CAZyme Information: MGYG000000147_04413

Basic Information

• Species: Bacillus paralicheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis
• CAZyme ID: MGYG000000147_04413
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2564		289418.19	5.6498

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000147	4371304	Isolate	United Kingdom	Europe

• Gene Location: Start: 4383; End: 12077 Strand: +

Full Sequence      

MAQETEIQDIYPLSYMQEGMLFHSLLHPDSNAYIEQISFTISGDLCLDSFQKSLDLLIER
YDIFRTIYIKEVPDLDGPQQVVLSHRKVAVQTEDISALTAEQQNTLINSRKQADRLQRFD
LQKGPLMRLTLYQTGEKRHTCVWTHHHIMMDGWSLGIVLQDFFHMYYALRNSRPFRLGKP
APYSTYMTWLRGQNREKTAAFWSDYLEGYGESVSVPGSKSKTTEGGYTPRHLQYSLKPET
VEKLSDLARRLGVTLNTLFTSIWGLLLHRYNATDDAVFGAVVSGRPSAIDGIESMAGLFI
NTVPVRIRSSAGMSFSSLAKQVQKDILTCEDHGYYPLYEIQNESGLNKDLVNHILVFENY
PVQMQKEVNGWEESEENALHLDHFSTSEETNYDLNIVIVPGETFYIKFSYNAEVYDQTDI
LRLQGHVKEVIDCILSDPDQLITSIDPVPLAEKKLIHSFHGKQRTYPDQTVYELFEEQAA
KTPKQEALRFNETSWSYRELDERANQIARALRKEGAGPNQVAAVMLRRSKETVAALLGIW
KSGSAYMPLDPDHPPERLSFLLRDSQAKWLVTQQELLPFIPADYKGKIVTIEETDAEPKA
ALSAQSDSENWAYIIYTSGTTGQPKGVLVSHRSISNTLQWRREEYSMTDRDIALHLFSYV
FDGSITGLFTPLLSGSCVLLTDEDDAKDVVAMKQLIAQHGVSHLLFVPSLYRVLLETLTK
TDAETLRAVTFAGEAVTPDLITVSREICSNAELINEYGPTENSVSTTVLRNLQKSERLTI
GRPVDNTSVYIMHGNLLQPIGAVGELCISGKGLAEGYFQQKELTDQAFTAHPFHEGERLY
RTGDKARFLPDGTIEYLGRLDHQVKVRGFRIELGEIESALRGISGVKDAAALVRTTADGE
QELAAYVVLQKETERLDLHRALAGKLPAYMMPDSFTILPKMPLTTSGKLDRSGLPEPAHS
GGTDVMPKAPRTLLETELMSIWQDVLKRERISIHDDFFQLGGQSLKAAALVSKIYQRLNV
QLPIREVFSYPTIASMASAIDRVKSETRPEIKPAPEKNLYPLSFAQKRLYALHQLAKDST
SYNMPACLELCGTLNRKRLKETFATLIDRHEALRTSFVLQDGEPMQKVVSSAEVKWTELH
IQSEKSLNEVLESFVQPFDLERAPLIRVCLAALNKDRHFFLLDMHHLIADGMSMSTFIRE
FSAIYSGKELPPLTLQYKDFAVWQNEQFSAGAFGSQKQYWLEVLKGTLPVLDLPLDQKRP
LLPDFSGDTLTTHIDRETGAKLRQLMDETGSTLYMVLLAGFSVFLSKLSGQEDIVIGSPA
HGRERAELDGVIGMFVNTMAMRSKPEGNKTVRTYLKEIKTLTLEAVDNQYYPFEELVQHL
DAPREVNRNPLFDAMLVLENSDDFKVELPELTLLSHKLPHHSSKFDLTLHAEEQDDGTIS
CHFEYSTALFEKATVARWSDHFKALIGSMSANHDMKLSDMQMLTPKEQNMLINAAGETAE
YPRQENIASLFEKQAMAAPDQIAAVIDDRQLSYRELDEKAERTAAVLNEHGVGSGQVVGL
MTDRSLDMLVGILGILKAGGAYLPIDPDYPAERIRFMLSDSGAKLLLTQSGQQWEEPIDI
PVLYIDEAEKAAAKKRRQPISAEQPAYVIYTSGTTGKPKGVVIEHRNVVSLIKHDELPFS
FGSRDVWTLFHSYCFDFSVWEIFGALLHGGKIVIVPKETARDPHVYRRLLQKEGVTVLNQ
TPTAFHGLIDEELRHSDRLQLRYVIFGGEALQPGMLMNWIEKYPETDLINMYGITEITVH
ATYKKLTRTDMKHNKSNIGKPLATLQAYVADAYMNLQPVGVPGELYIAGAGVARGYINRE
ELTASRFITNPYVGGQRLYRTGDIVKRMPNGELEYVGRKDAQVKIRGYRIELGEIRSALQ
ELPPIKEAAVITRNDKDGQQSIYGYAVTAQSLNEAEIRTSLRTLLPEYMIPARIIQVDEL
PLTANGKLDENALPEPAANQGAGEDISPRNDIEQMMAEIWEELLGMEGLGVNAHFFHLGG
DSIKALQVCARLKQRGYETTVRELFKHQTLGELSKRVTKVRREIDQAPVNGEVPLTPVQH
WFFSQSLSHDHFHQSVMLHSSARFDETALQKTLAHIVVHHDALRMVCGYQDGVLTQYNRA
EELAKEELFSFELLDVREAGSLAQEHVMIERAAEHIQKSIQLQTGPLVAAGVFRGSDGDH
LLLVIHHLVIDGVSWRILFEDLTAGYKQALAGKEIVLPEKTDSYQTYAKRLTDYATSRQL
LREIDYWTEREKTRVEPLPKDAETITNLLQDTDTIDIRLTKQETERLLTAVNKPYTTDTN
DILLAALGLALHKWTGNDRFKISLEGHGREAHLEDIDISRTVGWFTSIYPVLLDASLPES
ADDHERFGYHIKRTKDMLRRIPYKGVGYGVLKYIGGMWEPEDFQRPDISFNYLGQFDEDI
KSSGFRVSPVKAGHEISPDWERPHLLDISGAISSECLVMHFVYNRLQYEKGTVQALADHV
QFFLKTIIKHCTEKENHEKSATDFTDEDLTLEELSDIMGAVNKL

Enzyme Prediction     

No EC number prediction in MGYG000000147_04413.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19543	DCL_NRPS	0.0	10	438	1	423	DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (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). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as 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. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
PRK12316	PRK12316	0.0	6	2554	1552	4089	peptide synthase; Provisional
PRK12316	PRK12316	0.0	6	1045	4098	5144	peptide synthase; Provisional
PRK12467	PRK12467	0.0	6	1234	2642	3763	peptide synthase; Provisional
cd17643	A_NRPS_Cytc1-like	0.0	1519	1993	1	450	similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	5	2096	555	2679
ACX49739.1	2.12e-203	12	1753	11	1826
BAY90071.1	9.24e-176	1235	2075	313	1175
BAY30132.1	2.89e-175	1235	2075	314	1178
BAZ00088.1	5.09e-175	1235	2075	314	1176

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	468	2090	204	1810	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	2.23e-301	468	2006	204	1725	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	5.76e-233	4	1038	6	1037	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.31e-193	1060	1993	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]
5U89_A	1.60e-185	454	1495	9	1074	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39847	0.0	1	2564	1	2555	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P94459	0.0	3	2558	1049	3600	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	11	2077	9	2107	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q04747	0.0	3	2557	1050	3574	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P39846	0.0	1	2564	1	2560	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB 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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000147_04413.