CAZyme Information: MGYG000000227_04862

Basic Information

• Species: Bacillus sonorensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus sonorensis
• CAZyme ID: MGYG000000227_04862
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2566		289695.58	5.1671

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000227	4782975	Isolate	China	Asia

• Gene Location: Start: 4985; End: 12685 Strand: +

Full Sequence      

MTQATQIQDIYPLSYMQEGMLFHSLLDFSSKAYVEQTSFTITGNLCIDSFQQSLHLLVSR
YDIFRTIFIKEVPDLTGPQQVVLSKRELTVHREDLSHLSHHEQLALIDEFMKKDREKGFD
LQKDPLMRLALFERGNSHYTCVWTHHHIIMDGWCLGIILKEFFGMYESLKKGKPVQLGST
VPYSRYIEWLGEQNKEETAAYWSDYLREYGNTASIPGIKSSSADGHYEAAHIRFALEPEI
VEKLTAVAKKCGVTLNTLFMTIWGILLHRYNAADDAVFGSVISGRPSEIDGIESMVGLFI
NTVPVRIRSHEGMSFSSLVKAVQEDILASEQHGYYPLYDIQNHSPLKQGLIDHILVFENY
PVQLQQALNIGSENEENALKLDDISMSEQTNYDFNIVIVPGKPFYIKFSYNAAVYQQEEI
RRIQGHFKQALHCILADPEIAVSDINIVPPEERKVIQSFNATDRPYINKTVFQMFEEQAY
KTPEAAALRMGDECWTYRQLNERANQIAHTLLDKGAGAGAIVAVMMRRSLEMAAALLGVW
KAGCAYMPLDPNYPIERLSFLLQDSQASLLLTEQELISFLPLDYKGSIVTAEHTTSRKTV
SPDASFGELAYLIYTSGTTGRPKGVLINHQGIANTLQWRRKEYSMTERDIALHLFSYVFD
GCVTSLFTPLISGACVLLTTEDEAKDVFALKRKIAEHKVSHMIIVPSLYRVLLEVLTDED
AKSLRIVTFAGEPVTSDLLETSRKICPSAELANEYGPTENSVATTVLRHLNEKERITIGR
PIANTKVFVLHGNQLQPIGAAGELCISGAGLACGYYKRAELTEKAFTDHPFLNGERIYRT
GDAGRFLPDGTIEYMGRFDDQVKIRGYRIELSEIEAVLRKAPGVKEAAVIAHDVSAGEKE
LAAYIVPKMGDGLPDLHQRLAGTLPSYMIPANIIKISRMPLTSSGKLDRSALPAPADTTS
QTYIAPRTIAEADLARIWEEVLHKPKIGIRDDFFQLGGQSLKAATLASRIHKTLNIELPL
SDVFSYPTVESMAAKLMGLKEQAFTQIEPADARDFYPLSFSQKRLYALHQLAADSTGYNM
PAVLKLSGNVDLPRLRKALTELVNRHESLRTVFVADNGEPMQIIHPEMTFELQELENESD
HLLQSAIASFIKPFNLSAGPLFRASFISMGNENAFLLLDMHHIIADGVSMGTLVQEFTDL
YCGKELPALNLQYKDFAVWQLERFSGELYSKQEAYWLNQLGGSLPVLDLPLDKTRPRLPD
FSGGTFEVNIDKRTADELQRIMFETGTTMYMILLAVYSILLSKLSGQEDIIVGSPVAGRP
HADLERVIGMFVNTLAMRSQPEGDKTFRSYLQEIRELALTAFENQDYPFEQLVNQLDIHR
EVNRNPLFDAMLVLQNSEDFQFDVPGLSISSVTPAHEVSKFDLTLHAETHSDGIRCRFEY
STALFEEETIARWASYFIGLVREITADIHMKLSEMQLLPASERNLLIEKMGQYACYPKDE
SIVSVFEQQAAEHSEHIAVVYGQTRLTYQELNERAERTAAMLIKQGVRTGDIVGVMLDRS
PDMVIGILSILKAGGAYLPIDPEYPQERISFMLNDSGAKILLTDYGQNKPAGYQGQMLYI
NESENEPIPGDFRVRETAADQPAYVIYTSGTTGQPKGVIVGHRNVISLLKHQDMPFDFGS
QDVWTLFHSYCFDFSVWEMFGALLNGSTLVVVSKETARAPNAFRLLLKKEGVTVLNQTPT
AFYGLMHEEQNHTDRLNIRYVIFGGEALQPGMLQSWNQKYPDTDLINMYGITETTVHVTY
KKLSAADIAKNRSNIGKPLATLQAYVMDAYMNLQPTGVPGELYIGGEGVARGYLNRDELT
SARFVPNPYLPGNRLYRTGDLAKRLANGELEYMGRIDDQVKVRGHRIELGEIQAALLQLP
MINEAAVITRTDQQGQTAVYAYMVTDDRQVANVSDIRASLRAVLPDFMIPARFIQIGSIP
LTVNGKLDQKALPEPDKLTQADDDISPRNEIEKAMAEIWEELLEAEELGVSANFFELGGD
SIKALQVCARLKQRGFETTVREMFEHQTLGELSARVRKVLRVIDQSPVEGEMPWTPIQRW
FFSQSLEAHHFNQSVMLYRAERFDDVALREVLKSIVKHHDALRIVCRYEDGRPVQVNRGT
DIPDDELYALELFDLRDSTAQARREIEDAADRMQQQIRLETGPMLHAGLFRAQDGDHLFL
TIHHLVIDAVSWRILFEDFSIAYEQAVSGEPIVLPQKTDSYLTYSRKVADYSGSRRLHRE
IAYWNERENRHIKPIPKDHDVASNTFKDTQVIDVELSRQDTELLLTAVNKAYSTETNDIL
LSALGLALQKWTGNDEFKISMEGHGREAYLDDIDISRTVGWFTSIYPVWLDISEFDQTDK
DEWLGRHIKQTKDMLHRIPHKGTGYGVLKYMNNLWGSEQSNPEISFNYLGQFDQDIQSKA
FEVSDIKTGNEISPDWERPYVLDISGAVSSGCLNMHIIYNRFQFNEKTIRAFASHFKHAL
ENIIQHCAGKEKREWSAADFTDEDLTLDELSEIMGAVNKLQGEEIR

Enzyme Prediction     

No EC number prediction in MGYG000000227_04862.

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	4	2560	1550	4102	peptide synthase; Provisional
cd17643	A_NRPS_Cytc1-like	0.0	1515	1992	2	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.
COG1020	EntF	0.0	1270	1920	1	642	Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].
PRK12467	PRK12467	0.0	4	1247	2640	3773	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	7	2090	557	2674
ACX49739.1	1.87e-209	12	1740	11	1816
BAY90071.1	1.78e-196	959	2078	2124	3285
BAZ00088.1	2.43e-195	966	2078	2142	3294
BAZ75991.1	2.43e-195	966	2078	2142	3294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	2.65e-318	467	2084	203	1805	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	6.67e-299	467	1996	203	1716	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	6.76e-243	6	1036	8	1039	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	2.70e-194	1054	1992	4	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	1.91e-191	451	1487	6	1071	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
P39846	0.0	1	2560	1	2560	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P94459	0.0	8	2553	1054	3596	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	11	2076	9	2107	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P39847	0.0	1	2560	1	2555	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	8	2553	1055	3574	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
1.000027	0.000011	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000227_04862.