CAZyme Information: MGYG000002490_03608

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_03608
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4387		491515.31	4.5249

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002490	6537383	Isolate	Japan	Asia

• Gene Location: Start: 92; End: 13255 Strand: +

Full Sequence      

MAAWLPDGNIEYLGRIDHQVKIRGYRIELDEIETQLLNVEGVEEAVVLACQDGGGEKALV
AYFVADRTLTVSEMRTSLAQGMPGYMIPSYFVQLERMPLTSNGKVDRKALPEPQGGLQTG
VEYVAPRNRTESQLVKIWEEVLGYSGIGVLDNFFELGGHSLRATNLVSKIRKEMNVELPL
RDVFRYMTVESMAGAIASLEETQHSLIPKAEEKAYYPVSSAQKRLYVLHQLDDSELNYNL
PSALQLEGALNEGKVEKALTTLVARHDMLRTGFEIVNGEPVQRIHPLVAFKVEKLQASED
QVAAILEGFIQPFDLTQPPLLRALLIELEKEKFLLALDIHHIGSDGLSMDVLLREFVRLY
NGEELPELRIQYKDYAVWQQSEEQRQRIKRQEEYWRGVFSSELPVLELPLDFSRPAVQQF
DGQTLMFTLDAEKSEALKRLAGDSGATLYMLLLAAYSVLLHKYAGQEDIVVGTPIAARSH
ADLQPIIGMFVNTLALRLGPAAERTFLDYLQEVKETTLGAYEHQDYPFEELVEALQVSRD
LSRNPLFDTMFSLQKHESLDLTLEGLQWSLFDIEEKTAKFDLSLDIVEFDNELVCKIEYA
TSLFRQETMVRLAGHYEQLLASILAQPGARISDLDFLTDSEKHDLLVGFDVSSSALAKQP
AAEGTGLEADESWRERTFHELFEEQAERTPGALAVVYEDSKLTYAELNAKANRLAYALRA
RGVKPEQVVGILAGRSAELLIGVLGVWKAGGAYVPLDPDYPAERIEYMLADSGASVLLTQ
TRLLEQVEAWRSDGALVLQTVLALDDAATYSLGAAGEAAAETSATAEAEKNVQAADLASN
PTNVNKPGDLAYVIYTSGTTGRPKGVAVEHRSLVNTAAGYRRDYRLDQFPIRLLQLASFS
FDVFVGDIARTLYNGGTMIIVPKDDRIDPTRLYGWIRDYAVTVFESTPALIMPFMEHVHA
EGLDLSSMQLLITSSDACSVADYRTLQERFGSQFRIINSYGVTEAAIDSSFYDEPLEKLP
KTGSVPIGKAWLNAKFYIVDANLKPVPVGVLGELIIGGAGVARGYLNRPDLTAEKFVDSP
FVAGERLYRTGDLARWMPDGNVDFIGRIDNQVKIHGYRIELGEIEAAMQNFAGVRQALVI
DQTDERGQKYLCGYVVADSSFGLEGLVAHLDAALPSHMVPSRIMRLGQMPLTPNGKIDRK
ALPVPEGSIRAEAAYTAPRTPAEQALASVWQSVLGVDQVGTMDNFFALGGDSIKALQVSS
RLLQTGYKLVMKDLFHYPTISTLSLQLQTAERTASQAEVTGEVILTPIQRWFFEQNPADV
HHSNQAFMQFSKQGFDEEALRQAVRQLVVHHDALRTVYRETENGYTVWNRGAGENEALFD
LEVVDFKGVGDVKEAVEAKANDIQASIDLENGPLVKLGLFRCDDGDHLLIAIHHLVVDGV
SWRILLEDFAAGYEQALQGQPIRLPLKTDSFQTWAKQLADYANGPAMESEREYWQHIEQL
TYEPLPKDFEQGRSKLKDSGLVTVRWTAEETEQLLKQAHRAYHTEMNDLLLAALGLAVQA
WSGRERVLVNLEGHGREDVLPDVDITRTVGWFTSQFPIVLEPGHAQALGHQMKQVKESLR
RIPNKGIGYGILRYLSVPRDGERFALEPEISFNYLGQFDQDYESSGSQPSPFSPGSDSSP
NAVMDYVLDINGMVSEGVLELTIRYGETQYKRETVERLSTLLQSSLREVISHCVSKERPE
LTPSDVLLQDVTVEELERLAEHTAALGELENVYTLTPLQKGMLFHSLLDADSEAYFEQVT
FDLYGSLNVEAFTQGLDTLVQRNEALRTNFITGWRDEPIQVVFRERKCEVYFEDIRSVSD
EDPEKTIADFVSADKANKFDLARGSLMRVTVLRTGYESYHVIWSHHHILMDGWCMSFMIK
EVFDTYFAFQEKRTLELPPVTSYSRYIEWLEAQDAAKASRYWSEYLAGYDQQTKLPQEKT
QLKQGAFEAAEIDVELSKELTGQIERVARQQQVTLNTFIQTVWGLVLQVYNNSEDVVFGS
VVSGRPAEIPGIESMIGLFINTIPVRIQGKAEETVADILRKTQDQALASGAYETFPLFEI
QSLSEQKRDLINHIMVFENYPMEEQIEQVVGGDKEALKIANIQSPEQTNYDLDITVIPEE
HIMLRFTYNALTFREEDIRLIHGHFARALEKVAANPNIRVNQLEFLTAAEKEQILGAFNP
AQPEAAPAAAFHRLFEEQAERTPEAEAVVYENDRLTYAELNERANRLAATLRASGIGRES
IVGILAERSVDLLVAVLAVWKAGGAYVPLDPDYPADRVRFMLEDSGAKVLLTQMPLRERA
EAWLGEEELALAAVLYLDDETSYSEERTNAPIGSGMVSGKLTAAVDDGDESHQNVGMGSF
HEARPEDLAYVIYTSGTTGKPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFD
VFVGDIARTLYNGGTMVIVPKDDRIDPSRLHHWMEREQVTIFESTPALIVPFLEYVHEQG
LDMSWMELLITSSDSCSVADYRTLQERFGSLFWIINAYGVTEAAIDSSFYDEELAKLPQT
GHVPIGKAWLNAKFYIVDAHLNPVPVGVLGELVIGGVGVARGYLNRPELTEEKFVDSPFA
AGERLYRTGDLARWMEDGNVDFIGRIDNQAKIRGYRIETGEVEAKLLSAGGVKEAVVVVR
EDQEGQKALCAYYTAEEGLTAADLKRAMASGLPGYMIPSYFVELERLPLTPNGKIDRKAL
PAPEGGAGGGREYVAPRTELEAKLAAIWQEVLVREKAVGVTDNFFDLGGHSLRATTLVSK
MHKELGIEFPLRDVFRYSTVEEMAAAMEWLEIGSFTAIPAAEPSEYYPLSSAQKRLYILN
QLEGGELSYNIPGAMLLEGELDRQRFEEAFRGLVARHETLRTGFEMVKGEAVQRIYEEAA
FQVEYVQISGEQAEETVRQFVRPFDLAKPPLLRVGLAEMAPDRHILMFDTHHIVSDGVSM
DVLIDEFVRLYSGEPLEPLRIQYKDYAVWQQSDEQKAQLVKQEAYWLDMFCGDLPILELP
TDYPRPAMQSYEGRTLQLFMNSEKSEGLKRLAAENGATLYMVLLAGYTILLHKYTSQEDV
VVGTPIAGRNHSDIQPLIGMFVNTLAIRSYPTAGKTFLDYLKEIKETTLGAFEHQNYPFE
ELVDKVNVARDLSRNPLFDTMFALQNTENLEIQLPGLHLSTYASEEIVSKFDLSLDVTEI
EEGLEYLFEYATALYKTETVEKLAAHYLQLLESILRNPSATIAELGILTPAEKEQIIGAF
NPAQPEAAPAAAFHRLFEEQAELTPEAEAIVYENNRLTYAELNERANRLAATLRASGIGR
ETIVGILAERSVDLLVAVLAVWKAGGAYVPLDPDYPADRVRFMLEDSGAKVLLTQTALRE
RAEAWLGEEELALAAVLYLDDEASYSEERENAPIGSGMVSGKLTDAVNDGDGTHQNVDTY
SFHEALPEDLAYVIYTSGTTGKPKGVMIEHCSLVNTAAGYRREYRLDQFPVRLLQLASFS
FDVFVGDIARTLYNGGTMVIVPKDDRIDPSRLYHWMERERVTIFESTPALIVPFLEYVHE
KGLDMSWMELLITSSDSCSVADYRTLQERFGSLFRIINAYGVTEAAIDSSFYDEELTKLP
QTGHVPIGKAWLNAKFYIVDAHLNPVPVGVLGELVIGGVGVARGYLNRPELTEEKFVDSP
FAAGERLYRTGDLARWMEDGNVDFIGRIDNQAKIRGYRIEMGEIESQLLRVAGVREAVVL
VRSDANGQKALCAYYTTDGELTAADLKRAIASELPGYMIPSYFVELERLPLTPNGKIDRK
ALPAPEGEAGSGTEYVAPRNELETKLVGIWQEVLGLTKEIGVHDNFFDLGGHSLRATTLV
SKVHKELSVDLPLRDVFRHSTIEAMAEAISQLERQEHLSIPVLDKRDYYPLSSVQKRLYI
QQQMEGAELSYNMSGMTVLVGRLERNQFEAALKGLIARHEILRTGFEMVHGEPVQRIYPD
LKFAVEYTKATESETKSIVDGFVRVFDLERPPLLRVGLVEWEAERHLLMLDIHHIVTDGM
SMGIFVAELLRLYNGETLEPLRIQYKEFAAWQQSEPVKERLKRQEAYWLDVLEGELPTLE
LPTDFVRPAARSFEGDVLPFSIDKQMTDSLQRIADENGATLYMVLFAAYSILLSKYSGQE
DFIVGTPVSGRTHADLEPLIGMFVNTLAIRHNPSGEKTFLAYLNEVKETMLGAYDHQDYP
FEELVKKLQVPRDQSRNPIFDVMFALETKEDNVQSFGDIQIESYPETHTVSQFDLTLVIS
LLDEGMNGQFEYATKLFTRNLIDNFAQDLLVIITQICEQPSVLLKDISLNGQSEQEQDVL
EVIDIIF

Enzyme Prediction     

No EC number prediction in MGYG000002490_03608.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	2233	2764	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	2243	2760	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.
cd17650	A_NRPS_PpsD_like	0.0	690	1202	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.
cd17650	A_NRPS_PpsD_like	0.0	3325	3842	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.
cd19531	LCL_NRPS-like	0.0	215	627	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	754	3943	1	2673
BAY90071.1	1.34e-310	394	3931	317	3285
BAZ00088.1	3.05e-304	394	3931	318	3294
BAZ75991.1	3.05e-304	394	3931	318	3294
BAY30132.1	5.02e-299	394	3931	318	3296

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	2231	3930	207	1798	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	3.67e-317	2231	3851	207	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]
2VSQ_A	6.43e-209	1768	2848	8	1040	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
5U89_A	5.14e-198	2210	3299	6	1073	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6P1J_A	1.17e-195	2864	3842	3	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94459	0.0	1767	4377	5	2517	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	1	3983	835	4727	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
Q0VZ70	0.0	217	2848	24	3061	Chondramide synthase cmdD OS=Chondromyces crocatus OX=52 GN=cmdD PE=1 SV=1
Q04747	0.0	1769	4376	6	2524	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
Q70LM5	0.0	1	4250	3435	7603	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC 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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002490_03608.