNGAGVYPVAKDVLLDAEKLREFLQVNQITIM
FLTTPLFNQLSQGTEEMFAGLRSLIVGGDALSPKHINNVKRKCPNLAMWNGYGPTENTTF
STCFLIDKEYDDSIPIGKAISNSTVYIMGRYGQLQPVGIPGELCVGGDGVARGYMNQPAL
TAEKFVPNPFVPGGRMYRTGDLARWLPDGTIEYLGRIDHQVKIRGYRIEPGEIETLLVKH
KKVKEAVIMVVEDNNAQKALCAYYVPEEKVTVSELREYIAKELPVYMVPAYFVQIEQMPL
TQNGKVDRKALPKPEGECGTATEYVAPSSDIEIKLAEIWHNVLGINRIGVLDNFFELGGH
SLRAMTIIAQVHKEFGVELPLKVLFATPTISALAQYIADGEKGRYSAIQPAALQDYYPVS
SAQKRMYILYEFEGAGITYNVPSVMFIEGKLDYQRFEYAIRSLVNRHEALRTSFYSINGE
PVQKIHQNVELQIAYSEAKEDQVEQIVESFVQPFDLGLAPLLRVGLVKLALDRHLFLIDM
HHIISDGVSMQMITNEFADLYKGKELAELRIQYKDFAVWQNEWFQSDAIEKQEAYWLNTF
AEEIPVLNLSTDYPRPMIQSFEGDIVTFNSGRRLAEELKRLATETGTTLYMLLLAAYNVL
LHKYSGQEEIVVGTPIAGRSHADMENIVGMFVNTLALKNTPIAARSFREFLLEVKQNALE
AFENQDYPFENLVEKLQVRRDLSRNPLFDTMFSLNNADEQVGIEIEGLSFRPYEMQYWIA
KFDISLDALEKQDEIQFYFNYCTNLFKKETMERLATHFMHILQEIVTNPEVKLCEINMLS
EEEQQRVRYDFNATDVTYATNKTFHQLFEEQVEKTPDSVAVIDEKEKLSYRELNAKANRL
ARVLRQKGVQPGSMVGIMVDRSLDMIVGMLGVLKAGGAYVPIDIDYPQERISYMMEDSRA
VLLLTQQKLAQQIAFPGDILYLDQAESFHEEASNLEPVAHPQDIAYIIYTSGTTGKPKGV
MIEHQSYVNVAMAWKDAYRLDTFPVRLLQMASFAFDVSAGDFARALLTGGQLIVCPNEVK
MDPASLYSIIRKYEITIFEATPALVMPLMEYIYEQKLDISQLQILIVGSDSCSMEDFRTL
VSRFGSTMRIVNSYGVTEACIDTSYYEQPLSSLHATGTVPIGKPYANMRMYIMNQYLQVQ
PVGVIGELCIGGAGVARGYLNRAELTAEKFVPNPFVPGEKLYRTGDLARWMPDGNVEFLG
RNDHQVKIRGIRIELGEIEAQLRKHDSIKEAIVIAREDHIKEKYLCAYMVTEGEINVAEL
RAYLANELPVAMIPSYFVSLEAMPLTPNGKIDKRSLPEPDNSVSIGTEYVAPRTMLEGQL
EEIWKNVLGLQRVGIHDDFFTIGGHSLKAMAVISQVHKECQAEVPLRVLFETPTIQGMAK
YIEETDTEHYMAIQPVSKQEYYPVSSAQKRMFIVNQFDGVGISYNMPSIMLIEGKLEPQR
LETAFKRLIQRHESLRTSFEIINGKPVQKIHEEIDFNMSYQVVSNDQVEKMIDEFIQPFD
LSVAPLLRVELLKLEEDRHILIFDMHHIISDGISSGILMNELGELYQDNALPELRIQYKD
FAVWQNKWFQSEAFKKQEEYWLNAFADELPILDIPTDYSRPMQQSFDGAQLTFGTGKQLM
DGLYRVAAETGTTLYMVLLAAYNVLLSKYSAQEDIIVGTPIVGRSHVDLENIVGMFVNTL
AMRNKPEGEKTFKALVLEVKQNALEAFENQDYPFEELIEKLEIQRDLSRNPLFDTLFSLQ
NMDEESFELAGLTCQPFDVASKLEQVKFDLSLVAVEEEEEIVFGLQYCTKLYKRETIEQM
IQHFIQIVKAIVENPDVKLHDIDMLNEAEKKQIMFEFNDTKRQYLHNQTMQELFEEQVRK
TPEHIAIVWEGQALTYDELNIKANQLARVLREKGVAPNRPVAIMAERSLEMIIGMFGILK
AGGAYVPIDPAYPQERIQYLLEDSGATLLLAQPHVLNKLPVDIEWMNLTDEQNYTGDGAN
PPFINQSTDLAYIIYTSGTTGKPKGVMIEHQSIINCLQWRKEEYGFGPGDTVLQVFSFAF
DGFVASLFAPIFAGAKSVLPREEEAKDPVALKKLITSEEITHYYGVPSLFSAILAVSSRN
DMQNLRCVTLGGEKLPAQIVKKIKEKNGGIEVNNEYGPTENSVVTTIMRNIQVEQEITIG
RPLANVEVYIVNHNHQLQPVGVVGELCIGGRGLARGYLNKPDLTADKFVSNPFVPGERMY
KTGDLAKWRSDGMIEYVGRVDEQVKVRGYRIELGEIESAILEYEKIKEAVVIVSEHTTSE
QILCAYIVGEEEVSTLNLRSYLAKSLPSYMIPNYFIQLDTMPLTPNGKVDRKALPEPQTI
GLMTREYVAPRNEIEAQLAFIWQEVLGIELIGITDNFFELGGHSLKATLLVAKIYEHMQI
EMPLNIVFKHSTIMKIAEYIMLQQSENKVHQPIPVNAEAEEDTLSSTDRKPRTTVELPIL
LNEEAERNAFCFAPIGAQGIFYKKLAEQIHTASLYGFDFIEDDDRIQQYIEAMVQIQSDG
QYVLIGYSSGGNLAFEVARQMEKQGYHVSDLVLFDVYWKGRVFEQTKEEEEENIKVIMDE
LRENPGMFNMTREEFELYFTNEFVKQSFTRKMRKYMSFYTQLVNYGEVGATIHLIQAEFE
EEKIDENERFDEEEKTYLEEKWNEKAWSKAAKRFVKYNGYGAHSNMLGGDGLERNSSILK
QILQGTFVLK

Enzyme Prediction     

No EC number prediction in MGYG000001453_01839.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	2546	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.
cd17656	A_NRPS_ProA	0.0	481	957	1	479	gramicidin S synthase 2, also known as ATP-dependent proline adenylase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. 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	2556	3036	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.
cd17655	A_NRPS_Bac	0.0	3592	4077	1	489	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.
cd19531	LCL_NRPS-like	0.0	3141	3555	1	427	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	1584	4295	1	2784
BAY90071.1	0.0	190	3125	306	3286
BAY30132.1	0.0	196	3125	313	3297
BAZ00088.1	0.0	196	3125	313	3295
BAZ75991.1	0.0	196	3125	313	3295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFY_A	0.0	467	2001	204	1722	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	467	2079	204	1799	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
2VSQ_A	2.58e-256	1	1060	1	1057	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFW_A	9.67e-214	467	1487	204	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	4.44e-213	467	1487	204	1205	Crystalstructure of a 4-domain construct of a mutant 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
P39846	0.0	9	2373	7	2384	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	6	3416	3	3410	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	5	3579	3	3585	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	5	2550	3	2554	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q70LM4	0.0	8	4235	3	4744	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001453_01839.